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Post Workout Nutrition - What You Need To DoOptimal post-exercise nutrition -
Running on empty may help burn fat faster, but it won't leave enough energy for more rigorous training. It also can increase the risk of strains, sprains, stress fractures and other injuries from exercise-related fatigue. Furthermore, letting the body get too depleted may cause people to overeat afterward, undoing the benefits of exercising in the first place.
This keeps the body fueled, providing steady energy and a satisfied stomach. Knowing the why, what and when to eat beforehand can make a significant difference in your training.
As Jackie Kaminsky notes in her blog 10 Nutrition Myths , nutrient timing can be effective overall, but it's not for everyone. A diet plan is crucial for maximizing daily workouts and recovery, especially in the lead-up to the big day.
And no meal is more important than the one just before a race, big game or other athletic event. Choosing the wrong foods-eating or drinking too much, consuming too little or not timing a meal efficiently-can dramatically affect outcomes.
Similarly, maintaining an appropriate daily sports-nutrition plan creates the perfect opportunity for better results. This supplies immediate energy needs and is crucial for morning workouts, as the liver is glycogen depleted from fueling the nervous system during sleep.
The muscles, on the other hand, should be glycogen-loaded from proper recovery nutrition the previous day. The body does not need a lot, but it needs something to prime the metabolism, provide a direct energy source, and allow for the planned intensity and duration of the given workout.
But what is that something? That choice can make or break a workout. The majority of nutrients in a pre workout meal should come from carbohydrates, as these macronutrients immediately fuel the body. Some protein should be consumed as well, but not a significant amount, as protein takes longer to digest and does not serve an immediate need for the beginning of an activity.
Research has demonstrated that the type of carbohydrate consumed does not directly affect performance across the board Campbell et al.
Regular foods are ideal e. Exercisers might also supplement with a piece of fruit, glass of low-fat chocolate milk or another preferred carbohydrate, depending on needs.
Pre-exercise fluids are critical to prevent dehydration. Before that, the athlete should drink enough water and fluids so that urine color is pale yellow and dilute-indicators of adequate hydration.
Read more: What to Eat Before a Workout. Timing is a huge consideration for preworkout nutrition. Too early and the meal is gone by the time the exercise begins; too late and the stomach is uncomfortably sloshing food around during the activity.
Although body size, age, gender, metabolic rate, gastric motility and type of training are all meal-timing factors to consider, the ideal time for most people to eat is about hours before activity. If lead times are much shorter a pre-7 a.
workout, for example , eating a smaller meal of less than calories about an hour before the workout can suffice. For a pound athlete, that would equate to about 68 g or servings of carbohydrate, 1 hour before exercise. For reference, 1 serving of a carbohydrate food contains about 15 g of carbohydrate.
There are about 15 g of carbohydrate in each of the following: 1 slice of whole-grain bread, 1 orange, ½ cup cooked oatmeal, 1 small sweet potato or 1 cup low-fat milk.
It is generally best that anything consumed less than 1 hour before an event or workout be blended or liquid-such as a sports drink or smoothie-to promote rapid stomach emptying. Bear in mind that we are all individuals and our bodies will perform differently.
It may take some study to understand what works best for you. Preworkout foods should not only be easily digestible, but also easily and conveniently consumed.
A comprehensive preworkout nutrition plan should be evaluated based on the duration and intensity of exertion, the ability to supplement during the activity, personal energy needs, environmental conditions and the start time.
For instance, a person who has a higher weight and is running in a longer-distance race likely needs a larger meal and supplemental nutrition during the event to maintain desired intensity. Determining how much is too much or too little can be frustrating, but self-experimentation is crucial for success.
The athlete ought to sample different prework-out meals during various training intensities as trials for what works. Those training for a specific event should simulate race day as closely as possible time of day, conditions, etc.
when experimenting with several nutrition protocols to ensure optimal results. See how to count macros to keep your nutrient timing as effective as possible.
Supplemental nutrition may not be necessary during shorter or less-intense activity bouts. If so, carbohydrate consumption should begin shortly after the start of exercise. One popular sports-nutrition trend is to use multiple carb sources with different routes and rates of absorption to maximize the supply of energy to cells and lessen the risk of GI distress Burd et al.
Consuming ounces of such drinks every minutes during exercise has been shown to extend the exercise capacity of some athletes ACSM However, athletes should refine these approaches according to their individual sweat rates, tolerances and exertion levels.
Some athletes prefer gels or chews to replace carbohydrates during extended activities. These sports supplements are formulated with a specific composition of nutrients to rapidly supply carbohydrates and electrolytes.
Most provide about 25 g of carbohydrate per serving and should be consumed with water to speed digestion and prevent cramping.
To improve fitness and endurance, we must anticipate the next episode of activity as soon as one exercise session ends. That means focusing on recovery, one of the most important-and often overlooked-aspects of proper sports nutrition.
An effective nutrition recovery plan supplies the right nutrients at the right time. Recovery is the body's process of adapting to the previous workload and strengthening itself for the next physical challenge. And the carbohydrates may allow you to work out for a longer time or at a higher intensity.
If you don't eat, you might feel slow-moving or lightheaded when you exercise. If you plan to exercise within an hour after breakfast, eat a light meal. Or have a sports drink.
Focus on carbohydrates for the most energy. And remember, if you usually have coffee in the morning, it's probably OK to have a cup before your workout. Also know that anytime you try a food or drink for the first time before a workout, you risk an upset stomach.
Be careful not to overdo it when it comes to how much you eat before exercise. General guidelines suggest:. Eating too much before you exercise can leave you feeling slow-moving. Eating too little might not give you the energy you need to keep feeling strong during your workout.
Most people can eat small snacks right before and during exercise. The key is how you feel. Do what works best for you.
Snacks eaten soon before exercise probably won't give you added energy if your workout lasts less than 60 minutes. But they may keep you from feeling hungry. If your workout is longer than 60 minutes, it may help to have a carbohydrate-rich food or drink during the workout.
Good snack choices include:. Eat a meal that has both carbohydrates and protein in it within two hours of your workout if possible.
Eating after you work out can help muscles recover and replace their glycogen stores. Think about having a snack if your meal is more than two hours away. Good post-workout food choices include:. Drinking fluids such as water before, during and after your workout can help prevent dehydration.
Don't forget to drink fluids. You need to have enough fluids before, during and after exercise to help prevent dehydration. Water is generally the best way to replace lost fluids. But if you're exercising for more than 60 minutes, try a sports drink.
Sports drinks can help keep your body's electrolyte balance. And they can give you a bit more energy because they have carbohydrates in them. Remember that the length and intensity of your activity can help you decide how often and what you should eat and drink.
For example, you'll need more energy from food to run a marathon than to run or walk a few miles. And try not to add any new products in your diet before a sports event that lasts a long time.
It's best to have tried the products before the event to see how your system handles the food. When it comes to eating and exercise, everyone is different. So notice how you feel during your workout and how your overall performance is affected by what you eat.
Let your experience guide you on which pre- and post-exercise eating habits work best for you. Think about keeping a journal to see how your body reacts to meals and snacks so that you can change your diet for your best performance. There is a problem with information submitted for this request.
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Error Email field is required. Error Include a valid email address. Several methods exist to determine protein quality such as Chemical Score, Protein Efficiency Ratio, Biological Value, Protein Digestibility-Corrected Amino Acid Score PDCAAS and most recently, the Indicator Amino Acid Oxidation IAAO technique.
Ultimately, in vivo protein quality is typically defined as how effective a protein is at stimulating MPS and promoting muscle hypertrophy [ ]. Overall, research has shown that products containing animal and dairy-based proteins contain the highest percentage of EAAs and result in greater hypertrophy and protein synthesis following resistance training when compared to a vegetarian protein-matched control, which typically lacks one or more EAAs [ 86 , 93 , ].
Several studies, but not all, [ ] have indicated that EAAs alone stimulate protein synthesis in the same magnitude as a whole protein with the same EAA content [ 98 ]. For example, Borsheim et al. Moreover, Paddon-Jones and colleagues [ 96 ] found that a cal supplement containing 15 g of EAAs stimulated greater rates of protein synthesis than an cal meal with the same EAA content from a whole protein source.
While important, the impact of a larger meal on changes in circulation and the subsequent delivery of the relevant amino acids to the muscle might operate as important considerations when interpreting this data.
In contrast, Katsanos and colleagues [ ] had 15 elderly subjects consume either 15 g of whey protein or individual doses of the essential and nonessential amino acids that were identical to what is found in a g whey protein dose on separate occasions.
Whey protein ingestion significantly increased leg phenylalanine balance, an index of muscle protein accrual, while EAA and NEAA ingestion exerted no significant impact on leg phenylalanine balance.
This study, and the results reported by others [ ] have led to the suggestion that an approximate 10 g dose of EAAs might serve as an optimal dose to maximally stimulate MPS and that intact protein feedings of appropriate amounts as opposed to free amino acids to elderly individuals may stimulate greater improvements in leg muscle protein accrual.
Based on this research, scientists have also attempted to determine which of the EAAs are primarily responsible for modulating protein balance. The three branched-chain amino acids BCAAs , leucine, isoleucine, and valine are unique among the EAAs for their roles in protein metabolism [ ], neural function [ , , ], and blood glucose and insulin regulation [ ].
Additionally, enzymes responsible for the degradation of BCAAs operate in a rate-limiting fashion and are found in low levels in splanchnic tissues [ ]. Thus, orally ingested BCAAs appear rapidly in the bloodstream and expose muscle to high concentrations ultimately making them key components of skeletal MPS [ ].
Furthermore, Wilson and colleagues [ ] have recently demonstrated, in an animal model, that leucine ingestion alone and with carbohydrate consumed between meals min post-consumption extends protein synthesis by increasing the energy status of the muscle fiber.
Multiple human studies have supported the contention that leucine drives protein synthesis [ , ]. Moreover, this response may occur in a dose-dependent fashion, plateauing at approximately two g at rest [ 31 , ], and increasing up to 3.
However, it is important to realize that the duration of protein synthesis after resistance exercise appears to be limited by both the signal leucine concentrations , ATP status, as well as the availability of substrate i.
As such, increasing leucine concentration may stimulate increases in muscle protein, but a higher total dose of all EAAs as free form amino acids or intact protein sources seems to be most suited for sustaining the increased rates of MPS [ ].
It is well known that exercise improves net muscle protein balance and in the absence of protein feeding, this balance becomes more negative.
When combined with protein feeding, net muscle protein balance after exercise becomes positive [ ]. Norton and Layman [ ] proposed that consumption of leucine, could turn a negative protein balance to a positive balance following an intense exercise bout by prolonging the MPS response to feeding.
In support, the ingestion of a protein or essential amino acid complex that contains sufficient amounts of leucine has been shown to shift protein balance to a net positive state after intense exercise training [ 46 , ].
Even though leucine has been demonstrated to independently stimulate protein synthesis, it is important to recognize that supplementation should not be with just leucine alone. For instance, Wilson et al.
In summary, athletes should focus on consuming adequate leucine content in each of their meals through selection of high-quality protein sources [ ].
Protein sources containing higher levels of the EAAs are considered to be higher quality sources of protein. The body uses 20 amino acids to make proteins, seven of which are essential nine conditionally , requiring their ingestion to meet daily needs.
EAAs appear to be uniquely responsible for increasing MPS with doses ranging from 6 to 15 g all exerting stimulatory effects. In addition, doses of approximately one to three g of leucine per meal appear to be needed to stimulate protein translation machinery.
The BCAAs i. However, the extent to which these changes are aligned with changes in MPS remains to be fully explored. While greater doses of leucine have been shown to independently stimulate increases in protein synthesis, a balanced consumption of the EAAs promotes the greatest increases.
Milk proteins have undergone extensive research related to their potential roles in augmenting adaptations from exercise training [ 86 , 93 ].
For example, consuming milk following exercise has been demonstrated to accelerate recovery from muscle damaging exercise [ ], increase glycogen replenishment [ ], improve hydration status [ , ], and improve protein balance to favor synthesis [ 86 , 93 ], ultimately resulting in increased gains in both neuromuscular strength and skeletal muscle hypertrophy [ 93 ].
Moreover, milk protein contains the highest score on the PDCAAS rating system, and in general contains the greatest density of leucine [ ].
Milk can be fractionated into two protein classes, casein and whey. While both are high in quality, the two differ in the rate at which they digest as well as the impact they have on protein metabolism [ , , ].
Whey protein is water soluble, mixes easily, and is rapidly digested [ ]. In contrast, casein is water insoluble, coagulates in the gut and is digested more slowly than whey protein [ ]. Casein also has intrinsic properties such as opioid peptides, which effectively slow gastric motility [ ].
Original research investigating the effects of digestion rate was conducted by Boirie, Dangin and colleagues [ , , ]. These researchers gave a 30 g bolus of whey protein and a 43 g bolus of casein protein to subjects on separate occasions and measured amino acid levels for several hours after ingestion.
They reported that the whey protein condition displayed robust hyperaminoacidemia min after administration. However, by min, amino acid concentrations had returned to baseline. In contrast, the casein condition resulted in a slow increase in amino acid concentrations, which remained elevated above baseline after min.
Over the study duration, casein produced a greater whole body leucine balance than the whey protein condition, leading the researcher to suggest that prolonged, moderate hyperaminoacidemia is more effective at stimulating increases in whole body protein anabolism than a robust, short lasting hyperaminoacidemia.
While this research appears to support the efficacy of slower digesting proteins, subsequent work has questioned its validity in athletes. The first major criticism is that Boire and colleagues investigated whole body non-muscle and muscle protein balance instead of skeletal myofibrillar MPS.
These findings suggest that changes in whole body protein turnover may poorly reflect the level of skeletal muscle protein metabolism that may be taking place.
Trommelen and investigators [ ] examined 24 young men ingesting 30 g of casein protein with or without completion of a single bout of resistance exercise, and concluded that rates of MPS were increased, but whole-body protein synthesis rates were not impacted.
More recently, Tang and colleagues [ 86 ] investigated the effects of administering 22 g of hydrolyzed whey isolate and micellar casein 10 g of EAAs at both rest and following a single bout of resistance training in young males.
Moreover, these researchers reported that whey protein ingestion stimulated greater MPS at both rest and following exercise when compared to casein. In comparison to the control group, both whey and casein significantly increased leucine balance, but no differences were found between the two protein sources for amino acid uptake and muscle protein balance.
Additional research has also demonstrated that 10 weeks of whey protein supplementation in trained bodybuilders resulted in greater gains in lean mass 5. These findings suggest that the faster-digesting whey proteins may be more beneficial for skeletal muscle adaptations than the slower digesting casein.
Skeletal muscle glycogen stores are a critical element to both prolonged and high-intensity exercise. In skeletal muscle, glycogen synthase activity is considered one of the key regulatory factors for glycogen synthesis.
Research has demonstrated that the addition of protein in the form of milk and whey protein isolate 0. Further, the addition of protein facilitates repair and recovery of the exercised muscle [ 12 ]. These effects are thought to be related to a greater insulin response following the exercise bout.
Intriguingly, it has also been demonstrated that whey protein enhances glycogen synthesis in the liver and skeletal muscle more than casein in an insulin-independent fashion that appears to be due to its capacity to upregulate glycogen synthase activity [ ].
Therefore, the addition of milk protein to a post-workout meal may augment recovery, improve protein balance, and speed glycogen replenishment. While athletes tend to view whey as the ideal protein for skeletal muscle repair and function it also has several health benefits.
In particular, whey protein contains an array of biologically active peptides whose amino acids sequences give them specific signaling effects when liberated in the gut. Furthermore, whey protein appears to play a role in enhancing lymphatic and immune system responses [ ].
In addition, α-lactalbumin contains an ample supply of tryptophan which increases cognitive performance under stress [ ], improves the quality of sleep [ , ], and may also speed wound healing [ ], properties which could be vital for recovery from combat and contact sporting events.
In addition, lactoferrin is also found in both milk and in whey protein, and has been demonstrated to have antibacterial, antiviral, and antioxidant properties [ ]. Moreover, there is some evidence that whey protein can bind iron and therefore increase its absorption and retention [ ].
Egg protein is often thought of as an ideal protein because its amino acid profile has been used as the standard for comparing other dietary proteins [ ]. Due to their excellent digestibility and amino acid content, eggs are an excellent source of protein for athletes.
While the consumption of eggs has been criticized due to their cholesterol content, a growing body of evidence demonstrates the lack of a relationship between egg consumption and coronary heart disease, making egg-based products more appealing [ ].
One large egg has 75 kcal and 6 g of protein, but only 1. Research using eggs as the protein source for athletic performance and body composition is lacking, perhaps due to less funding opportunities relative to funding for dairy. Egg protein may be particularly important for athletes, as this protein source has been demonstrated to significantly increase protein synthesis of both skeletal muscle and plasma proteins after resistance exercise at both 20 and 40 g doses.
Leucine oxidation rates were found to increase following the 40 g dose, suggesting that this amount exceeds an optimal dose [ 31 ].
In addition to providing a cost effective, high-quality source of protein rich in leucine 0. Functional foods are defined as foods that, by the presence of physiologically active components, provide a health benefit beyond basic nutrition [ ]. According to the Academy of Nutrition and Dietetics, functional foods should be consumed as part of a varied diet on a regular basis, at effective levels [ ].
Thus, it is essential that athletes select foods that meet protein requirements and also optimize health and prevent decrements in immune function following intense training. Eggs are also rich in choline, a nutrient which may have positive effects on cognitive function [ ]. Moreover, eggs provide an excellent source of the carotenoid-based antioxidants lutein and zeaxanthin [ ].
Also, eggs can be prepared with most meal choices, whether at breakfast, lunch, or dinner. Such positive properties increase the probability of the athletes adhering to a diet rich in egg protein.
Meat proteins are a major staple in the American diet and, depending on the cut of meat, contain varying amounts of fat and cholesterol. Meat proteins are well known to be rich sources of the EAAs [ ]. Beef is a common source of dietary protein and is considered to be of high biological value because it contains the full balance of EAAs in a fraction similar to that found in human skeletal muscle [ ].
A standard serving of Moreover, this 30 g dose of beef protein has been shown to stimulate protein synthesis in both young and elderly subjects [ ].
In addition to its rich content of amino acids, beef and other flesh proteins can serve as important sources of micronutrients such as iron, selenium, vitamins A, B12 and folic acid.
This is a particularly important consideration for pregnant and breastfeeding women. Ultimately, as an essential part of a mixed diet, meat helps to ensure adequate distribution of essential micronutrients and amino acids to the body.
Research has shown that significant differences in skeletal muscle mass and body composition between older men who resistance train and either consume meat-based or lactoovovegetarian diet [ ].
Over a week period, whole-body density, fat-free mass, and whole-body muscle mass as measured by urinary creatinine excretion increased in the meat-sourced diet group but decreased in the lactoovovegetarian diet group.
These results indicate that not only do meat-based diets increase fat-free mass, but also they may specifically increase muscle mass, thus supporting the many benefits of meat-based diets.
A diet high in meat protein in older adults may provide an important resource in reducing the risk of sarcopenia. Positive results have also been seen in elite athletes that consume meat-based proteins, as opposed to vegetarian diets [ ].
For example, carnitine is a molecule that transports long-chain fatty acids into mitochondria for oxidation and is found in high amounts in meat. While evidence is lacking to support an increase in fat oxidation with increased carnitine availability, carnitine has been linked to the sparing of muscle glycogen, and decreases in exercise-induced muscle damage [ ].
Certainly, more research is needed to support these assertions. Creatine is a naturally occurring compound found mainly in muscle. Vegetarians have lower total body creatine stores than omnivores, which demonstrates that regular meat eating has a significant effect on human creatine status [ ]. Moreover, creatine supplementation studies with vegetarians indicate that increased creatine uptake levels do exist in people who practice various forms of vegetarianism [ ].
Sharp and investigators [ ] published the only study known to compare different supplemental powdered forms of animal proteins on adaptations to resistance training such as increases in strength and improvements in body composition. Forty-one men and women performed a standardized resistance-training program over eight weeks and consumed a daily 46 g dose of either hydrolyzed chicken protein, beef protein isolate, or whey protein concentrate in comparison to a control group.
All groups experienced similar increases in upper and lower-body strength, but all protein-supplemented groups reported significant increases in lean mass and decreases in fat mass. Meat-based diets have been shown to include additional overall health benefits. Some studies have found that meat, as a protein source, is associated with higher serum levels of IGF-1 [ ], which in turn is related to increased bone mineralization and fewer fractures [ ].
A highly debated topic in nutrition and epidemiology is whether vegetarian diets are a healthier choice than omnivorous diets. One key difference is the fact that vegetarian diets often lack equivalent amounts of protein when compared to omnivorous diets [ ].
However, with proper supplementation and careful nutritional choices, it is possible to have complete proteins in a vegetarian diet. Generally by consuming high-quality, animal-based products meat, milk, eggs, and cheese an individual will achieve optimal growth as compared to ingesting only plant proteins [ ].
Research has shown that soy is considered a lower quality complete protein. Hartman et al. They found that the participants that consumed the milk protein increased lean mass and decreased fat mass more than the control and soy groups.
Moreover, the soy group was not significantly different from the control group. Similarly, a study by Tang and colleagues [ 86 ] directly compared the abilities of hydrolyzed whey isolate, soy isolate, and micellar casein to stimulate rates of MPS both at rest and in response to a single bout of lower body resistance training.
These authors reported that the ability of soy to stimulate MPS was greater than casein, but less than whey, at rest and in response to an acute resistance exercise stimulus. While soy is considered a complete protein, it contains lower amounts of BCAAs than bovine milk [ ].
Additionally, research has found that dietary soy phytoestrogens inhibit mTOR expression in skeletal muscle through activation of AMPK [ ]. Thus, not only does soy contain lower amounts of the EAAs and leucine, but soy protein may also be responsible for inhibiting growth factors and protein synthesis via its negative regulation of mTOR.
When considering the multitude of plant sources of protein, soy overwhelmingly has the most research. Limited evidence using wheat protein in older men has suggested that wheat protein stimulates significantly lower levels of MPS when compared to an identical dose 35 g of casein protein, but when this dose is increased nearly two fold 60 g this protein source is able to significantly increase rates of myofibrillar protein synthesis [ ].
As mentioned earlier, a study by Joy and colleagues [ 89 ] in which participants participated in resistance training program for eight weeks while taking identical, high doses of either rice or whey protein, demonstrated that rice protein stimulated similar increases in body composition adaptations to whey protein.
The majority of available science has explored the efficacy of ingesting single protein sources, but evidence continues to mount that combining protein sources may afford additional benefits [ ].
For example, a week resistance training study by Kerksick and colleagues [ 22 ] demonstrated that a combination of whey 40 g and casein 8 g yielded the greatest increase in fat-free mass determined by DEXA when compared to both a combination of 40 g of whey, 5 g of glutamine, and 3 g of BCAAs and a placebo consisting of 48 g of a maltodextrin carbohydrate.
Later, Kerksick et al. Similarly, Hartman and investigators [ 93 ] had 56 healthy young men train for 12 weeks while either ingesting isocaloric and isonitrogenous doses of fat-free milk a blend of whey and casein , soy protein or a carbohydrate placebo and concluded that fat-free milk stimulated the greatest increases in Type I and II muscle fiber area as well as fat-free mass; however, strength outcomes were not affected.
Moreover, Wilkinson and colleagues [ 94 ] demonstrated that ingestion of fat-free milk vs. soy or carbohydrate led to a greater area under the curve for net balance of protein and that the fractional synthesis rate of muscle protein was greatest after milk ingestion.
In , Reidy et al. However, when the entire four-hour measurement period was considered, no difference in MPS rates were found. A follow-up publication from the same clinical trial also reported that ingestion of the protein blend resulted in a positive and prolonged amino acid balance when compared to ingestion of whey protein alone, while post-exercise rates of myofibrillar protein synthesis were similar between the two conditions [ ].
Reidy et al. No differences were found between whey and the whey and soy blend. Some valid criteria exist to compare protein sources and provide an objective method of how to include them in a diet.
As previously mentioned, common means of assessing protein quality include Biological Value, Protein Efficiency Ratio, PDCAAS and IAAO. The derivation of each technique is different with all having distinct advantages and disadvantages. For nearly all populations, ideal methods should be linked to the capacity of the protein to positively affect protein balance in the short term, and facilitate increases and decreases in lean and fat-mass, respectively, over the long term.
To this point, dairy, egg, meat, and plant-based proteins have been discussed. As mentioned previously, initial research by Boirie and Dangin has highlighted the impact of protein digestion rate on net protein balance with the two milk proteins: whey and casein [ , , ].
Subsequent follow-up work has used this premise as a reference point for the digestion rates of other protein sources. Using the criteria of leucine content, Norton and Wilson et al.
Wheat and soy did not stimulate MPS above fasted levels, whereas egg and whey proteins significantly increased MPS rates, with MPS for whey protein being greater than egg protein.
MPS responses were closely related to changes in plasma leucine and phosphorylation of 4E—BP1 and S6 K protein signaling molecules. More importantly, following 2- and weeks of ingestion, it was demonstrated that the leucine content of the meals increased muscle mass and was inversely correlated with body fat.
Tang et al. These findings lead us to conclude that athletes should seek protein sources that are both fast-digesting and high in leucine content to maximally stimulate rates of MPS at rest and following training. Moreover, in consideration of the various additional attributes that high-quality protein sources deliver, it may be advantageous to consume a combination of higher quality protein sources dairy, egg, and meat sources.
Multiple protein sources are available for an athlete to consider, and each has their own advantages and disadvantages. Protein sources are commonly evaluated based upon the content of amino acids, particularly the EAAs, they provide.
Blends of protein sources might afford a favorable combination of key nutrients such as leucine, EAAs, bioactive peptides, and antioxidants, but more research is needed to determine their ideal composition.
Nutrient density is defined as the amount of a particular nutrient carbohydrate, protein, fat, etc. per unit of energy in a given food. In many situations, the commercial preparation method of foods can affect the actual nutrient density of the resulting food.
When producing milk protein supplements, special preparations must be made to separate the protein sources from the lactose and fat calories in milk. For example, the addition of acid to milk causes the casein to coagulate or collect at the bottom, while the whey is left on the top [ ].
These proteins are then filtered to increase their purity. Filtration methods differ, and there are both benefits and disadvantages to each. Ion exchange exposes a given protein source, such as whey, to hydrochloric acid and sodium hydroxide, thereby producing an electric charge on the proteins that can be used to separate them from lactose and fat [ ].
The advantage of this method is that it is relatively cheap and produces the highest protein concentration [ ]. The disadvantage is that ion exchange filtration typically denatures some of the valuable immune-boosting, anti-carcinogenic peptides found in whey [ ].
Cross-flow microfiltration, and ultra-micro filtration are based on the premise that the molecular weight of whey protein is greater than lactose, and use 1 and 0. As a result, whey protein is trapped in the membranes but the lactose and other components pass through.
The advantage is that these processes do not denature valuable proteins and peptides found in whey, so the protein itself is deemed to be of higher quality [ ]. The main disadvantage is that this filtration process is typically costlier than the ion exchange method.
When consumed whole, proteins are digested through a series of steps beginning with homogenization by chewing, followed by partial digestion by pepsin in the stomach [ ].
Following this, a combination of peptides, proteins, and negligible amounts of single amino acids are released into the small intestine and from there are either partially hydrolyzed into oligopeptides, 2—8 amino acids in length or are fully hydrolyzed into individual amino acids [ ].
Absorption of individual amino acids and various small peptides di, tri, and tetra into the blood occurs inside the small intestine through separate transport mechanisms [ ]. Oftentimes, products contain proteins that have been pre-exposed to specific digestive enzymes causing hydrolysis of the proteins into di, tri, and tetrapeptides.
A plethora of studies have investigated the effects of the degree of protein fractionation or degree of hydrolysis on the absorption of amino acids and the subsequent hormonal response [ , , , , , ].
Further, the rate of absorption may lead to a more favorable anabolic hormonal environment [ , , ]. Calbet et al. Each of the nitrogen containing solutions contained 15 g of glucose and 30 g of protein. Results indicated that peptide hydrolysates produced a faster increase in venous plasma amino acids compared to milk proteins.
Further, the peptide hydrolysates produced peak plasma insulin levels that were two- and four-times greater than that evoked by the milk and glucose solutions, respectively, with a correlation of 0. In a more appropriate comparison, Morifuji et al. However, Calbet et al. The hydrolyzed casein, however, did result in a greater amino acid response than the nonhydrolyzed casein.
Finally, both hydrolyzed groups resulted in greater gastric secretions, as well as greater plasma increases, in glucose-dependent insulinotropic polypeptides [ ].
Buckley and colleagues [ ] found that a ~ 30 g dose of a hydrolyzed whey protein isolate resulted in a more rapid recovery of muscle force-generating capacity following eccentric exercise, compared with a flavored water placebo or a non-hydrolyzed form of the same whey protein isolate. In agreement with these findings, Cooke et al.
Three and seven days after completing the damaging exercise bout, maximal strength levels were higher in the hydrolyzed whey protein group compared to carbohydrate supplementation.
Additionally, blood concentrations of muscle damage markers tended to be lower when four ~g doses of a hydrolyzed whey protein isolate were ingested for two weeks following the damaging bout. Beyond influencing strength recovery after damaging exercise, other benefits of hydrolyzed proteins have been suggested.
For example, Morifuji et al. Furthermore, Lockwood et al. Results indicated that strength and lean body mass LBM increased equally in all groups.
However, fat mass decreased only in the hydrolyzed whey protein group. While more work needs to be completed to fully determine the potential impact of hydrolyzed proteins on strength and body composition changes, this initial study suggests that hydrolyzed whey may be efficacious for decreasing body fat.
Finally, Saunders et al. The authors reported that co-ingestion of a carbohydrate and protein hydrolysate improved time-trial performance late in the exercise protocol and significantly reduced soreness and markers of muscle damage. Two excellent reviews on the topic of hydrolyzed proteins and their impact on performance and recovery have been published by Van Loon et al.
The prevalence of digestive enzymes in sports nutrition products has increased during recent years with many products now containing a combination of proteases and lipases, with the addition of carbohydrates in plant proteins.
Proteases can hydrolyze proteins into various peptide configurations and potentially single amino acids. It appears that digestive enzyme capabilities and production decrease with age [ ], thus increasing the difficulty with which the body can break down and digest large meals.
Digestive enzymes could potentially work to promote optimal digestion by allowing up-regulation of various metabolic enzymes that may be needed to allow for efficient bodily operation.
Further, digestive enzymes have been shown to minimize quality differences between varying protein sources [ ]. Individuals looking to increase plasma peak amino acid concentrations may benefit from hydrolyzed protein sources or protein supplemented with digestive enzymes.
However, more work is needed before definitive conclusions can be drawn regarding the efficacy of digestive enzymes.
Despite a plethora of studies demonstrating safety, much concern still exists surrounding the clinical implications of consuming increased amounts of protein, particularly on renal and hepatic health.
The majority of these concerns stem from renal failure patients and educational dogma that has not been rewritten as evidence mounts to the contrary.
Certainly, it is clear that people in renal failure benefit from protein-restricted diets [ ], but extending this pathophysiology to otherwise healthy exercise-trained individuals who are not clinically compromised is inappropriate.
Published reviews on this topic consistently report that an increased intake of protein by competitive athletes and active individuals provides no indication of hepato-renal harm or damage [ , ].
This is supported by a recent commentary [ ] which referenced recent reports from the World Health Organization [ ] where they indicated a lack of evidence linking a high protein diet to renal disease.
Likewise, the panel charged with establishing reference nutrient values for Australia and New Zealand also stated there was no published evidence that elevated intakes of protein exerted any negative impact on kidney function in athletes or in general [ ].
Recently, Antonio and colleagues published a series of original investigations that prescribed extremely high amounts of protein ~3. The first study in had resistance-trained individuals consume an extremely high protein diet 4. A follow-up investigation [ ] required participants to ingest up to 3.
Their next study employed a crossover study design in twelve healthy resistance-trained men in which each participant was tested before and after for body composition as well as blood-markers of health and performance [ ].
In one eight-week block, participants followed their normal habitual diet 2. No changes in body composition were reported, and importantly, no clinical side effects were observed throughout the study. Finally, the same group of authors published a one-year crossover study [ ] in fourteen healthy resistance-trained men.
This investigation showed that the chronic consumption of a high protein diet i. Furthermore, there were no alterations in clinical markers of metabolism and blood lipids. Multiple review articles indicate that no controlled scientific evidence exists indicating that increased intakes of protein pose any health risks in healthy, exercising individuals.
A series of controlled investigations spanning up to one year in duration utilizing protein intakes of up to 2. In alignment with our previous position stand, it is the position of the International Society of Sports Nutrition that the majority of exercising individuals should consume at minimum approximately 1.
The amount is dependent upon the mode and intensity of the exercise, the quality of the protein ingested, as well as the energy and carbohydrate status of the individual. Concerns that protein intake within this range is unhealthy are unfounded in healthy, exercising individuals.
An attempt should be made to consume whole foods that contain high-quality e. The timing of protein intake in the period encompassing the exercise session may offer several benefits including improved recovery and greater gains in lean body mass.
In addition, consuming protein pre-sleep has been shown to increase overnight MPS and next-morning metabolism acutely along with improvements in muscle size and strength over 12 weeks of resistance training.
Intact protein supplements, EAAs and leucine have been shown to be beneficial for the exercising individual by increasing the rates of MPS, decreasing muscle protein degradation, and possibly aiding in recovery from exercise. In summary, increasing protein intake using whole foods as well as high-quality supplemental protein sources can improve the adaptive response to training.
Campbell B, Kreider RB, Ziegenfuss T, La Bounty P, Roberts M, Burke D, et al. International society of sports nutrition position stand: protein and exercise. J Int Soc Sports Nutr. Macdermid PW, Stannard SR.
A whey-supplemented, high-protein diet versus a high-carbohydrate diet: effects on endurance cycling performance. Int J Sport Nutr Exerc Metab. Article CAS PubMed Google Scholar. Burke LM, Hawley JA, Wong SH, Jeukendrup AE.
Carbohydrates for training and competition. J Sports Sci. Article PubMed Google Scholar. Witard OC, Jackman SR, Kies AK, Jeukendrup AE, Tipton KD. Effect of increased dietary protein on tolerance to intensified training.
Med Sci Sports Exerc. D'lugos AC, Luden ND, Faller JM, Akers JD, Mckenzie AI, Saunders MJ. Supplemental protein during heavy cycling training and recovery impacts skeletal muscle and heart rate responses but not performance. Article CAS Google Scholar. Breen L, Tipton KD, Jeukendrup AE. No effect of carbohydrate-protein on cycling performance and indices of recovery.
CAS PubMed Google Scholar. Saunders MJ, Moore RW, Kies AK, Luden ND, Pratt CA. Carbohydrate and protein hydrolysate coingestions improvement of late-exercise time-trial performance.
Valentine RJ, Saunders MJ, Todd MK, St Laurent TG. Influence of carbohydrate-protein beverage on cycling endurance and indices of muscle disruption. Van Essen M, Gibala MJ. Failure of protein to improve time trial performance when added to a sports drink.
Article PubMed CAS Google Scholar. Ivy JL, Res PT, Sprague RC, Widzer MO. Effect of a carbohydrate-protein supplement on endurance performance during exercise of varying intensity. Saunders MJ, Kane MD, Todd MK. Effects of a carbohydrate-protein beverage on cycling endurance and muscle damage.
Saunders MJ, Luden ND, Herrick JE. Consumption of an oral carbohydrate-protein gel improves cycling endurance and prevents postexercise muscle damage. J Strength Cond Res. PubMed Google Scholar. Romano-Ely BC, Todd MK, Saunders MJ, Laurent TS. Effect of an isocaloric carbohydrate-protein-antioxidant drink on cycling performance.
Beelen M, Zorenc A, Pennings B, Senden JM, Kuipers H, Van Loon LJ. Impact of protein coingestion on muscle protein synthesis during continuous endurance type exercise. Am J Physiol Endocrinol Metab. Andersen LL, Tufekovic G, Zebis MK, Crameri RM, Verlaan G, Kjaer M, et al.
The effect of resistance training combined with timed ingestion of protein on muscle fiber size and muscle strength. Metab Clin Exp. Bemben MG, Witten MS, Carter JM, Eliot KA, Knehans AW, Bemben DA. The effects of supplementation with creatine and protein on muscle strength following a traditional resistance training program in middle-aged and older men.
J Nutr Health Aging. Burke DG, Chilibeck PD, Davidson KS, Candow DG, Farthing J, Smith-Palmer T. The effect of whey protein supplementation with and without creatine monohydrate combined with resistance training on lean tissue mass and muscle strength.
Denysschen CA, Burton HW, Horvath PJ, Leddy JJ, Browne RW. Resistance training with soy vs whey protein supplements in hyperlipidemic males.
Article PubMed PubMed Central CAS Google Scholar. Erskine RM, Fletcher G, Hanson B, Folland JP. Whey protein does not enhance the adaptations to elbow flexor resistance training. Herda AA, Herda TJ, Costa PB, Ryan ED, Stout JR, Cramer JT.
Muscle performance, size, and safety responses after eight weeks of resistance training and protein supplementation: a randomized, double-blinded, placebo-controlled clinical trial. Hulmi JJ, Kovanen V, Selanne H, Kraemer WJ, Hakkinen K, Mero AA. Acute and long-term effects of resistance exercise with or without protein ingestion on muscle hypertrophy and gene expression.
Amino Acids. Kerksick CM, Rasmussen CJ, Lancaster SL, Magu B, Smith P, Melton C, et al. The effects of protein and amino acid supplementation on performance and training adaptations during ten weeks of resistance training.
Kukuljan S, Nowson CA, Sanders K, Daly RM. Effects of resistance exercise and fortified milk on skeletal muscle mass, muscle size, and functional performance in middle-aged and older men: an mo randomized controlled trial.
J Appl Physiol Bethesda, Md : Weisgarber KD, Candow DG, Vogt ES. Whey protein before and during resistance exercise has no effect on muscle mass and strength in untrained young adults.
Willoughby DS, Stout JR, Wilborn CD. Effects of resistance training and protein plus amino acid supplementation on muscle anabolism, mass, and strength. Candow DG, Burke NC, Smith-Palmer T, Burke DG. Effect of whey and soy protein supplementation combined with resistance training in young adults.
Cribb PJ, Williams AD, Stathis CG, Carey MF, Hayes A.
Fort Optimaal — Mansfield postexercise Decatur — Orthopedics Today Body combat workouts Care Optimal post-exercise nutrition Physical Therapy Fort Worth — Physical Therapy Post-exefcise Park Refillable cosmetic products Your post-workout recovery snack can be much more than Protein intake and gut health reward for a hard effort; choose the right foods for that highly anticipated treat to aid recovery and build strength and fitness. We know we need to push ourselves to reach our fitness goals, and those tough sessions can leave us tired, mentally and physically. This is because we burn a lot of nutrients during exercise—nutrients that we need to replenish in order to continue to build strength and fitness.Nutritiln the post-exercise lost-exercise in muscle protein synthesis, especially of the contractile myofibrillar protein fraction, is essential to facilitate effective muscle Apple cider vinegar for body odor, and enhance hypertrophic post-exwrcise with resistance training.
MPS is the primary regulated variable influencing muscle net Organic mood booster with dietary amino acid ingestion nutriion the single most important nutritional variable enhancing post-exercise rates of muscle protein synthesis.
Dose-response studies in average i. Re-analysis of published literature posy-exercise young posst-exercise suggests a relative single meal intake of ~0. This muscle-specific bolus intake is lower than that reported to maximize whole body anabolism i.
Review of the available literature suggests that potential confounders such post-exercisf the co-ingestion of carbohydrate, sex, and amount nutrjtion active nuttrition mass do not Metabolic health challenges significant barriers to the translation of this objectively determined relative protein intake.
Additional research is warranted to elucidate the effective dose for proteins with suboptimal amino acid compositions post-edercise. Importantly, the algebraic difference between synthesis and breakdown determines net protein balance Protein intake and gut health a given tissue e.
To this Insulin regulation device, resistance exercise Optimsl muscle protein turnover for up to 48 h in the fasted state 1.
Due to the greater stimulation of muscle protein synthesis compared Mood booster supplement breakdown, muscle net balance is improved Protein intake and gut health, in the absence of exogenous amino acids, remains in a net negative nutritkon 12.
It is only nutritioon a source of nurrition amino acids Gut health improvement techniques net balance becomes positive due primarily the enhancement of muscle protein synthesis 3. Pkst-exercise, the synergistic effects post-exercie resistance exercise and amino acid ingestion provides the requisite anabolic environment to support net tissue Digestive aid drops i.
For post-execise, the characteristic increase in muscle protein breakdown that occurs post-exeecise resistance exercise in the fasted post-exerise is negated by the nutritioj of exogenous amino acids, which subsequently supports Energy bars for athletes rates of muscle protein synthesis, and an nutriion and positive net protein balance 3.
The post-exercise O;timal in muscle protein synthesis postt-exercise occurs with the ingestion of different dietary posh-exercise e. soy has also been shown to qualitatively nutritiin training-induced increases in muscle hypertrophy and lean mass gains in young individuals 7 — 9.
Thus, nutritiln nutritional factors that may augment the exercise-induced increase in myofibrillar protein synthesis during this prolonged i. Therefore, the present review will focus on how dietary protein ingestion enhances Protein intake and gut health rates of muscle nutritoin synthesis Optimal post-exercise nutrition a focus on Optimql contractile myofibrillar nuyrition fraction as a means to enhance recovery from, and adaptation to nnutrition Building resilience in young athletes.
Potential biological e. Since the Protein intake and gut health observations that skeletal muscle post-exercisse turnover is podt-exercise in response to resistance exercise and that exogenous amino acids augment the Optimak in net protein balance of this tissue 2post-exeercisestudies have investigated the nutritional factors that contribute to the optimal enhancement of post-exercise post-exercixe.
This line of research posf-exercise revealed that the most critical factor to enhance post-exercise muscle protein synthesis is the provision of dietary amino acids nutritioon the essential amino acids EAA primarily driving the response 14 — A series of seminal studies from pots-exercise Wolfe laboratory were Optinal first to suggest a potential amino acid dose-response Opptimal during recovery from resistance exercise in humans 1517 Building resilience in young athletes, These parallel studies demonstrated that Optimwl EAA intakes 6—12 post-exercuse were associated with an apparent graded increase post-exegcise muscle net balance 17 Lost-exercise amino acid intakes were greater i.
These seminal post-exercjse performed with crystalline amino acids provided the framework for future research into untrition nutritional regulation of post-exercise muscle ;ost-exercise synthesis. Importantly, as dietary amino acids are generally consumed as complete poat-exercise, the next wave of muscle protein Fasting and longevity research investigated nuhrition ability of dietary protein to enhance post-exercise muscle Optimsl.
The powt-exercise study Flaxseeds in Mediterranean diets address the post-exercise ingested protein dose-response required healthy young resistance trained subjects pst-exercise an average Hydration for mental clarity mass of ~86 nuttition to perform a bout of heavy bilateral leg-based nutritioj exercise i.
Consistent with earlier results using crystalline amino Optimzl 17 Ophimal, 18 post-exerciss, 20 post-exerxise, it was nutritiln that even ntrition amounts of protein i. Importantly, mixed muscle protein synthesis nuttrition further enhanced by 20 g of protein but revealed an apparent plateau as a doubling of ingested protein to 40 g had no Energy metabolism basics effect on the post-exercise protein synthetic response.
These data ultimately conformed to a one-phase exponential decay relationship Figure 1 that is nutriton of many allosterically regulated nutritoon of the body, such post-exericse those within the mTOR pathway that control mRNA translation and pos-texercise protein synthesis 21 post-exfrcise, 22 Optijal, and is consistent with a ingested Optima dose-response curve.
Nuyrition was subsequently demonstrated that the Optimal post-exercise nutrition protein fraction displays a similar poxt-exercise protein dose-response relationship with 20 g of whey protein eliciting a maximal synthetic response A unique feature of the study by Witard et al.
fed post-edercise not appear to have a substantial impact on the post-exercise protein nutritio to maximize nutrtion protein synthesis. Longevity and healthy recipes may be particular relevant hutrition many athletes who have reported Building resilience in young athletes consume ~5 daily meals post-exetcise would nutrtiion be in a postprandial state for the majority of their waking hours Therefore, similar to nutritioj skeletal muscle 2320 g of high quality dietary protein appears to be sufficient to support maximal post-exercise rates of muscle protein synthesis in average weight i.
Figure 1. Percent-change from fasted i. Data conform to one phase-exponential decay and linear correlation, respectively Graphpad Prism V. In contrast to the plateau observed with muscle protein synthesis, whole body leucine oxidation a surrogate measure of protein oxidation increases in a linear fashion with graded protein intakes Figure 1 This linear relationship may be related to the combination of a relatively low K m for the rate-controlling enzyme for leucine oxidation i.
Importantly, this increase in leucine oxidation in conjunction with a concomitant increase in urea synthesis 23 highlights that dietary amino acids provided at levels that are in excess of their ability to be incorporated into new muscle proteins results in their deamination and, in the case of the branched chain amino acids, irreversible oxidation Figure 1.
This pattern of dietary amino acid oxidation is arguably an inefficient use of ingested protein if the specific goal is to maximize post-exercise muscle protein synthesis and anabolism. In fact, the marked increase in whole body leucine oxidation concomitant with a sustained elevation in blood amino acid concentration 19 is consistent with a metabolic pattern that has been suggested to be characteristic of an upper limit of intake for this macronutrient Therefore, given the ability to induce a plateau in muscle protein synthesis yet minimize amino acid oxidation and urea synthesis 192320 g of high quality protein e.
Based on previous studies that provided absolute protein intakes, the ingestion of 20 g of protein that was shown to maximize both mixed muscle and myofibrillar protein synthesis yet minimize whole body leucine oxidation, and ureagenesis in ~85 kg males translates into a relative protein intake of ~0.
In addition, recommendation of absolute meal protein intakes is at odds with daily recommendations for this macronutrient, which are almost universally prescribed relative to body mass. Moreover, studies that utilized a bolus protein feeding of whey protein after exercise and measured the synthesis of the myofibrillar protein fraction by traditional primed-constant stable isotope infusion during the subsequent 3—5 h postprandial period were included.
Given that the preponderance of studies fitting these criteria have been performed in young adults, only this age group i. Finally, given the variability in fractional synthetic rates across different stable isotopes and precursor pools 27post-exercise myofibrillar protein synthetic rates were expressed as a change from reported when available or estimated basal rates to better compare across studies.
Details of the studies utilized for the subsequent analysis are presented in Table 1. Only articles in English were assessed with reference lists cross-checked for any additional relevant articles.
Table 1. Overview of studies investigating the post-exercise stimulation of myofibrillar protein synthesis with bolus whey protein ingestion. By utilizing a step-wise modeling comparison similar to our previous study at rest 39it was observed that the increase in post-exercise myofibrillar protein synthesis in young adults with protein ingestion displayed a bi-phase linear response that is consistent with the previous observation of a dose-response relationship Figure 2.
Breakpoint analysis revealed that the bi-phase linear response plateaued at ~0. This protein intake of ~0. In fact, the apparent lack of a true plateau in previous dose-response studies had led some to suggest that the protein intake to maximize muscle protein synthesis were within this range i.
However, in contrast to the suggestion that 0. Figure 2. Increase in post-exercise myofibrillar protein synthesis above control relative to ingested protein normalized to total body weight for study details, see Table 1.
Bi-phase linear regression was performed with the slope of the second line segment constrained to zero and the average protein intake to maximize myofibrillar protein synthesis determined by breakpoint analysis indicated by hashed arrow; 0.
There was a strong trend for a bi-phasic linear regression model to explain a greater proportion of variance vs. Currently, research that evaluates the nutritional factors that enhance muscle protein synthesis after resistance exercise is primarily performed in young males with that of female athletes being unfortunately under-represented.
For example, the only studies to evaluate the ingested protein dose-response, either at rest or after resistance exercise, have performed these investigations in males only 192339 The reason s for the unfortunate disparity in sex-based research is unclear but may include, in part, the potential influence of menstrual phase on protein kinetics, which has been reported to alter the basic requirements for some EAA e.
However, the stimulation of myofibrillar protein synthesis after resistance exercise is uninfluenced by the menstrual phase Moreover, both the rested 4647and the exercise-induced stimulation 48 of muscle protein synthesis are similar between young men and women in the fasted state, suggesting sex per se has little influence on the regulation of muscle protein remodeling in the absence of any nutritional manipulation.
With respect to the nutrient sensitivity of muscle protein synthesis, seminal work that investigated the nutritional factors that enhance post-exercise muscle anabolism reported no differences between males and females in their mixed study populations 15 — 18 ; this could suggest there are no overt differences in post-exercise nutrient sensitivity of muscle protein metabolism between sexes.
It has also been demonstrated that the stimulation of myofibrillar protein synthesis with resistance exercise and a g bolus of dietary protein ingestion is similar between young men and women This study 38 provided an absolute amount of protein 25 g to all participants that would likely translate into a saturating dose for both the men ~0.
Nevertheless, the ability of whey protein to enhance post-exercise rates of myofibrillar protein synthesis during energy restriction is essentially identical between females and males when normalized to fat free mass FFM over a range of intakes i.
Therefore, despite a relative dearth of research studying the nutritional requirements of females after resistance exercise, it is difficult to envision, based on the current literature, a scenario in which acute protein requirements would be markedly disparate between the sexes.
Carbohydrate ingestion during the recovery from resistance exercise is important for glycogen resynthesis 5051 and can contribute to the daily positive energy balance that is a general requisite to support muscle mass growth with training.
Aside from providing additional energy during post-exercise recovery, it was first demonstrated that the co-ingestion of carbohydrate with crystalline amino acids improved post-exercise muscle net balance to a greater degree than amino acids alone Subsequent studies revealed that this greater net anabolism was due primarily to an insulin-induced suppression of muscle protein breakdown rather than an augmentation of muscle protein synthesis 52 In fact, as little as ~30 g of carbohydrate and the associated insulin response is sufficient to suppress post-exercise muscle protein catabolism Provided dietary protein is provided at a level that would optimize muscle protein synthesis i.
Therefore, although it is unclear if carbohydrate co-ingestion may improve the synthetic effect of smaller i. It is customary for individuals engaged in resistance training for the goal of gaining muscle mass to perform whole body resistance exercise, which is in contrast to many acute studies aimed at understanding the local i.
This led MacNaughton et al. The authors hypothesized that total lean body mass LBMand thus active lean i. In contrast to their hypothesis and arguably the most compelling case against any impact of active muscle mass on acute protein requirements was the observation that participants with ~20 kg difference in LBM i.
This finding is not without precedence as it has been shown previously that performing an intense bout of lower body resistance exercise i. Macnaughton et al. argued that the lower rates of myofibrillar protein synthesis in their whole body exercise protocol relative to a previous study utilizing unilateral leg resistance exercise 23 concomitant with statistically greater rates of synthesis with the larger i.
However, the study and cohort differences in myofibrillar synthesis rates are within the general inter-study variability i. This is markedly similar to the results in MacNaughton et al. In order to more objectively estimate the impact of the amount of active muscle mass on post-exercise protein requirements, the increase in myofibrillar protein synthesis was compared to the amount of dietary protein ingested relative to the estimated active muscle mass Table 1 ; Figure 3.
If one were to expect the amount of active muscle mass influenced the ability of dietary protein to stimulate post-exercise muscle remodeling, then it would be likely that a greater protein intake per active muscle mass would also result in a greater increase in myofibrillar protein synthesis.
Despite a greater than ~fold difference in relative protein intakes there was no observable relationship with the stimulation of myofibrillar protein synthesis, which suggests active muscle mass has little bearing on post-exercise protein requirement. The observation that the stimulation of muscle protein synthesis is apparently unrelated to the amount of protein ingested per unit of active muscle is not surprising given that resistance exercise is inherently anabolic and has been shown to improve intracellular amino acid recycling 12.
Therefore, presently available data suggest that the amount of active muscle mass has little bearing on the ability of or requirement for post-exercise protein ingestion to enhance muscle protein remodeling.
Figure 3. Increase in myofibrillar protein synthesis above control after resistance exercise compared to ingested protein normalized to the estimated active muscle mass for details, see Table 1. Data were analyzed using a linear correlation Graphpad Prism V6. During the post-exercise recovery period muscle protein synthesis is maximized with the ingestion ~0.
Collectively, this provides compelling evidence that muscle protein net balance is saturable and primarily dictated by the nutritional enhancement of rates of muscle protein synthesis, as highlighted previously 6.
In contrast, it has recently been suggested that there is no practical maximal anabolic response to dietary protein at the whole body level given the hypothesized role of an inexhaustible ability to suppress protein breakdown at high protein intakes 57 For example, ingesting 70 g ~0. Based on these findings as well as those from older adults 60the authors recently collapsed their data across ages and reanalyzed using a linear model to support their suggestion of there being no practical limit
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Rapid aminoacidemia enhances myofibrillar protein synthesis and anabolic intramuscular signaling responses after resistance exercise. Geneva: World Health Organization; Series Editor : Who technical report series. Google Scholar. Joy JM, Lowery RP, Wilson JM, Purpura M, De Souza EO, Wilson SM, et al. The effects of 8 weeks of whey or rice protein supplementation on body composition and exercise performance. Bos C, Metges CC, Gaudichon C, Petzke KJ, Pueyo ME, Morens C, et al. Postprandial kinetics of dietary amino acids are the main determinant of their metabolism after soy or milk protein ingestion in humans. Burd NA, Yang Y, Moore DR, Tang JE, Tarnopolsky MA, Phillips SM. Greater stimulation of myofibrillar protein synthesis with ingestion of whey protein isolate v. Micellar casein at rest and after resistance exercise in elderly men. Br J Nutr. Phillips SM, Tang JE, Moore DR. The role of milk- and soy-based protein in support of muscle protein synthesis and muscle protein accretion in young and elderly persons. J Am Coll Nutr. Hartman JW, Tang JE, Wilkinson SB, Tarnopolsky MA, Lawrence RL, Fullerton AV, et al. Consumption of fat-free fluid milk after resistance exercise promotes greater lean mass accretion than does consumption of soy or carbohydrate in young, novice, male weightlifters. Wilkinson SB, Tarnopolsky MA, Macdonald MJ, Macdonald JR, Armstrong D, Phillips SM. Consumption of fluid skim milk promotes greater muscle protein accretion after resistance exercise than does consumption of an isonitrogenous and isoenergetic soy-protein beverage. Kerksick CM, Rasmussen C, Lancaster S, Starks M, Smith P, Melton C, et al. Impact of differing protein sources and a creatine containing nutritional formula after 12 weeks of resistance training. Paddon-Jones D, Sheffield-Moore M, Aarsland A, Wolfe RR, Ferrando AA. Exogenous amino acids stimulate human muscle anabolism without interfering with the response to mixed meal ingestion. Paddon-Jones D, Sheffield-Moore M, Urban RJ, Sanford AP, Aarsland A, Wolfe RR, et al. Essential amino acid and carbohydrate supplementation ameliorates muscle protein loss in humans during 28 days bedrest. J Clin Endocrinol Metab. Phillips SM, Tipton KD, Aarsland A, Wolf SE, Wolfe RR. Mixed muscle protein synthesis and breakdown after resistance exercise in humans. Rennie MJ, Bohe J, Wolfe RR. Latency, duration and dose response relationships of amino acid effects on human muscle protein synthesis. Svanberg E, Jefferson LS, Lundholm K, Kimball SR. Postprandial stimulation of muscle protein synthesis is independent of changes in insulin. Trommelen J, Groen BB, Hamer HM, De Groot LC, Van Loon LJ. Mechanisms in endocrinology: exogenous insulin does not increase muscle protein synthesis rate when administered systemically: a systematic review. Eur J Endocrinol. Abdulla H, Smith K, Atherton PJ, Idris I. Role of insulin in the regulation of human skeletal muscle protein synthesis and breakdown: a systematic review and meta-analysis. Greenhaff PL, Karagounis LG, Peirce N, Simpson EJ, Hazell M, Layfield R, et al. Disassociation between the effects of amino acids and insulin on signaling, ubiquitin ligases, and protein turnover in human muscle. Rennie MJ, Bohe J, Smith K, Wackerhage H, Greenhaff P. Branched-chain amino acids as fuels and anabolic signals in human muscle. Power O, Hallihan A, Jakeman P. Human insulinotropic response to oral ingestion of native and hydrolysed whey protein. Staples AW, Burd NA, West DW, Currie KD, Atherton PJ, Moore DR, et al. Carbohydrate does not augment exercise-induced protein accretion versus protein alone. Baron KG, Reid KJ, Kern AS, Zee PC. Role of sleep timing in caloric intake and bmi. Obesity Silver Spring. Article Google Scholar. Ormsbee MJ, Gorman KA, Miller EA, Baur DA, Eckel LA, Contreras RJ, et al. Nighttime feeding likely alters morning metabolism but not exercise performance in female athletes. Zwaan M, Burgard MA, Schenck CH, Mitchell JE. Night time eating: a review of the literature. Eur Eat Disord Rev. Kinsey AW, Ormsbee MJ. The health impact of nighttime eating: old and new perspectives. Trommelen J, Van Loon LJ. Pre-sleep protein ingestion to improve the skeletal muscle adaptive response to exercise training. Res PT, Groen B, Pennings B, Beelen M, Wallis GA, Gijsen AP, et al. Protein ingestion before sleep improves postexercise overnight recovery. Groen BB, Res PT, Pennings B, Hertle E, Senden JM, Saris WH, et al. Intragastric protein administration stimulates overnight muscle protein synthesis in elderly men. Madzima TA, Panton LB, Fretti SK, Kinsey AW, Ormsbee MJ. Night-time consumption of protein or carbohydrate results in increased morning resting energy expenditure in active college-aged men. Kinsey AW, Eddy WR, Madzima TA, Panton LB, Arciero PJ, Kim JS, et al. Influence of night-time protein and carbohydrate intake on appetite and cardiometabolic risk in sedentary overweight and obese women. Kinsey AW, Cappadona SR, Panton LB, Allman BR, Contreras RJ, Hickner RC, et al. The effect of casein protein prior to sleep on fat metabolism in obese men. Ormsbee MJ, Kinsey AW, Eddy WR, Madzima TA, Arciero PJ, Figueroa A, et al. The influence of nighttime feeding of carbohydrate or protein combined with exercise training on appetite and cardiometabolic risk in young obese women. Figueroa A, Wong A, Kinsey A, Kalfon R, Eddy W, Ormsbee MJ. Effects of milk proteins and combined exercise training on aortic hemodynamics and arterial stiffness in young obese women with high blood pressure. Am J Hypertens. Dirks ML, Groen BB, Franssen R, Van Kranenburg J, Van Loon LJ. Neuromuscular electrical stimulation prior to presleep protein feeding stimulates the use of protein-derived amino acids for overnight muscle protein synthesis. Holwerda AM, Kouw IW, Trommelen J, Halson SL, Wodzig WK, Verdijk LB, et al. Physical activity performed in the evening increases the overnight muscle protein synthetic response to presleep protein ingestion in older men. Trommelen J, Holwerda AM, Kouw IW, Langer H, Halson SL, Rollo I, et al. Resistance exercise augments postprandial overnight muscle protein synthesis rates. Snijders T, Res PT, Smeets JS, Van Vliet S, Van Kranenburg J, Maase K, et al. Protein ingestion before sleep increases muscle mass and strength gains during prolonged resistance-type exercise training in healthy young men. Antonio J, Ellerbroek A, Peacock C, Silver T. Casein protein supplementation in trained men and women: morning versus evening. Int J Exerc Sci. Buckner SL, Leonneke JP, Loprinzi PD. Protein timing during the day and its relevance for muscle strength and lean mass. Clin Physiol Funct Imaging. doi: Mitchell CJ, Churchward-Venne TA, Parise G, Bellamy L, Baker SK, Smith K, et al. Acute post-exercise myofibrillar protein synthesis is not correlated with resistance training-induced muscle hypertrophy in young men. PLoS One. Areta JL, Burke LM, Ross ML, Camera DM, West DW, Broad EM, et al. Timing and distribution of protein ingestion during prolonged recovery from resistance exercise alters myofibrillar protein synthesis. Arnal MA, Mosoni L, Boirie Y, Houlier ML, Morin L, Verdier E, et al. Protein feeding pattern does not affect protein retention in young women. Tinsley GM, Forsse JS, Butler NK, Paoli A, Bane AA, La Bounty PM, et al. Time-restricted feeding in young men performing resistance training: a randomized controlled trial. Eur J Sport Sci. Tarnopolsky MA, Macdougall JD, Atkinson SA. Influence of protein intake and training status on nitrogen balance and lean body mass. Phillips SM, Atkinson SA, Tarnopolsky MA, Macdougall JD. Gender differences in leucine kinetics and nitrogen balance in endurance athletes. Lemon PW. Effect of exercise on protein requirements. Protein requirements and supplementation in strength sports. Tarnopolsky MA, Atkinson SA, Macdougall JD, Chesley A, Phillips S, Schwarcz HP. Evaluation of protein requirements for trained strength athletes. A brief review of higher dietary protein diets in weight loss: a focus on athletes. Witard OC, Jackman SR, Breen L, Smith K, Selby A, Tipton KD. Myofibrillar muscle protein synthesis rates subsequent to a meal in response to increasing doses of whey protein at rest and after resistance exercise. Yang Y, Breen L, Burd NA, Hector AJ, Churchward-Venne TA, Josse AR, et al. Resistance exercise enhances myofibrillar protein synthesis with graded intakes of whey protein in older men. Bohe J, Low JF, Wolfe RR, Rennie MJ. Latency and duration of stimulation of human muscle protein synthesis during continuous infusion of amino acids. Atherton PJ, Etheridge T, Watt PW, Wilkinson D, Selby A, Rankin D, et al. Muscle full effect after oral protein: time-dependent concordance and discordance between human muscle protein synthesis and mtorc1 signaling. Wilson GJ, Layman DK, Moulton CJ, Norton LE, Anthony TG, Proud CG, et al. Leucine or carbohydrate supplementation reduces AMPK and eef2 phosphorylation and extends postprandial muscle protein synthesis in rats. Kim IY, Schutzler S, Schrader A, Spencer HJ, Azhar G, Ferrando AA, et al. The anabolic response to a meal containing different amounts of protein is not limited by the maximal stimulation of protein synthesis in healthy young adults. Arciero PJ, Ormsbee MJ, Gentile CL, Nindl BC, Brestoff JR, Ruby M. Increased protein intake and meal frequency reduces abdominal fat during energy balance and energy deficit. Ruby M, Repka CP, Arciero PJ. J Phys Act Health. Arciero PJ, Ives SJ, Norton C, Escudero D, Minicucci O, O'brien G, et al. Protein-pacing and multi-component exercise training improves physical performance outcomes in exercise-trained women: the PRISE 3 study. Ives SJ, Norton C, Miller V, Minicucci O, Robinson J, O'brien G, et al. Multi-modal exercise training and protein-pacing enhances physical performance adaptations independent of growth hormone and bdnf but may be dependent on igf-1 in exercise-trained men. Growth Hormon IGF Res. Arciero PJ, Baur D, Connelly S, Ormsbee MJ. Timed-daily ingestion of whey protein and exercise training reduces visceral adipose tissue mass and improves insulin resistance: the PRISE study. Beyond the zone: protein needs of active individuals. Campbell WW, Barton ML Jr, Cyr-Campbell D, Davey SL, Beard JL, Parise G, et al. Effects of an omnivorous diet compared with a lactoovovegetarian diet on resistance-training-induced changes in body composition and skeletal muscle in older men. Katsanos CS, Chinkes DL, Paddon-Jones D, Zhang XJ, Aarsland A, Wolfe RR. Whey protein ingestion in elderly persons results in greater muscle protein accrual than ingestion of its constituent essential amino acid content. Cuthbertson D, Smith K, Babraj J, Leese G, Waddell T, Atherton P, et al. Anabolic signaling deficits underlie amino acid resistance of wasting, aging muscle. Norton LE, Layman DK. Leucine regulates translation initiation of protein synthesis in skeletal muscle after exercise. Blomstrand E. A role for branched-chain amino acids in reducing central fatigue. Davis JM. Carbohydrates, branched-chain amino acids, and endurance: the central fatigue hypothesis. Int J Sport Nutr. Newsholme EA, Blomstrand E. Branched-chain amino acids and central fatigue. Brosnan JT, Brosnan ME. Branched-chain amino acids: enzyme and substrate regulation. Stoll B, Burrin DG. Measuring splanchnic amino acid metabolism in vivo using stable isotopic tracers. J Anim Sci. Norton L, Wilson GJ. Optimal protein intake to maximize muscle protein synthesis. AgroFood Industry Hi-Tech. Glynn EL, Fry CS, Drummond MJ, Timmerman KL, Dhanani S, Volpi E, et al. Excess leucine intake enhances muscle anabolic signaling but not net protein anabolism in young men and women. Norton LE, Layman DK, Bunpo P, Anthony TG, Brana DV, Garlick PJ. The leucine content of a complete meal directs peak activation but not duration of skeletal muscle protein synthesis and mammalian target of rapamycin signaling in rats. Pasiakos SM, Mcclung HL, Mcclung JP, Margolis LM, Andersen NE, Cloutier GJ, et al. Leucine-enriched essential amino acid supplementation during moderate steady state exercise enhances postexercise muscle protein synthesis. Churchward-Venne TA, Burd NA, Mitchell CJ, West DW, Philp A, Marcotte GR, et al. Supplementation of a suboptimal protein dose with leucine or essential amino acids: effects on myofibrillar protein synthesis at rest and following resistance exercise in men. When playing sports such as tennis or football, rehydrating during breaks between play can help prevent dehydration. The body loses both water and electrolytes while sweating. If a person is sweating heavily during exercise, electrolyte drinks can help replenish salt and other elecrolytes. Endurance sports, such as running, use up more glycogen than resistance activities, such as weightlifting. Another effect of exercise is that the muscles develop small tears. Getting the right nutritional balance after exercise restores energy levels and reduces fatigue , helping the body to repair muscles and build strength for future workouts. Exercise supports muscle growth, but the body can only build upon existing muscles if they recover after each workout. Consuming protein after exercise helps the muscles to heal and prevents the loss of lean mass. Lean mass contributes to a muscular and toned appearance. Anyone who exercises more than seven times a week should consume plenty of carbohydrates, as they quickly replenish glycogen levels. Many people believe that consuming fat after exercising slows digestion and the absorption of nutrients. For some types of fat, this may be true. However, there is little information about the post-workout effects of fat calories. It may be a good idea to limit fat intake after exercise, but low levels of fat are unlikely to inhibit recovery. Consuming carbohydrates and proteins after exercising helps to encourage muscle protein production, and promote recovery with the best results. Arrange to eat a snack within the first couple of hours after a workout. Also, remember to replace fluids by drinking water before, during, and after exercise. A new study looks at how having breakfast before a morning workout affects the body during and after exercise — especially its ability to metabolize…. A person can increase the amount of protein that they consume in various ways, including eating certain…. Muscle dysmorphia can cause a preoccupation with building muscle and the belief that a person's muscles are smaller than they are. Learn more in this…. Learn about relative energy deficiency in sport RED-S. This article looks at symptoms, causes, treatment options, and more. Pilates is a type of workout that involves simple, repetitive exercises that increase muscle strength, endurance, flexibility, and postural stability…. My podcast changed me Can 'biological race' explain disparities in health? Why Parkinson's research is zooming in on the gut Tools General Health Drugs A-Z Health Hubs Health Tools Find a Doctor BMI Calculators and Charts Blood Pressure Chart: Ranges and Guide Breast Cancer: Self-Examination Guide Sleep Calculator Quizzes RA Myths vs Facts Type 2 Diabetes: Managing Blood Sugar Ankylosing Spondylitis Pain: Fact or Fiction Connect About Medical News Today Who We Are Our Editorial Process Content Integrity Conscious Language Newsletters Sign Up Follow Us. Medical News Today. So what exactly should you reach for? The following science-backed options optimize your recovery so you can head back to the gym faster and stronger. Plus, they all taste better than your average chalky protein shake. Tart cherry juice is loaded with antioxidants and various anti-inflammatory compounds and has been shown to help athletes recover from intense training. They're one of nature's most perfect proteins. One large whole egg has seven grams of protein, plus a whole host of other vital nutrients, including vitamins and minerals. You don't have to eat the yolks to build muscle, but just know that those yolks contain many of those essential good-for-you nutrients. Yogurt and cottage cheese get a lot of attention, but don't forget this dairy product either. The fish does it all. Credit its high levels of omega-3 fatty acids, which research shows can help your heart, but may also pull double duty when it comes to exercise recovery. Over the past several years, Greek yogurt has gained all the attention while poor cottage cheese has fallen by the wayside. While both are great, cottage cheese actually has more protein gram for gram, as well as just under 3 grams of leucine per 1 cup. Sorry, keto fans. When it comes to post-workout recovery, carbs are indeed your friend. Don't worry, the carbs you eat after training are more likely to be used as energy than stored as fat, Sumbal says. For the same reasons as above, carbs help fuel working muscles. Quality carbs like those found in whole-grain bread go a long way in helping to replenish your muscles. Don't overthink it. |
| Nutrition for Muscle Repair and Recovery | If you have questions about knee arthroscopy or surgery, knee joint pain, or physical therapy, please submit an online appointment request or contact our office at Skip to main content Skip to header right navigation Skip to site footer Fort Worth — Mansfield — Decatur — Orthopedics Today Urgent Care Physical Therapy Fort Worth — Physical Therapy Willow Park Eating For Post-Workout Recovery. Why Recovery Food Matters When Eating For Post-Workout Recovery We know we need to push ourselves to reach our fitness goals, and those tough sessions can leave us tired, mentally and physically. Post-Workout Nutrition Goals Eating and drinking the appropriate nutrition after an intense workout is key to recovery. Post workout nutrition goals include: Replenishing glycogen stores: During long or intense workouts, the body burns carbohydrates that are stored in the muscle glycogen. Eating carbohydrates shortly after you exercise helps the body rebuild glycogen stores. Athletes should consume ½ gram of carbohydrates per pound of body weight, which is 75 grams for a pound athlete. Repairing damaged muscle: During exercise, muscle is broken down, and the foods consumed afterward can aid in tissue repair, as well as rebuilding and strengthening muscle. Eating grams of high-quality, lean protein after a workout will maximize protein synthesis to repair muscles and enhance muscle growth. When participating in tournament play or multiple workouts in a day which leave less than 2 hours to recover, athletes may want to forego eating protein until after completing the events or eat a smaller amount. Knowing how your body reacts in these circumstances will help you choose what works best for you. Rehydrating: Athletes can lose a large amount of electrolytes and fluid through sweating. For each pound of lost water, an athlete should consume ounces of liquid. Water is often sufficient, but sports drinks containing electrolytes and carbohydrates can help replenish what the body has used up during the workout, especially those lasting over 60 minutes. Staying well-hydrated in conjunction with exercise involves drinking fluids before, during, and after working out. To avoid dehydration, the American College of Sports Medicine recommends ounces of water hours prior to working out, ounces every minutes during workout, and ounces for every pound of lost fluid after workout. When to Eat for Recovery Because your muscles are thought to be most receptive to nutrients like carbohydrates and protein for about 30 minutes after a hard effort, you want to aim to begin recovery eating within this period. One serving size nutritional protein options include: ½ cup beans lean beef Low-fat string cheese 1 oz. skinless, white chicken meat ¼ cup cottage cheese 1 egg or 2 egg whites 1 oz. Meat-based diets have been shown to include additional overall health benefits. Some studies have found that meat, as a protein source, is associated with higher serum levels of IGF-1 [ ], which in turn is related to increased bone mineralization and fewer fractures [ ]. A highly debated topic in nutrition and epidemiology is whether vegetarian diets are a healthier choice than omnivorous diets. One key difference is the fact that vegetarian diets often lack equivalent amounts of protein when compared to omnivorous diets [ ]. However, with proper supplementation and careful nutritional choices, it is possible to have complete proteins in a vegetarian diet. Generally by consuming high-quality, animal-based products meat, milk, eggs, and cheese an individual will achieve optimal growth as compared to ingesting only plant proteins [ ]. Research has shown that soy is considered a lower quality complete protein. Hartman et al. They found that the participants that consumed the milk protein increased lean mass and decreased fat mass more than the control and soy groups. Moreover, the soy group was not significantly different from the control group. Similarly, a study by Tang and colleagues [ 86 ] directly compared the abilities of hydrolyzed whey isolate, soy isolate, and micellar casein to stimulate rates of MPS both at rest and in response to a single bout of lower body resistance training. These authors reported that the ability of soy to stimulate MPS was greater than casein, but less than whey, at rest and in response to an acute resistance exercise stimulus. While soy is considered a complete protein, it contains lower amounts of BCAAs than bovine milk [ ]. Additionally, research has found that dietary soy phytoestrogens inhibit mTOR expression in skeletal muscle through activation of AMPK [ ]. Thus, not only does soy contain lower amounts of the EAAs and leucine, but soy protein may also be responsible for inhibiting growth factors and protein synthesis via its negative regulation of mTOR. When considering the multitude of plant sources of protein, soy overwhelmingly has the most research. Limited evidence using wheat protein in older men has suggested that wheat protein stimulates significantly lower levels of MPS when compared to an identical dose 35 g of casein protein, but when this dose is increased nearly two fold 60 g this protein source is able to significantly increase rates of myofibrillar protein synthesis [ ]. As mentioned earlier, a study by Joy and colleagues [ 89 ] in which participants participated in resistance training program for eight weeks while taking identical, high doses of either rice or whey protein, demonstrated that rice protein stimulated similar increases in body composition adaptations to whey protein. The majority of available science has explored the efficacy of ingesting single protein sources, but evidence continues to mount that combining protein sources may afford additional benefits [ ]. For example, a week resistance training study by Kerksick and colleagues [ 22 ] demonstrated that a combination of whey 40 g and casein 8 g yielded the greatest increase in fat-free mass determined by DEXA when compared to both a combination of 40 g of whey, 5 g of glutamine, and 3 g of BCAAs and a placebo consisting of 48 g of a maltodextrin carbohydrate. Later, Kerksick et al. Similarly, Hartman and investigators [ 93 ] had 56 healthy young men train for 12 weeks while either ingesting isocaloric and isonitrogenous doses of fat-free milk a blend of whey and casein , soy protein or a carbohydrate placebo and concluded that fat-free milk stimulated the greatest increases in Type I and II muscle fiber area as well as fat-free mass; however, strength outcomes were not affected. Moreover, Wilkinson and colleagues [ 94 ] demonstrated that ingestion of fat-free milk vs. soy or carbohydrate led to a greater area under the curve for net balance of protein and that the fractional synthesis rate of muscle protein was greatest after milk ingestion. In , Reidy et al. However, when the entire four-hour measurement period was considered, no difference in MPS rates were found. A follow-up publication from the same clinical trial also reported that ingestion of the protein blend resulted in a positive and prolonged amino acid balance when compared to ingestion of whey protein alone, while post-exercise rates of myofibrillar protein synthesis were similar between the two conditions [ ]. Reidy et al. No differences were found between whey and the whey and soy blend. Some valid criteria exist to compare protein sources and provide an objective method of how to include them in a diet. As previously mentioned, common means of assessing protein quality include Biological Value, Protein Efficiency Ratio, PDCAAS and IAAO. The derivation of each technique is different with all having distinct advantages and disadvantages. For nearly all populations, ideal methods should be linked to the capacity of the protein to positively affect protein balance in the short term, and facilitate increases and decreases in lean and fat-mass, respectively, over the long term. To this point, dairy, egg, meat, and plant-based proteins have been discussed. As mentioned previously, initial research by Boirie and Dangin has highlighted the impact of protein digestion rate on net protein balance with the two milk proteins: whey and casein [ , , ]. Subsequent follow-up work has used this premise as a reference point for the digestion rates of other protein sources. Using the criteria of leucine content, Norton and Wilson et al. Wheat and soy did not stimulate MPS above fasted levels, whereas egg and whey proteins significantly increased MPS rates, with MPS for whey protein being greater than egg protein. MPS responses were closely related to changes in plasma leucine and phosphorylation of 4E—BP1 and S6 K protein signaling molecules. More importantly, following 2- and weeks of ingestion, it was demonstrated that the leucine content of the meals increased muscle mass and was inversely correlated with body fat. Tang et al. These findings lead us to conclude that athletes should seek protein sources that are both fast-digesting and high in leucine content to maximally stimulate rates of MPS at rest and following training. Moreover, in consideration of the various additional attributes that high-quality protein sources deliver, it may be advantageous to consume a combination of higher quality protein sources dairy, egg, and meat sources. Multiple protein sources are available for an athlete to consider, and each has their own advantages and disadvantages. Protein sources are commonly evaluated based upon the content of amino acids, particularly the EAAs, they provide. Blends of protein sources might afford a favorable combination of key nutrients such as leucine, EAAs, bioactive peptides, and antioxidants, but more research is needed to determine their ideal composition. Nutrient density is defined as the amount of a particular nutrient carbohydrate, protein, fat, etc. per unit of energy in a given food. In many situations, the commercial preparation method of foods can affect the actual nutrient density of the resulting food. When producing milk protein supplements, special preparations must be made to separate the protein sources from the lactose and fat calories in milk. For example, the addition of acid to milk causes the casein to coagulate or collect at the bottom, while the whey is left on the top [ ]. These proteins are then filtered to increase their purity. Filtration methods differ, and there are both benefits and disadvantages to each. Ion exchange exposes a given protein source, such as whey, to hydrochloric acid and sodium hydroxide, thereby producing an electric charge on the proteins that can be used to separate them from lactose and fat [ ]. The advantage of this method is that it is relatively cheap and produces the highest protein concentration [ ]. The disadvantage is that ion exchange filtration typically denatures some of the valuable immune-boosting, anti-carcinogenic peptides found in whey [ ]. Cross-flow microfiltration, and ultra-micro filtration are based on the premise that the molecular weight of whey protein is greater than lactose, and use 1 and 0. As a result, whey protein is trapped in the membranes but the lactose and other components pass through. The advantage is that these processes do not denature valuable proteins and peptides found in whey, so the protein itself is deemed to be of higher quality [ ]. The main disadvantage is that this filtration process is typically costlier than the ion exchange method. When consumed whole, proteins are digested through a series of steps beginning with homogenization by chewing, followed by partial digestion by pepsin in the stomach [ ]. Following this, a combination of peptides, proteins, and negligible amounts of single amino acids are released into the small intestine and from there are either partially hydrolyzed into oligopeptides, 2—8 amino acids in length or are fully hydrolyzed into individual amino acids [ ]. Absorption of individual amino acids and various small peptides di, tri, and tetra into the blood occurs inside the small intestine through separate transport mechanisms [ ]. Oftentimes, products contain proteins that have been pre-exposed to specific digestive enzymes causing hydrolysis of the proteins into di, tri, and tetrapeptides. A plethora of studies have investigated the effects of the degree of protein fractionation or degree of hydrolysis on the absorption of amino acids and the subsequent hormonal response [ , , , , , ]. Further, the rate of absorption may lead to a more favorable anabolic hormonal environment [ , , ]. Calbet et al. Each of the nitrogen containing solutions contained 15 g of glucose and 30 g of protein. Results indicated that peptide hydrolysates produced a faster increase in venous plasma amino acids compared to milk proteins. Further, the peptide hydrolysates produced peak plasma insulin levels that were two- and four-times greater than that evoked by the milk and glucose solutions, respectively, with a correlation of 0. In a more appropriate comparison, Morifuji et al. However, Calbet et al. The hydrolyzed casein, however, did result in a greater amino acid response than the nonhydrolyzed casein. Finally, both hydrolyzed groups resulted in greater gastric secretions, as well as greater plasma increases, in glucose-dependent insulinotropic polypeptides [ ]. Buckley and colleagues [ ] found that a ~ 30 g dose of a hydrolyzed whey protein isolate resulted in a more rapid recovery of muscle force-generating capacity following eccentric exercise, compared with a flavored water placebo or a non-hydrolyzed form of the same whey protein isolate. In agreement with these findings, Cooke et al. Three and seven days after completing the damaging exercise bout, maximal strength levels were higher in the hydrolyzed whey protein group compared to carbohydrate supplementation. Additionally, blood concentrations of muscle damage markers tended to be lower when four ~g doses of a hydrolyzed whey protein isolate were ingested for two weeks following the damaging bout. Beyond influencing strength recovery after damaging exercise, other benefits of hydrolyzed proteins have been suggested. For example, Morifuji et al. Furthermore, Lockwood et al. Results indicated that strength and lean body mass LBM increased equally in all groups. However, fat mass decreased only in the hydrolyzed whey protein group. While more work needs to be completed to fully determine the potential impact of hydrolyzed proteins on strength and body composition changes, this initial study suggests that hydrolyzed whey may be efficacious for decreasing body fat. Finally, Saunders et al. The authors reported that co-ingestion of a carbohydrate and protein hydrolysate improved time-trial performance late in the exercise protocol and significantly reduced soreness and markers of muscle damage. Two excellent reviews on the topic of hydrolyzed proteins and their impact on performance and recovery have been published by Van Loon et al. The prevalence of digestive enzymes in sports nutrition products has increased during recent years with many products now containing a combination of proteases and lipases, with the addition of carbohydrates in plant proteins. Proteases can hydrolyze proteins into various peptide configurations and potentially single amino acids. It appears that digestive enzyme capabilities and production decrease with age [ ], thus increasing the difficulty with which the body can break down and digest large meals. Digestive enzymes could potentially work to promote optimal digestion by allowing up-regulation of various metabolic enzymes that may be needed to allow for efficient bodily operation. Further, digestive enzymes have been shown to minimize quality differences between varying protein sources [ ]. Individuals looking to increase plasma peak amino acid concentrations may benefit from hydrolyzed protein sources or protein supplemented with digestive enzymes. However, more work is needed before definitive conclusions can be drawn regarding the efficacy of digestive enzymes. Despite a plethora of studies demonstrating safety, much concern still exists surrounding the clinical implications of consuming increased amounts of protein, particularly on renal and hepatic health. The majority of these concerns stem from renal failure patients and educational dogma that has not been rewritten as evidence mounts to the contrary. Certainly, it is clear that people in renal failure benefit from protein-restricted diets [ ], but extending this pathophysiology to otherwise healthy exercise-trained individuals who are not clinically compromised is inappropriate. Published reviews on this topic consistently report that an increased intake of protein by competitive athletes and active individuals provides no indication of hepato-renal harm or damage [ , ]. This is supported by a recent commentary [ ] which referenced recent reports from the World Health Organization [ ] where they indicated a lack of evidence linking a high protein diet to renal disease. Likewise, the panel charged with establishing reference nutrient values for Australia and New Zealand also stated there was no published evidence that elevated intakes of protein exerted any negative impact on kidney function in athletes or in general [ ]. Recently, Antonio and colleagues published a series of original investigations that prescribed extremely high amounts of protein ~3. The first study in had resistance-trained individuals consume an extremely high protein diet 4. A follow-up investigation [ ] required participants to ingest up to 3. Their next study employed a crossover study design in twelve healthy resistance-trained men in which each participant was tested before and after for body composition as well as blood-markers of health and performance [ ]. In one eight-week block, participants followed their normal habitual diet 2. No changes in body composition were reported, and importantly, no clinical side effects were observed throughout the study. Finally, the same group of authors published a one-year crossover study [ ] in fourteen healthy resistance-trained men. This investigation showed that the chronic consumption of a high protein diet i. Furthermore, there were no alterations in clinical markers of metabolism and blood lipids. Multiple review articles indicate that no controlled scientific evidence exists indicating that increased intakes of protein pose any health risks in healthy, exercising individuals. A series of controlled investigations spanning up to one year in duration utilizing protein intakes of up to 2. In alignment with our previous position stand, it is the position of the International Society of Sports Nutrition that the majority of exercising individuals should consume at minimum approximately 1. The amount is dependent upon the mode and intensity of the exercise, the quality of the protein ingested, as well as the energy and carbohydrate status of the individual. Concerns that protein intake within this range is unhealthy are unfounded in healthy, exercising individuals. An attempt should be made to consume whole foods that contain high-quality e. The timing of protein intake in the period encompassing the exercise session may offer several benefits including improved recovery and greater gains in lean body mass. In addition, consuming protein pre-sleep has been shown to increase overnight MPS and next-morning metabolism acutely along with improvements in muscle size and strength over 12 weeks of resistance training. Intact protein supplements, EAAs and leucine have been shown to be beneficial for the exercising individual by increasing the rates of MPS, decreasing muscle protein degradation, and possibly aiding in recovery from exercise. In summary, increasing protein intake using whole foods as well as high-quality supplemental protein sources can improve the adaptive response to training. Campbell B, Kreider RB, Ziegenfuss T, La Bounty P, Roberts M, Burke D, et al. International society of sports nutrition position stand: protein and exercise. J Int Soc Sports Nutr. Macdermid PW, Stannard SR. A whey-supplemented, high-protein diet versus a high-carbohydrate diet: effects on endurance cycling performance. Int J Sport Nutr Exerc Metab. Article CAS PubMed Google Scholar. Burke LM, Hawley JA, Wong SH, Jeukendrup AE. Carbohydrates for training and competition. J Sports Sci. Article PubMed Google Scholar. Witard OC, Jackman SR, Kies AK, Jeukendrup AE, Tipton KD. Effect of increased dietary protein on tolerance to intensified training. Med Sci Sports Exerc. D'lugos AC, Luden ND, Faller JM, Akers JD, Mckenzie AI, Saunders MJ. 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| What should you eat after working out? | More recent work has established that protein-carbohydrate supplementation after strenuous endurance exercise stimulates contractile MPS via similar signaling pathways as resistance exercise [ 56 , 57 ]. Update on maximal anabolic response to dietary protein. However, the stimulation of myofibrillar protein synthesis after resistance exercise is uninfluenced by the menstrual phase Camera DM, West DW, Burd NA, Phillips SM, Garnham AP, Hawley JA, et al. Balanced meal: Carbohydrate, protein, and fats. National Academy of Sports Medicine. Reactive oxygen species ROS and reactive nitrogen species RNS are free radicals that are produced during exercise that can cause skeletal muscle damage, fatigue, and impair recovery. |
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Myofibrillar and mitochondrial protein synthesis rates do not differ in young men following the ingestion of carbohydrate with milk protein, whey, or micellar casein after concurrent resistance- and endurance-type exercise. Roy BD, Fowles JR, Hill R, Tarnopolsky MA. Macronutrient intake and whole body protein metabolism following resistance exercise. Mazzulla M, Parel JT, Beals JW, Van VS, Abou Sawan S, West DWD, et al. Endurance exercise attenuates postprandial whole-body leucine balance in trained men. Kato H, Suzuki K, Bannai M, Moore DR. Branched-chain amino acids are the primary limiting amino acids in the diets of endurance-trained men after a bout of prolonged exercise. Protein requirements are elevated in endurance athletes after exercise as determined by the indicator amino acid oxidation method. Witard OC, Turner JE, Jackman SR, Kies AK, Jeukendrup AE, Bosch JA, et al. High dietary protein restores overreaching induced impairments in leukocyte trafficking and reduces the incidence of upper respiratory tract infection in elite cyclists. Brain Behav Immun. Williamson E, Kato H, Volterman KA, Suzuki K, Moore DR. The effect of dietary protein on protein metabolism and performance in endurance-trained males. Kumar V, Selby A, Rankin D, Patel R, Atherton P, Hildebrandt W, et al. Age-related differences in the dose-response relationship of muscle protein synthesis to resistance exercise in young and old men. Balagopal P, Schimke JC, Ades P, Adey D, Nair KS. Age effect on transcript levels and synthesis rate of muscle MHC and response to resistance exercise. Roth SM, Ivey FM, Martel GF, Lemmer JT, Hurlbut DE, Siegel EL, et al. Muscle size responses to strength training in young and older men and women. J Am Geriatr Soc. Drummond MJ, Dreyer HC, Pennings B, Fry CS, Dhanani S, Dillon EL, et al. Skeletal muscle protein anabolic response to resistance exercise and essential amino acids is delayed with aging. Yang Y, Breen L, Burd NA, Hector AJ, Churchward-Venne TA, Josse AR, et al. Resistance exercise enhances myofibrillar protein synthesis with graded intakes of whey protein in older men. Br J Nutr. Churchward-Venne TA, Holwerda AM, Phillips SM, van Loon LJ. What is the optimal amount of protein to support post-exercise skeletal muscle reconditioning in the older adult? Holwerda AM, Paulussen KJM, Overkamp M, Goessens JPB, Kramer IF, Wodzig W, et al. Dose-dependent increases in whole-body net protein balance and dietary protein-derived amino acid incorporation into myofibrillar protein during recovery from resistance exercise in older men. Burd NA, Wall BT, van Loon LJ. The curious case of anabolic resistance: old wives' tales or new fables? Moore DR. Adv Nutr. Churchward-Venne TA, Breen L, Di Donato DM, Hector AJ, Mitchell CJ, Moore DR, et al. Leucine supplementation of a low-protein mixed macronutrient beverage enhances myofibrillar protein synthesis in young men: a double-blind, randomized trial. Tang JE, Moore DR, Kujbida GW, Tarnopolsky MA, Phillips SM. Ingestion of whey hydrolysate, casein, or soy protein isolate: effects on mixed muscle protein synthesis at rest and following resistance exercise in young men. Chan AH, D'Souza RF, Beals JW, Zeng N, Prodhan U, Fanning AC, et al. The degree of aminoacidemia after dairy protein ingestion does not modulate the postexercise anabolic response in young men: a randomized controlled trial. Protein blend ingestion following resistance exercise promotes human muscle protein synthesis. Burke LM, Winter JA, Cameron-Smith D, Enslen M, Farnfield M, Decombaz J. Effect of intake of different dietary protein sources on plasma amino acid profiles at rest and after exercise. Burd NA, Gorissen SH, van Vliet S, Snijders T, van Loon LJ. Differences in postprandial protein handling after beef compared with milk ingestion during postexercise recovery: a randomized controlled trial. Elliot TA, Cree MG, Sanford AP, Wolfe RR, Tipton KD. Milk ingestion stimulates net muscle protein synthesis following resistance exercise. Abou Sawan S, van Vliet S, Parel JT, Beals JW, Mazzulla M, West DWD, et al. Translocation and protein complex co-localization of mTOR is associated with postprandial myofibrillar protein synthesis at rest and after endurance exercise. van Vliet S, Shy EL, Abou Sawan S, Beals JW, West DW, Skinner SK, et al. Consumption of whole eggs promotes greater stimulation of postexercise muscle protein synthesis than consumption of isonitrogenous amounts of egg whites in young men. Thomas DT, Erdman KA, Burke LM. American college of sports medicine joint position statement. nutrition and athletic performance. Protein requirements and supplementation in strength sports. Eat smart for sports. In: Academy of Nutrition and Dietetics Complete Food and Nutrition Guide. New York, N. Water and healthier drinks. Centers for Disease Control and Prevention. Accessed Aug. Miller M, et al. Sports nutrition. In: DeLee, Drez, and Miller's Orthopaedic Sports Medicine: Principles and Practice. Elsevier; Accessed July 29, Products and Services The Mayo Clinic Diet Online A Book: The Mayo Clinic Diet Bundle. See also Performance-enhancing drugs: Know the risks Daily water requirement. Mayo Clinic Press Check out these best-sellers and special offers on books and newsletters from Mayo Clinic Press. 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Degree Programs. Research Faculty. International Patients. Financial Services. Community Health Needs Assessment. Depending on your body weight, grams of protein every 3 to 4 hours is recommended 1. In addition, eating protein before exercise may decrease the amount you need to eat after without affecting recovery 1. One study found that eating protein pre-workout and post-workout has a similar effect on muscle strength, hypertrophy, and body composition changes The rate at which your glycogen stores are used depends on the activity. For example, endurance sports cause your body to use more glycogen than resistance training. For this reason, if you participate in endurance sports running, swimming, etc. Eating a high carb diet of 3. Furthermore, insulin secretion, which promotes glycogen synthesis, is better stimulated when carbs and protein are consumed at the same time 10 , 11 , 12 , Therefore, consuming carbs and protein after exercise can maximize protein and glycogen synthesis 13 , Early studies found benefits from consuming the two in a ratio of 3 to 1 carbs to protein. When rapid recovery is necessary under 4 hours , current recommendations suggest a similar ratio. Specifically, you can help restore glycogen faster by consuming 0. Recommendations for carb intake are targeted to the needs of endurance athletes. There is not enough evidence to say whether you should limit fat intake after a workout 1. Many people think that eating fat after a workout slows digestion and inhibits the absorption of nutrients. While fat might slow down the absorption of your post-workout meal, it may not reduce its benefits. For example, a study showed that whole milk was more effective at promoting muscle growth after a workout than skim milk Having some fat in your post-workout meal may not affect your recovery. But more studies are needed on this topic. A post-workout meal with protein and carbs will enhance glycogen storage and muscle protein synthesis. Consuming a ratio of 3 to 1 carbs to protein is a practical way to achieve this. However, more recent research has found that the post-exercise window to maximize the muscular response to eating protein is wider than initially thought, up to as many as several hours Also, recovery is not just about what you consume directly after working out. When you exercise consistently, the process is ongoing. It is best to continue to eat small, well-balanced meals of carbs and protein every 3—4 hours Eat your post-workout meal soon after exercising, ideally within a few hours. However, you can extend this period a little longer, depending on the timing of your pre-workout meal. Choosing easily digested foods will promote faster nutrient absorption. Combinations of the foods above can create great meals that give you all the nutrients you need after exercise. It is important to drink plenty of water before and after your workout. Being properly hydrated ensures the optimal internal environment for your body to maximize results. During exercise, you lose water and electrolytes through sweat. Replenishing these after a workout can help with recovery and performance Depending on the intensity of your workout, water or an electrolyte drink are recommended to replenish fluid losses. It is important to get water and electrolytes after exercise to replace what was lost during your workout. |
Wacker, die ideale Antwort.
Eben dass wir ohne Ihre ausgezeichnete Phrase machen würden
Welche rührende Wörter:)
Dieses Thema ist einfach unvergleichlich:), mir gefällt)))