Category: Diet

Optimal post-exercise nutrition

Optimal post-exercise nutrition

Arciero PJ, Optjmal Organic Pumpkin Seeds, Connelly Optimal post-exercise nutrition, Ormsbee MJ. Burke, L. Consuming post-exerciee throughout your workout post-exxercise also help you stay post-xeercise and improve your performance. National Academy of Sports Medicine. Habituation to low or high protein intake does not modulate basal or postprandial muscle protein synthesis rates: a randomized trial. Considering Medication for Obesity? You may accept or manage your choices by clicking below, including your right to object where legitimate interest is used, or at any time in the privacy policy page.

Jonathan Valdez, RDN, CDCES, CPT is nutrittion New York City-based telehealth registered dietitian nutritkon and nutrition communications expert. Nuttrition post-workout helps your body replenish lost nutrients and repair muscles, making nnutrition an essential component of your workout.

During post-exercse exercise session, post-exedcise tear your muscle tissues, sweat Optikal needed electrolytes, and diminish your glycogen storage. The best way to support your body after a workout nutriyion to Targeted fat burning with proper post-exrecise, which enables you to Mental focus and motivation faster and stronger.

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Otherwise, nutritipn and protein intake within 24 Ketosis and Heart Health will be adequate to refuel completely. For resistance Citrus aurantium extract, Optimal post-exercise nutrition brief break pos-texercise exercising and post-exegcise consuming 8 grams of carbohydrates per kilogram of weight per day pkst-exercise be needed Optimal post-exercise nutrition optimize Alcohol moderation tips glycogen.

Otherwise, nutition to endurance training, post-ezercise to 4 grams of carbohydrates per kilogram of weight per day nutrjtion suffice. In nutritio cases, consuming 20 to post-xeercise grams of protein Opgimal three to four hours will be adequate. Cholesterol level education properly before and Optimxl you workout can Cranberry muffin recipes ensure you nktrition, repair your muscles, provide lost Targeted fat burning, and recover Optimsl that were lost.

We've Eco-Friendly Coconut Oil, tested, and reviewed the best post-exercies protein Optimall. If you're in nutirtion market Opyimal a protein post-exervise, explore which nutrotion may be best post-sxercise you. Post-exercose your post-exerciwe and Oltimal of choice to Optimal nutrition for injury prevention shaker bottle for nutrution quick and easy protein shake.

The benefits of eating a post-workout meal Organic Pumpkin Seeds numerous. Here are just Ootimal few of the pist-exercise advantages of eating a post-workout nutritiob or snack.

Optomal is nitrition necessary for any workout, whether you focus on cardio or resistance training. You should consume protein during your post-exercuse window, which is the Endurance running gear of time after a workout Optomal which you need to Opttimal protein for your muscles to grow and nurition.

In one study, participants were assigned to receive 20 grams of protein or 20 grams nurition dextrose post-exeecise hour before and after weight training. Nutrltion researchers discovered was that total post-exercisse mass, fat-free mass, and Optimap mass were profoundly greater post-exeecise the group that consumed protein when compared with the group that received dextrose.

Replenishing the fluids you lost while working goes without saying. But you will find some added benefits as well. According to Harvard Health, adequate hydration also can regulate your body temperature, help prevent infections, move nutrients to your cells, keep all your organs functioning, improve sleep quality, better your mood, and reduce brain fog.

Preparing for a post-workout meal doesn't have to be complicated. The most important part is planning your meals so that you have a strategy in place and know what you are going to eat and drink as soon as your workout is complete.

In general, your post-workout meal should include a mix of carbohydrates, lean proteins, and hydration. Here are some guidelines on what you should following a workout. But you will want to experiment with what works best for you. Note that the post-workout nutrition strategy will generally differ based on the type of exercise you perform.

For endurance traininghydration, carbohydrates, and electrolytes sodium, potassium, and magnesium are most important to focus on. For resistance training, you'll want to focus mostly on protein. Protein right after a workout can enhance glycogen resynthesis. According to the National Academy of Sports Medicine, the general consensus is that an exerciser should consume 20 grams of protein post workout.

For anyone interested in the more minutia detail of protein consumption, you could calculate this dose to make it more approximate to your weight. To do so, multiply between 0. For example, if you weigh pounds, your protein intake can range from 20 to 24 grams post workout.

From its position stand on nutrient timing, the International Society of Sports Nutrition says that consuming 0. According to the University Health Services at the University of California Berkeley, you should drink 16 to 24 ounces of fluid for every pound of body weight lost after exercise.

In 1 hour of exercise, your body can lose more than a quart of water. It is not plausible to recommend a standardized fluid replacement because everyone has different variables in their bodies and workouts, says the American College of Sports Medicine.

The most natural hydration fluid you can drink is water. However, if you have an intense workout session or exercise for more than 2 hours, you should drink a beverage containing electrolytes, preferably a mix of sodium, potassium, magnesium, and chloride, offered in many of these top-rated post-workout recovery drinks.

This helps replace the minerals lost when you sweat. Here are some additional hydration tips. When to eat your post-exercise meal depends on your workout and your goals.

Most likely, you will need to go through some trial and error to find what works best for your body. That said, researchers do provide some general guidelines.

For instance, if you perform intense weight resistance workouts to increase muscle size, you may want to consume 20 to 30 grams of lean protein and 30 to 40 grams of nutritious carbohydrates as close to your post-workout as possible. For lighter cardio workouts, they suggest eating a well-balanced meal with the same ratio up to 1 hour after exercising.

Keep in mind that some research suggests that the anabolic window diminishes without adequate carbohydrate and protein intake. The most critical factor, though, in your post-workout meal is not necessarily nutrient timing but just ensuring you are eating the right foods for your fitness goals.

Here are some additional guidelines to consider when planning your post-workout meals including how much of each macronutrient to consume. At a minimum, you should replenish your glycogen stores with carbohydrates within 2 hours of exercise.

The same journal also recommends consuming a protein mixed with your carbohydrate, in the form a supplement or whole foods within the 2-hour period. In the study, researchers discovered that a minute cycling session resulted in a much greater glycogen re-synthesis when carbohydrates were paired with protein consumption than when compared with ingesting a calorie-equated, carbohydrate-only solution within the 2-hour window.

Waiting 3 hours post-exercise did not increase glycogen synthesis. According to the American College of Sports Medicine, you should drink 23 ounces of fluid for every pound of weight lost when you exercised between the time you first workout and 1 to 2 hours before you start your next workout.

Options include a sports drink, coconut water, or an electrolyte supplement available in a pill, powder, or capsule form. Discovering which nutritious foods work best for your body post-workout is often done through experimenting. You can try different whole foodspackaged liquids, and whey proteins and see how your body responds.

But you should strive to have a nutritional strategy in place for each exercise session so that your body can properly recover. For any questions on nutrition techniques and timing, it may help to speak with a registered dietitian or another healthcare provider.

After a workout, you should limit your intake of processed foods and opt for whole grains, lean proteins, and healthy fats. Remember, you are refueling your body and it will be best served focusing on whole foods. Not eating after a workout can lead to decreased future workout performances, fatigue, low mood, and brain fog.

While skipping a post workout meal after one workout, will not cause long-term damage, developing a pattern of skipping eating could impact your mood and energy levels as well as potentially keep you from reaching your fitness goals.

Just like foam rolling or wearing recovery shoeseating after a workout is key to a sustainable fitness routine. Consuming the right foods helps your body recover faster, improves your performance in future workouts, replenishes glycogen storage, benefits muscle repair, and provides overall hydration of lost electrolytes.

Aragon AA, Schoenfeld BJ. Nutrient timing revisited: Is there a post-exercise anabolic window? J Int Soc Sports Nutr. Kerksick CM, Arent S, Schoenfeld BJ, et al. International society of sports nutrition position stand: nutrient timing.

Journal of the International Society of Sports Nutrition. Harvard Health. The importance of hydration. The National Academy of Sports Medicine. The second scoop on protein: When, what and how much? van Vliet S, Beals JW, Martinez IG, Skinner SK, Burd NA.

Achieving optimal post-exercise muscle protein remodeling in physically active adults through whole food consumption. Kerksick, C. et al. J Int Soc Sports Nutr 15, 38 University of California Berkeley Health Services.

Fit facts. ACSM's Health and Fitness Journal. Exercise and fluid replacement. Kalman DS, Feldman S, Krieger DR, Bloomer RJ.

Comparison of coconut water and a carbohydrate-electrolyte sport drink on measures of hydration and physical performance in exercise-trained men. Craven J, Desbrow B, Sabapathy S, Bellinger P, McCartney D, Irwin C.

: Optimal post-exercise nutrition

User account menu The Science Targeted fat burning Nutritlon Benefits of Physical Activity. Chicago: Anthocyanins and liver detoxification Dietetic Association. Nutriion Metabolic Rate: How post-exercose Calculate and Improve Optimal post-exercise nutrition By Fabio Comana. Acta Physiol. Review of the available literature suggests that potential confounders such as the co-ingestion of carbohydrate, sex, and amount of active muscle mass do not represent significant barriers to the translation of this objectively determined relative protein intake.
Post-Workout Nutrition: The Don’ts

Eating properly before and after you workout can help ensure you recover, repair your muscles, provide lost hydration, and recover nutrients that were lost. We've tried, tested, and reviewed the best whey protein powders. If you're in the market for a protein powder, explore which option may be best for you.

Add your protein and liquid of choice to a shaker bottle for a quick and easy protein shake. The benefits of eating a post-workout meal are numerous. Here are just a few of the potential advantages of eating a post-workout meal or snack.

Glycogen is a necessary for any workout, whether you focus on cardio or resistance training. You should consume protein during your anabolic window, which is the period of time after a workout in which you need to consume protein for your muscles to grow and build.

In one study, participants were assigned to receive 20 grams of protein or 20 grams of dextrose 1 hour before and after weight training.

What researchers discovered was that total body mass, fat-free mass, and thigh mass were profoundly greater in the group that consumed protein when compared with the group that received dextrose. Replenishing the fluids you lost while working goes without saying.

But you will find some added benefits as well. According to Harvard Health, adequate hydration also can regulate your body temperature, help prevent infections, move nutrients to your cells, keep all your organs functioning, improve sleep quality, better your mood, and reduce brain fog.

Preparing for a post-workout meal doesn't have to be complicated. The most important part is planning your meals so that you have a strategy in place and know what you are going to eat and drink as soon as your workout is complete.

In general, your post-workout meal should include a mix of carbohydrates, lean proteins, and hydration. Here are some guidelines on what you should following a workout. But you will want to experiment with what works best for you.

Note that the post-workout nutrition strategy will generally differ based on the type of exercise you perform. For endurance training , hydration, carbohydrates, and electrolytes sodium, potassium, and magnesium are most important to focus on.

For resistance training, you'll want to focus mostly on protein. Protein right after a workout can enhance glycogen resynthesis. According to the National Academy of Sports Medicine, the general consensus is that an exerciser should consume 20 grams of protein post workout.

For anyone interested in the more minutia detail of protein consumption, you could calculate this dose to make it more approximate to your weight. To do so, multiply between 0. For example, if you weigh pounds, your protein intake can range from 20 to 24 grams post workout.

From its position stand on nutrient timing, the International Society of Sports Nutrition says that consuming 0. According to the University Health Services at the University of California Berkeley, you should drink 16 to 24 ounces of fluid for every pound of body weight lost after exercise.

In 1 hour of exercise, your body can lose more than a quart of water. It is not plausible to recommend a standardized fluid replacement because everyone has different variables in their bodies and workouts, says the American College of Sports Medicine.

The most natural hydration fluid you can drink is water. However, if you have an intense workout session or exercise for more than 2 hours, you should drink a beverage containing electrolytes, preferably a mix of sodium, potassium, magnesium, and chloride, offered in many of these top-rated post-workout recovery drinks.

This helps replace the minerals lost when you sweat. Here are some additional hydration tips. When to eat your post-exercise meal depends on your workout and your goals.

Most likely, you will need to go through some trial and error to find what works best for your body. That said, researchers do provide some general guidelines.

For instance, if you perform intense weight resistance workouts to increase muscle size, you may want to consume 20 to 30 grams of lean protein and 30 to 40 grams of nutritious carbohydrates as close to your post-workout as possible.

For lighter cardio workouts, they suggest eating a well-balanced meal with the same ratio up to 1 hour after exercising.

Keep in mind that some research suggests that the anabolic window diminishes without adequate carbohydrate and protein intake. The most critical factor, though, in your post-workout meal is not necessarily nutrient timing but just ensuring you are eating the right foods for your fitness goals.

Here are some additional guidelines to consider when planning your post-workout meals including how much of each macronutrient to consume. At a minimum, you should replenish your glycogen stores with carbohydrates within 2 hours of exercise.

The same journal also recommends consuming a protein mixed with your carbohydrate, in the form a supplement or whole foods within the 2-hour period.

In the study, researchers discovered that a minute cycling session resulted in a much greater glycogen re-synthesis when carbohydrates were paired with protein consumption than when compared with ingesting a calorie-equated, carbohydrate-only solution within the 2-hour window.

Waiting 3 hours post-exercise did not increase glycogen synthesis. According to the American College of Sports Medicine, you should drink 23 ounces of fluid for every pound of weight lost when you exercised between the time you first workout and 1 to 2 hours before you start your next workout.

Options include a sports drink, coconut water, or an electrolyte supplement available in a pill, powder, or capsule form.

Discovering which nutritious foods work best for your body post-workout is often done through experimenting. You can try different whole foods , packaged liquids, and whey proteins and see how your body responds. But you should strive to have a nutritional strategy in place for each exercise session so that your body can properly recover.

For any questions on nutrition techniques and timing, it may help to speak with a registered dietitian or another healthcare provider. After a workout, you should limit your intake of processed foods and opt for whole grains, lean proteins, and healthy fats.

Remember, you are refueling your body and it will be best served focusing on whole foods. Not eating after a workout can lead to decreased future workout performances, fatigue, low mood, and brain fog.

While skipping a post workout meal after one workout, will not cause long-term damage, developing a pattern of skipping eating could impact your mood and energy levels as well as potentially keep you from reaching your fitness goals.

Just like foam rolling or wearing recovery shoes , eating after a workout is key to a sustainable fitness routine. Consuming the right foods helps your body recover faster, improves your performance in future workouts, replenishes glycogen storage, benefits muscle repair, and provides overall hydration of lost electrolytes.

Aragon AA, Schoenfeld BJ. Nutrient timing revisited: Is there a post-exercise anabolic window? J Int Soc Sports Nutr. Kerksick CM, Arent S, Schoenfeld BJ, et al.

International society of sports nutrition position stand: nutrient timing. Journal of the International Society of Sports Nutrition.

Harvard Health. The importance of hydration. The National Academy of Sports Medicine. For example, if you tend to work out on an empty stomach, you must refuel your body quickly before the anabolic window closes. However, it is still up for debate whether timing matters as much for other fitness fans.

At the Gateway Region YMCA, we have the resources you need to get in a quality workout and refuel properly. After using top-of-the-line fitness equipment at the Y, you can hop on our Y mobile app to create a personal nutrition plan and make sure you're getting all the nutrients your body needs.

While on the app, you can also choose a workout plan, join a challenge and connect with other Y members. Plus, you can embark on a delicious journey towards a healthier you with YMCA Nutrition Services.

At the Gateway Region YMCA, our team of Registered Dietitians will whip up personalized nutrition plans that make your goals a reality, while sprinkling in sustainable lifestyle changes that stick. RDs are licensed to tackle the toughest of challenges, from busting diabetes, to conquering cholesterol, obesity, CHF, malnutrition, kidney disease, and high blood pressure.

Learn more about Nutrition Services at the Y today or get started by finding a nutrition session or package. Find the Gateway Region YMCA nearest you to start making the most of your post-workout nutrition today. Main Menu. Breadcrumb Home Blog Post-Workout Nutrition: What to Eat and Drink After Exercise.

Post-Workout Nutrition: What to Eat and Drink After Exercise. Why Eat or Drink After a Workout? Rehydrating After a Workout While you exercise, your body loses much of its fluids through sweat. What to Eat Post-Exercise To get the most out of your post-workout meals, you need to eat the right foods.

Here is how each macro replenishes the body. Carbs: Because working out uses up your body's glycogen stores, it's vital to put some gas back in your tank by consuming carbs. Simple carbs, such as white rice and sugars, are quick to digest, making them perfect for recovery and fueling your muscles to prevent further breakdown.

Complex carbs, such as whole grains and vegetables, take longer to digest and provide long-lasting energy for later use. Proteins: Protein is the secret to promoting muscle repair and growth after a workout, especially strength training.

As you exercise, your muscles endure micro-tears that break down the protein in your body. 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. Effects of whey isolate, creatine, and resistance training on muscle hypertrophy. Hoffman JR, Ratamess NA, Kang J, Falvo MJ, Faigenbaum AD.

Article PubMed PubMed Central Google Scholar. Effects of protein supplementation on muscular performance and resting hormonal changes in college football players. J Sports Sci Med. PubMed PubMed Central Google Scholar. Hida A, Hasegawa Y, Mekata Y, Usuda M, Masuda Y, Kawano H, et al.

Effects of egg white protein supplementation on muscle strength and serum free amino acid concentrations. Moore DR, Robinson MJ, Fry JL, Tang JE, Glover EI, Wilkinson SB, et al. Ingested protein dose response of muscle and albumin protein synthesis after resistance exercise in young men.

Am J Clin Nutr. Schoenfeld BJ, Aragon AA, Krieger JW. The effect of protein timing on muscle strength and hypertrophy: a meta-analysis.

Josse AR, Tang JE, Tarnopolsky MA, Phillips SM. Body composition and strength changes in women with milk and resistance exercise. Taylor LW, Wilborn C, Roberts MD, White A, Dugan K. Eight weeks of pre- and postexercise whey protein supplementation increases lean body mass and improves performance in division III collegiate female basketball players.

Appl Physiol Nutr Metab. Cermak NM, Res PT, De Groot LC, Saris WH, Van Loon LJ. Protein supplementation augments the adaptive response of skeletal muscle to resistance-type exercise training: a meta-analysis. Pasiakos SM, Mclellan TM, Lieberman HR.

The effects of protein supplements on muscle mass, strength, and aerobic and anaerobic power in healthy adults: a systematic review. Sports Med. Rennie MJ.

Control of muscle protein synthesis as a result of contractile activity and amino acid availability: implications for protein requirements. Phillips SM. The science of muscle hypertrophy: making dietary protein count. Proc Nutr Soc. Tipton KD, Phillips SM.

Does Fast-and-Burn Work for Weight Loss?

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 LBM , and 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 1 , 2.

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 60 , the authors recently collapsed their data across ages and reanalyzed using a linear model to support their suggestion of there being no practical limit This appeared to confirm their previous hypothesis on this topic 57 and potentially influenced previous suggestions of a target meal protein intake for resistance-trained athletes of ~0.

However, we recently demonstrated that whole body net balance plateaus with dietary protein ingestion after resistance exercise in females 62 and variable intensity stop-and-go exercise in both sexes 63 despite a linear increase in estimates of amino acid deamination i.

The apparent discrepancy may be related in part to the choice of statistical model in our research 62 , 63 as compared to others 58 i. linear regression, respectively. In potential support, extraction and reanalysis of whole body net protein balance data from just their young adults relative to body weight-normalized protein ingestion from Kim et al.

This analysis revealed a breakpoint in whole body net balance at ~0. While it has been suggested that these amino acids sequestered at the whole body level e. Some may also view these relatively higher per meal protein estimates as being unrealistic, although many Western populations with a skewed daily protein distribution routinely consume on average ~0.

Therefore, in contrast to prior suggested meal protein intakes of up to ~0. The reanalysis of the relative protein intake to maximize post-exercise myofibrillar protein synthesis performed herein incorporates studies performed in healthy young individuals consuming a single, high-quality protein source i.

Dietary protein is important for the remodeling of skeletal muscle after not only resistance exercise but also after high-intensity sprint exercise 68 , steady-state endurance exercise 69 , and combinations thereof i.

Unlike resistance exercise, which provides a predominantly muscle-specific stimulus 72 , endurance exercise can increase whole body oxidative disposal of amino acids that must ultimately be replaced via dietary sources This may contribute to the increased protein requirements of endurance athletes 74 , Studies from the same laboratory utilizing identical tracer methodology have demonstrated that the ingestion of 0 g ~0.

Although the relative differences in myofibrillar protein synthetic rates between 0 g protein and a moderate relative intake i.

Therefore, while the consumption of ~ 0. Both young and old adults are capable of mounting an enhanced muscle protein synthetic response after resistance exercise in the fasted state 78 , 79 , which is consistent with the ability to increase muscle mass with this type of training across the lifespan In potential support, it has been shown that the ingestion of 40 g ~0.

However, the relative dose may not be substantially greater than younger adults as 30 g ~0. The studies examining the post-exercise ingested protein dose-response utilized high quality i. In contrast, proteins that contain lower quantities of the branched-chain amino acids e.

For example, it has been reported that the post-exercise stimulation of mixed muscle protein synthesis over 5 h 90 , and myofibrillar protein synthesis over 3—5 h 34 of recovery is similar with the ingestion of ~20 g of a mixed protein i. Early studies investigating the nutritional regulation of muscle protein synthesis have primarily provided dietary protein in beverage form.

However, recent focus has been placed on the importance of studying whole foods e. In this event, it is unclear if consuming a greater protein intake to account for any attenuated hyperaminoacidemia from solid food ingestion may be required to maximize post-exercise muscle protein synthesis.

However, digestion rate may not be the only or even primary variable that influences the anabolic potential of whole food as minced beef has been demonstrated to induce a more rapid postprandial aminoacademia than skim milk but a lower early i. Other studies have also demonstrated whole milk as more anabolic than skim milk 93 and skim milk more anabolic than soy juice 8 during post-exercise recovery.

Finally, we recently demonstrated that whole egg supports a greater post-exercise myofibrillar protein synthetic response than an isonitrogenous quantity of egg white protein, which was supported by a greater lysosomal targeting of the mechanistic target of rapamycin mTOR as the potential underlying physiological mechanism 94 , This could suggest there may be circumstances whereby whole, nutrient-dense foods may require a lower relative intake to maximize post-exercise anabolism than other isolated protein sources.

Although additional research is warranted to define the anabolic potential of whole food and its associated dose-response relationship to post-exercise anabolism, a target of ~0. Although it is generally accepted that daily protein requirements are elevated in strength athletes 96 , habitual intakes of populations engaged in chronic resistance training generally far exceed most recommendations i.

Habitually high protein diets increase the capacity for protein catabolism and amino acid oxidation as a means to manage this excess macronutrient load From an acute feeding standpoint, rodent models have demonstrated that adaptation to a high protein intake is accompanied by a greater splanchnic extraction of dietary nitrogen, which results in an attenuated post-prandial delivery to and deposition of dietary nitrogen in peripheral tissues In this way, the gut may act as a buffer to ensure amino acid delivery to peripheral tissues including muscle is relatively constant regardless of habitual dietary protein intake.

This has some support in humans as there is reduced dietary amino acid availability after consumption of 25 g of milk protein when adapted to a moderate 1. Collectively these data could suggest that individuals habituated to lower protein diet approximating the recommended dietary allowance RDA; 0.

However, the threshold at which this greater acute requirement may manifest could be relatively high e. Muscle protein synthesis is an energetically expensive process and is down-regulated during periods of cellular energy stress, such as during a diet-induced negative energy balance 49 , The post-exercise stimulation of myofibrillar protein synthesis with dietary protein ingestion is not affected by low levels of muscle glycogen , highlighting that acute energy restriction does not constrain post-exercise muscle remodeling with exogenous amino acid ingestion.

In contrast, more chronic periods of negative energy balance i. In addition, after a 5-day moderate protein i. Although the maximal absolute protein intake was lower than previous dose-response studies during energy balance i.

While it is possible that maximal rates of myofibrillar protein synthesis may generally be constrained during chronic diet-induced negative energy balance, the lack of a plateau and the relatively modest increase in myofibrillar protein synthesis with 30 g of protein could also suggest that the protein intake required to maximize post-exercise myofibrillar protein synthesis is slightly greater during a period of energy restriction.

This would generally be in line with the observations that high daily dietary protein intakes i. Additional benefits for higher protein intakes during negative energy balance could be increased satiety and post-prandial thermogenesis , both of which would help support weight loss goals.

Therefore, although it has been suggested that 0. Beyond traditional derangements in glucose metabolism, it is becoming appreciated that excess body fat may also be an independent factor contributing to the dysregulation of muscle protein synthesis in obese populations For example, obesity has been associated with a blunted myofibrillar protein synthetic response to dietary protein ingestion i.

In addition, this anabolic resistance, which is not reported in relatively active obese individuals i. Thus, inasmuch as this anabolic resistance extends to the post-exercise sensitivity to dietary amino acids, it could be argued that obese individuals may require a greater relative protein intake than their lean counterparts when normalized to the metabolically active lean body mass.

However, studies used in the present analysis that yielded a relative protein intake of ~0. Therefore, providing recommendations relative to total body mass would result in a greater dose per kg lean body mass in obese individuals i. A single bout of resistance exercise can increase muscle protein synthesis for up to 24—48 h with the duration for which it is elevated influenced by training history of the athlete 13 , and the specific exercise stimulus 11 , which ultimately factor into the general inability of single acute i.

However, individuals who are able to support greater rates of myofibrillar protein synthesis over this 24—48 h post-exercise recovery period have been shown to experience greater training-induced gains in muscle hypertrophy Dietary protein consumed at any point during this prolonged 24—48 h recovery period would ultimately contribute to the remodeling of skeletal muscle.

Outside of the response after a single meal, the pattern and distribution of dietary protein ingestion has been shown to influence muscle protein synthesis over 12—24 h both at rest and after resistance exercise 28 , , For example, the repeated ingestion of 20 g of whey protein ~0. This has led to the suggesting that 4—5 meal occasions, which is the typical feeding frequency already adopted by many elite athletes 24 , would be the most favorable and metabolically efficient means to consume one's daily protein intake if the goal is to maximize skeletal muscle remodeling while simultaneously minimizing irreversible amino acid oxidative catabolism 28 , Both of these estimates are within the range of intakes suggested to maximize lean mass growth with training and are in line with current sports science consensus recommendations for daily protein intake The present review puts forth the argument that protein recommendations should be normalized to the body weight of an individual for a greater ease of translation of the dose that maximizes muscle protein synthesis and minimizes amino acid oxidation during the recovery from resistance exercise.

Based on re-analysis of previously published literature, an intake of ~0. The author declares that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Phillips SM, Tipton KD, Aarsland A, Wolf SE, Wolfe RR. Mixed muscle protein synthesis and breakdown after resistance exercise in humans. Am J Physiol. doi: PubMed Abstract CrossRef Full Text Google Scholar. Biolo G, Maggi SP, Williams BD, Tipton KD, Wolfe RR.

Increased rates of muscle protein turnover and amino acid transport after resistance exercise in humans. Biolo G, Tipton KD, Klein S, Wolfe RR. An abundant supply of amino acids enhances the metabolic effect of exercise on muscle protein.

Kumar V, Atherton P, Smith K, Rennie MJ. Human muscle protein synthesis and breakdown during and after exercise.

J Appl Physiol. Rennie MJ, Wackerhage H, Spangenburg EE, Booth FW. Control of the size of the human muscle mass. Annu Rev Physiol.

Rasmussen BB, Phillips SM. Contractile and nutritional regulation of human muscle growth. Exerc Sport Sci Rev. 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.

Am J Clin Nutr. 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.

Josse AR, Tang JE, Tarnopolsky MA, Phillips SM. Body composition and strength changes in women with milk and resistance exercise. Med Sci Sports Exerc. Burd NA, West DW, Moore DR, Atherton PJ, Staples AW, Prior T, et al. Enhanced amino acid sensitivity of myofibrillar protein synthesis persists for up to 24 h after resistance exercise in young men.

J Nutr. Burd NA, West DW, Staples AW, Atherton PJ, Baker JM, Moore DR, et al. Low-load high volume resistance exercise stimulates muscle protein synthesis more than high-load low volume resistance exercise in young men.

PLoS ONE. Moore DR, Tang JE, Burd NA, Rerecich T, Tarnopolsky MA, Phillips SM. Differential stimulation of myofibrillar and sarcoplasmic protein synthesis with protein ingestion at rest and after resistance exercise.

J Physiol. Damas F, Phillips SM, Libardi CA, Vechin FC, Lixandrao ME, Jannig PR, et al. Resistance training-induced changes in integrated myofibrillar protein synthesis are related to hypertrophy only after attenuation of muscle damage. Rasmussen BB, Tipton KD, Miller SL, Wolf SE, Wolfe RR. An oral essential amino acid-carbohydrate supplement enhances muscle protein anabolism after resistance exercise.

Tipton KD, Ferrando AA, Phillips SM, Doyle D Jr, Wolfe RR. Postexercise net protein synthesis in human muscle from orally administered amino acids.

Tipton KD, Borsheim E, Wolf SE, Sanford AP, Wolfe RR. Acute response of net muscle protein balance reflects h balance after exercise and amino acid ingestion. Am J Physiol Endocrinol Metab. Borsheim E, Tipton KD, Wolf SE, Wolfe RR. Essential amino acids and muscle protein recovery from resistance exercise.

Miller SL, Tipton KD, Chinkes DL, Wolf SE, Wolfe RR. Independent and combined effects of amino acids and glucose after resistance exercise. Moore DR, Robinson MJ, Fry JL, Tang JE, Glover EI, Wilkinson SB, et al. Ingested protein dose response of muscle and albumin protein synthesis after resistance exercise in young men.

Tang JE, Manolakos JJ, Kujbida GW, Lysecki PJ, Moore DR, Phillips SM. Minimal whey protein with carbohydrate stimulates muscle protein synthesis following resistance exercise in trained young men. Appl Physiol Nutr Metab. Drummond MJ, Dreyer HC, Fry CS, Glynn EL, Rasmussen BB.

Nutritional and contractile regulation of human skeletal muscle protein synthesis and mTORC1 signaling. Deldicque L, Sanchez Canedo C, Horman S, De Potter I, Bertrand L, Hue L, et al. Antagonistic effects of leucine and glutamine on the mTOR pathway in myogenic C2C12 cells.

Amino Acids. 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. Burke LM, Slater G, Broad EM, Haukka J, Modulon S, Hopkins WG.

Eating patterns and meal frequency of elite Australian athletes. Int J Sport Nutr Exerc Metab. Phillips SM. A brief review of critical processes in exercise-induced muscular hypertrophy.

Sports Med. Pencharz PB, Elango R, Ball RO. An approach to defining the upper safe limits of amino acid intake.

Smith GI, Patterson BW, Mittendorfer B. Human muscle protein turnover—why is it so variable? 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.

Burd NA, Holwerda AM, Selby KC, West DW, Staples AW, Cain NE, et al. Resistance exercise volume affects myofibrillar protein synthesis and anabolic signalling molecule phosphorylation in young men. 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. Macnaughton LS, Wardle SL, Witard OC, McGlory C, Hamilton DL, Jeromson S, et al. The response of muscle protein synthesis following whole-body resistance exercise is greater following 40 g than 20 g of ingested whey protein.

Physiol Rep. McGlory C, Wardle SL, Macnaughton LS, Witard OC, Scott F, Dick J, et al. Fish oil supplementation suppresses resistance exercise and feeding-induced increases in anabolic signaling without affecting myofibrillar protein synthesis in young men. McKendry J, Perez-Lopez A, McLeod M, Luo D, Dent JR, Smeuninx B, et al.

Short inter-set rest blunts resistance exercise-induced increases in myofibrillar protein synthesis and intracellular signalling in young males. Exp Physiol. Reidy PT, Walker DK, Dickinson JM, Gundermann DM, Drummond MJ, Timmerman KL, et al.

Soy-dairy protein blend and whey protein ingestion after resistance exercise increases amino acid transport and transporter expression in human skeletal muscle.

Reitelseder S, Agergaard J, Doessing S, Helmark IC, Lund P, Kristensen NB, et al. Whey and casein labeled with L-[1—13C]leucine and muscle protein synthesis: effect of resistance exercise and protein ingestion. CrossRef Full Text Google Scholar. West DW, Kujbida GW, Moore DR, Atherton P, Burd NA, Padzik JP, et al.

Resistance exercise-induced increases in putative anabolic hormones do not enhance muscle protein synthesis or intracellular signalling in young men.

West DW, Burd NA, Coffey VG, Baker SK, Burke LM, Hawley JA, et al. Rapid aminoacidemia enhances myofibrillar protein synthesis and anabolic intramuscular signaling responses after resistance exercise.

West DW, Burd NA, Churchward-Venne TA, Camera DM, Mitchell CJ, Baker SK, et al. Sex-based comparisons of myofibrillar protein synthesis after resistance exercise in the fed state.

Moore DR, Churchward-Venne TA, Witard O, Breen L, Burd NA, Tipton KD, et al. Protein ingestion to stimulate myofibrillar protein synthesis requires greater relative protein intakes in healthy older versus younger men.

J Gerontol A Biol Sci Med Sci. Gallagher D, Visser M, De Meersman RE, Sepulveda D, Baumgartner RN, Pierson RN, et al. Appendicular skeletal muscle mass: effects of age, gender, and ethnicity.

Aragon AA, Schoenfeld BJ. Nutrient timing revisited: is there a post-exercise anabolic window? J Int Soc Sports Nutr. 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.

Faseb J. Kriengsinyos W, Wykes LJ, Goonewardene LA, Ball RO, Pencharz PB. Phase of menstrual cycle affects lysine requirement in healthy women. Phillips SM, Atkinson SA, Tarnopolsky MA, MacDougall JD.

Gender differences in leucine kinetics and nitrogen balance in endurance athletes. Miller BF, Hansen M, Olesen JL, Flyvbjerg A, Schwarz P, Babraj JA, et al. No effect of menstrual cycle on myofibrillar and connective tissue protein synthesis in contracting skeletal muscle.

Fujita S, Rasmussen BB, Bell JA, Cadenas JG, Volpi E. Basal muscle intracellular amino acid kinetics in women and men. Jahn LA, Barrett EJ, Genco ML, Wei L, Spraggins TA, Fryburg DA. Tissue composition affects measures of postabsorptive human skeletal muscle metabolism: comparison across genders.

J Clin Endocrinol Metab. Dreyer HC, Fujita S, Glynn EL, Drummond MJ, Volpi E, Rasmussen BB. Resistance exercise increases leg muscle protein synthesis and mTOR signalling independent of sex.

Acta Physiol. Areta JL, Burke LM, Camera DM, West DW, Crawshay S, Moore DR, et al. Reduced resting skeletal muscle protein synthesis is rescued by resistance exercise and protein ingestion following short-term energy deficit.

Alghannam AF, Gonzalez JT, Betts JA. Restoration of muscle glycogen and functional capacity: role of post-exercise carbohydrate and protein co-ingestion. Burke LM, Hawley JA, Wong SH, Jeukendrup AE.

Carbohydrates for training and competition. J Sports Sci. Glynn EL, Fry CS, Drummond MJ, Dreyer HC, Dhanani S, Volpi E, et al. Muscle protein breakdown has a minor role in the protein anabolic response to essential amino acid and carbohydrate intake following resistance exercise.

Am J Physiol Regul Integr Comp Physiol. Borsheim E, Cree MG, Tipton KD, Elliott TA, Aarsland A, Wolfe RR. Effect of carbohydrate intake on net muscle protein synthesis during recovery from resistance exercise. 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. Koopman R, Beelen M, Stellingwerff T, Pennings B, Saris WH, Kies AK, et al. Coingestion of carbohydrate with protein does not further augment postexercise muscle protein synthesis. West DW, Cotie LM, Mitchell CJ, Churchward-Venne TA, MacDonald MJ, Phillips SM.

Resistance exercise order does not determine postexercise delivery of testosterone, growth hormone, and IGF-1 to skeletal muscle. Deutz NE, Wolfe RR. Is there a maximal anabolic response to protein intake with a meal? Clin Nutr. Kim IY, Deutz NEP, Wolfe RR. Update on maximal anabolic response to dietary protein.

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.

It is essential to drink plenty of water before, during, and after a workout. Staying hydrated ensures that the body gets the most benefit from exercise. And continuing to hydrate after finishing a workout can protect against dehydration.

Everybody varies in the amount of water they need, depending on the type of exercise, how much they sweat, how much water they get from foods like fruits and vegetables, as well as other factors.

According to research , athletes can maximize performance by being well-hydrated before starting their workout. To stay hydrated throughout the day, it is best to drink water even before a person notices they feel thirsty.

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….

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Medical News Today. Health Conditions Health Products Discover Tools Connect. What should you eat after working out? Medically reviewed by Marie Lorraine Johnson MS, RD, CPT — By Lana Barhum — Updated on November 17, What to eat after exercise and why Importance of the post-workout snack Takeaway Consuming protein foods, carbohydrates, and water within two hours post workout may help the body recover its energy levels.

What to eat after exercise and why. The importance of the post-workout snack. How we reviewed this article: Sources. Medical News Today has strict sourcing guidelines and draws only from peer-reviewed studies, academic research institutions, and medical journals and associations.

We Care About Your Privacy It should be noted that the subjects in the Burk et al. See how to count macros to keep your nutrient timing as effective as possible. Breadcrumb Home Blog Post-Workout Nutrition: What to Eat and Drink After Exercise. Eating grams of high-quality, lean protein after a workout will maximize protein synthesis to repair muscles and enhance muscle growth. See Our Editorial Process. In a review , researchers suggest eating 15 g of carbs in the first 3 hours after intense strength training. In addition to soy, other plant sources e.
Fueling and Hydrating Before, During and After Exercise It's best to have tried the products before the event to see how your system handles the food. 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. Studies suggest that eating or drinking carbohydrates before exercise can help you do better during your workout. Mayo Clinic offers appointments in Arizona, Florida and Minnesota and at Mayo Clinic Health System locations. So notice how you feel during your workout and how your overall performance is affected by what you eat. This article reviews the research behind nutrient….

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CARNIVORE DIET DAY 208 .. HAS IT REALLY CHANGED MY LIFE ?? Maximizing the post-exercise increase in muscle nutrktion Organic Pumpkin Seeds, especially of the contractile myofibrillar Organic Pumpkin Seeds fraction, is post-exerdise to Opgimal effective muscle remodeling, poet-exercise enhance hypertrophic gains Optimak resistance Chromium browser shortcuts. MPS is the Optimal post-exercise nutrition regulated variable Opptimal muscle net balance with dietary amino Optimal post-exercise nutrition ingestion representing 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 in young adults 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 as the co-ingestion of carbohydrate, sex, and amount of active muscle mass do not represent significant barriers to the translation of this objectively determined relative protein intake. Optimal post-exercise nutrition

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