When Is the Best Time to Take Protein?

The best time to take protein supplements depends on your activity level, your personal goals, and the types of workouts you engage in. This article will provide you with specific, scientifically backed recommendations, and the reasoning behind that advice.

When taking protein supplements, people often wonder when exactly is the best time of day to consume them. Pre-workout? Post-workout? Is it okay to drink a protein shake before bed? Protein supplements can help people lose weight, build muscle, and recover from tissue damage due to injury or surgery. Because they’re so effective, most people want to be sure they’re utilizing protein the right way. So when is the best time to take protein? Short answer is: that depends on your health goals and the kinds of workouts you’re doing. For the longer answer and more detail, read on.

The Different Types of Protein Supplements

Protein is a source of energy for the body, essential for muscle growth, repairing damaged tissue, and preventing certain infections and diseases. Normal dietary protein comes from foods like meats, eggs, fish, dairy, grains, legumes, and seeds. Though animal products contain the most amount of protein, vegetables are sources of protein too, a fact well-known by those living a vegetarian or vegan lifestyle. Of the most popular protein powders on the market in fact, a significant portion are plant-based.

Plant-based proteins include:

  • Soy protein containing all nine essential amino acids.
  • Rice protein, which is lower in the essential amino acid lysine.
  • Pea protein, which has lower levels of the essential amino acid methionine and nonessential amino acid cysteine.
  • Hemp protein, which is low in lysine but high in fiber, and omega-3 and omega-6 fatty acids, both of which are essential, meaning your body can’t make them on its own, and needs to gain them from the foods you eat.

Dairy-based proteins include:

  • Whey protein, which is absorbed relatively quickly and contains all nine essential amino acids.
  • Casein protein from milk curds, also containing the essential amino acids, and with a slower digestion rate than whey (which is why people often take casein before they sleep, so it will digest throughout the night… more on that timing below).

Animal-based proteins include:

  • Egg protein powder made from pure egg white protein.
  • Creatine, which is not found in plants but can be synthetically created. Though it is an animal protein, depending on its origin source, it may nevertheless be possible for vegans to use creatine as a supplement.

These are among the most commonly known protein powders available to buy, but we here at the Amino Co. have also developed an essential amino acid (EAA) blend that isn’t lacking or low on any of the amino acids required for protein synthesis and new muscle growth. It also blends free-form amino acids with whey protein and creatine, a nonessential protein that nevertheless has great value as a supplement. These forms of protein are used to help those who want to build muscle rapidly, and can even benefit those with muscle, neurological, or neuromuscular diseases.

The Varied Uses of Protein Supplementation

From muscle building to weight loss, here’s a quick look at all that supplemental protein can do to benefit your body.

Exercise Performance and Recovery

Added protein has been shown to increase endurance during training and workouts, as well as reduce soreness and speed up post-workout recovery. The timing of your protein intake matters here, whether you’re eating high-protein foods or taking supplements. Read on to learn about workout-specific timing recommendations.

Muscle Building

Muscles can only be built when you have the proper amount of amino acids for protein synthesis, and when you’re consuming more protein than your body breaks down during workouts. Taking a protein supplement, especially one that contains all the necessary EAAs for muscle growth, can make a huge difference. Finding the right anabolic window, the period of time when the protein you take in will go directly to your muscles, is something the International Society of Sports Nutrition has done extensive research on, and we, too, will provide specific scientific reasoning below.

Muscle Loss Prevention

Muscle mass is lost not only during intensive workouts, but also naturally as we age. Each decade you live after the age of 30 brings with it a higher risk of losing muscle (anywhere between 3-8% per decade). Proper protein intake is not only valuable to athletes, bodybuilders, and anyone who works out regularly, but it’s also important for each and every one of us as we age. Most Americans reserve their protein more for dinner than breakfast (3 times the amount on average is the difference between the two meals), and could use a supplemental boost of protein first thing in the morning to shore up their protein stores and help prevent the loss of muscle mass due to aging.

Fat Loss Facilitation

Protein is filling enough to help curb hunger pangs and chemically contributes to appetite suppression by reducing the “hunger hormone” ghrelin. A high-protein diet raises your metabolism and increases levels of appetite-reducing hormones like peptide YY (PYY) and glucagon-like peptide-1 (GLP-1). More satiety means fewer calories consumed throughout the day, which quickly leads to safe, maintainable weight loss and the reduction of dangerous body fat.

The Enduring Power of Protein

Popular because they’re convenient and effective, protein powders and supplements are here to stay and can offer you a wide variety of options, from self-mix formulas and powders to ready-to-drink protein shakes. If you’ve got your preferred protein supplement ready to go, then it’s time to wonder: when should you drink protein?

The Best Time to Take Protein Depending on Your Workout

Depending on your goals and activities, there are recommended times to take protein for the greatest effectiveness for your energy levels and muscle-building needs. Here are specific recommendations based on different types of workout activity.

The best time to take protein supplements.

Aerobic/Cardiovascular Exercise

Best time to take protein: Pre-workout and post-workout

The amino acid leucine is one of the three branched-chain amino acids (BCAAs), and it promotes muscle recovery after workouts. Not only that, it activates protein synthesis, prompting new muscle to be built. One might think that due to leucine’s ability to boost endurance and stamina, one should take a BCAA supplement before a workout, but the science contradicts that idea. Not only are BCAAs only three of the nine essential amino acids needed to construct new muscle, leucine and the other BCAAs (isoleucine and valine) experience oxidative degradation during aerobic activity.

BCAAs are Insufficient Pre-Workout

Adding these limited amino acids before your workout, especially in the unbalanced form of BCAAs instead of a complete EAA formula, means that a greater percentage will be oxidized and used for energy instead of muscle building. Your body does not want to be out of balance, so a sudden overabundance of a few amino acids will cause the body to clean up and reduce them in order to maintain equilibrium.

Rather than risk burning off the protein you put in because your body is only looking for energy sources, it’s better to take a full measure of EAAs within the hour after your aerobic workout, when your body is looking for supplies to rebuild. Leucine will be there to prompt muscle protein synthesis, and the rest of the essential amino acids will all be included in the ideal ratio for generating new muscle growth.

EAAs are Effective Pre- and Post-Workout

That being said, taking a complete amino acid protein supplement before an aerobic cardiovascular workout (like a high-intensity interval training or HIIT class), not only provides the necessary ingredients for muscle building, but also helps fight fatigue in a way that only taking BCAAs can’t, by fueling your body with the amino acids that help produce dopamine and serotonin in the brain.

Whether you’re walking, cycling, running stairs, or jumping rope, start by taking your EAA supplement 30 minutes before your workout session. The biggest benefit comes when you take your EAA supplement within an hour after your workout, when your blood flow is strong and active. Not only will the amino acids rush in to replace damaged muscle fibers with new muscle, EAAs can also help calm unnecessary inflammation. That will help quicken your recovery, allowing you to feel only the good side effects of working out, like increased energy and light euphoria, instead of soreness and fatigue.

Resistance Exercise

Best time to take protein: Pre-workout, during, and post-workout

Research has shown that EAAs given 30 minutes before a resistance exercise workout prompt muscle protein synthesis much more effectively than consuming EAAs afterwards does. Taking a protein supplement before this type of workout helps prevent the breakdown of muscle protein during the activity, and also increases blood flow to the muscles, thus getting the amino acids quickly into the muscle where they’re needed.

Consuming EAAs after a resistance workout is not harmful by any means, as that method, too, will prompt the stimulation of muscle protein synthesis, but it’s not ideal to leave the consumption of EAAs until after your resistance training is complete. Our recommendation is to first and foremost take a complete protein supplement before a resistance workout, and if possible take them throughout and/or after as well to get the most benefit.

Bodybuilding

Best time to take protein: Pre- and post-workout, and also before bed.

Immediately before and after a weight-lifting workout, we recommend that you take 15 grams of EAAs each. An EAA supplement has been shown to have a faster effect on muscle protein synthesis than either whey or casein protein alone. However, our Amino Co. blend of free-form EAAs with whey and creatine support ensures that you get a fast dose of EAAs and that the EAAs from whey will digest more slowly as you work out, offering a steady supply to help prevent muscle breakdown. Creatine helps prevent catabolism by supplying faster energy than your body can naturally generate from muscle cell mitochondria. This means more energy for more reps, which ultimately means more work put in and more muscle gained.

An hour after your post-workout dose of EAAs, we recommend another 15-gram dose. On off days, continue taking these same doses, measured between meals instead of surrounding your workout. Lastly, it’s also recommended you take another 15-gram dose before bed to keep your muscles fed as you sleep and to help prevent muscle breakdown as much as possible. You work hard to gain your muscles, and we encourage you to protect those gains at every opportunity. Set your alarm to take one more dose around 4 am if you know you won’t have a problem falling back to sleep, that way your muscles never go hungry for fuel.

It should be noted here that bodybuilders aren’t the only ones who benefit from taking extra protein before bed. One study of 16 elderly men showed that those who consumed casein protein (which digests slowly) before bed had increased muscle growth over those who took a placebo, despite being less active individuals. When you’re sleeping, it’s the protein that counts, and not the activity.

Is There Any Downside to Taking Protein Supplements?

The majority of scientific studies into how our bodies process high amounts of protein show that you can safely consume plenty of protein without risk of harmful side effects. Unless your doctor advises against protein supplements or you have a known kidney issue like rhabdomyolysis, there is no need to worry about excessive protein intake; merely take your products as recommended and spread them throughout your day.

Timing Is Everything

At the end of the day, it’s true that people who work out need more protein, but even those with a less active lifestyle benefit from consuming extra protein for strength, for maintaining healthy weight levels, and for preventing the loss of muscle mass we all experience as we age.

Make a protein shake for breakfast, have another to curb your appetite between meals, and make another as a beneficial treat before bed. Know that the more regularly you take in balanced forms of protein like Amino Co.’s complete EAA blend, the more good you can do for your body. Whether you’re working out or not, upping your daily protein intake is safe and smart. Bulk up, slim down, and stay strong with protein!

What Are Nonpolar Amino Acids?

What are nonpolar amino acids? This article will help explain how these amino acids are designated and what purpose they serve in the body.

Of the 20 common amino acids in the human body that build protein structures, 9 of them are essential (meaning we must eat or otherwise consume them to get them), and half of them are nonpolar. What are nonpolar amino acids? Which are they, and what does “nonpolar” mean? The review of the topic in this article will help explain.

The Definition of a Nonpolar Molecule

The nonpolar molecules we’ll be talking about are hydrophobic amino acids, meaning “water fearing” because they don’t mix with water molecules. You know how oil and water don’t mix? That’s because oil is hydrophobic.

The opposite of a nonpolar molecule is, as you might guess, polar. Polar molecules are hydrophilic, meaning “water loving.” If you’d like to visualize: polar molecules are like puppy dogs who love water so much that they’ll go barreling straight into muddy or smelly water after a tennis ball, with no hesitation at all. That would make nonpolar molecules like cats, better known for avoiding water, no thank you, and cleaning themselves without it.

Molecules are classified this way based on the charges on the atoms bonded together to form the molecule. If you remember your first taste of high school chemistry, you may remember that atoms have a nucleus of neutral neutrons and positive protons in the middle, and negative electrons swirling all around. Protons have a positive charge that draws electrons to it, like how opposites attract.

When two atoms bond together, they share electrons. Two atoms of the same element have equal positivity, so don’t have the power to steal electrons from the other. These molecules are nonpolar because they have no resulting charge. When atoms of two different elements connect together, invariably one of them will have the higher charge and attract the most electrons to its end of the joint molecule. That means the molecule is polar, or charged, and that charge will then be identified as either a positive or negative charge.

Examples of Nonpolar Molecules

Methane gas is an example of a nonpolar molecule that is created during the breakdown of food and released as a gas (or more colloquially, a fart). Methane is made up of one carbon atom that is bound to four hydrogen atoms: this hydrogen bonding allows the atoms to all share electrons equally, so this smelly molecule has no charge and is nonpolar.

Inside our body, we have both polar and nonpolar molecules, which includes those 20 amino acids mentioned above.

Nonpolar Amino Acids

The chemical properties of amino acids are largely determined by one group of molecules, what’s known as the R group: a side chain that differs on each amino acid. To visualize the amino acid groups, picture a pizza with four toppings, and a little support table in the middle that’s there to keep the cheese from sticking to the lid. That table is the alpha carbon to which all the groups or toppings are attached.

Every amino acid has three groups/toppings in common: the amino group (-NH2), the carboxyl group (COOH), and a hydrogen atom, which in pizza terms would be three standard toppings, say pepperoni, sausage, and cheese (cheese is hydrogen, which is just one atom and not a group of them, and so it gets the plainest topping). That fourth quarter of the pizza? That is the R group, the functional group that identifies and characterizes different amino acids—when you think of the R group, think R for Radical, because that is a completely different and unique topping, and every R group amino acid side chain has a distinct flavor of its own. To get up to 20 it would have to be pineapple, spinach, olives, Canadian bacon, jalapeño, garlic, anchovies, bell pepper, salami, feta cheese, beef, oregano, bacon, barbecue sauce, chicken, pesto, chorizo, broccoli, eggplant, and mushroom. Some are weirder than others.

The nonpolar amino acids have R groups mostly made up of hydrocarbons, though the amino acids methionine and cysteine also each feature a sulphur atom. The nonpolar amino acids are as follows, with more information on each one.

Glycine

  • Three letter code: gly
  • One letter code: G

The body needs glycine to make compounds like as glutathione, creatine, and collagen, which is the most abundant protein in your body. Collagen is a vital part of your muscles, blood, skin, cartilage, ligaments, and bones. Glycine may also protect your liver from alcohol damage, contribute to heart health, and improve your sleep quality. Glycine might also protect those with type 2 diabetes from muscle-wasting. You can gain more glycine by eating certain meat products or by taking a collagen supplement.

Alanine

  • Three letter code: ala
  • One letter code: A

Alanine is an amino acid that helps convert glucose into energy and helps eliminate excess toxins from your liver. Alanine keeps muscle protein from being cannibalized by the body during intense aerobic exercise or activity, and it’s needed to balance nitrogen and glucose levels in the body, which it does via the alanine cycle.

Alanine is a nonessential amino acid, which means that usually your body can make the substance on its own and doesn’t need you to ingest it from outside. However, people with eating disorders, extremely low-protein diets, diabetes, liver disease, or certain genetic conditions that cause UCDs (urea cycle disorders), may need to take a supplement or adjust their diet to gain this amino acid.

Good sources of alanine are meat, fish, poultry, eggs, and dairy products, as well as some protein-rich plant foods, like avocado. There are supplements containing alanine on the market, however, taking any one amino acid alone could upset the balance of nitrogen in the body, putting stress on the liver and kidneys as they try to eliminate waste. It is advisable that those with liver or kidney disease should consult a trusted medical professional before taking any amino acid supplement.

Proline

  • Three letter code: pro
  • One letter code: P

Proline is needed for the manufacture of cartilage and collagen, which helps heal cartilage and cushion our joints and vertebrae. It keeps joints flexible, and skin supple when it is affected by sun damage or signs of normal aging. Proline breaks down proteins for cell creation, and is essential at sites of injury where the tissue must be rebuilt to heal. Proline supplementation is sometimes valuable to people with chronic back pain or osteoarthritis.

Proline is also needed for the maintenance of muscle tissue, and is sometimes found low in long-distance runners and other serious athletes. Proline is usually nonessential, as the body naturally derives proline from its supplies of glutamic acid. However, if necessary, proline can be found in natural sources like dairy, meat, and eggs, or can be gained from amino acid supplementation.

Valine

  • Three letter code: val
  • One letter code: V

Valine is a branched-chain amino acid (BCAA) that works with the other two BCAAs (isoleucine and leucine) to regulate blood sugar, repair tissues, and provide the body with energy. Valine assists in stimulating the central nervous system and is necessary for mental functioning. Valine helps provide muscles with extra glucose energy during intense physical activity, which prevents muscle breakdown, and helps remove toxic excess nitrogen from the liver. Valine may help the liver and gallbladder recover from damage due to alcoholism or drug abuse, as well as help possibly reverse alcohol-related brain damage, or hepatic encephalopathy.

Valine is an essential amino acid, and must be obtained through a diet including meats, mushrooms, dairy products, peanuts, and/or soy protein. Most people have no problem getting enough valine, however maple syrup urine disease or MSUD is caused by an inability to metabolize leucine, isoleucine, and valine. Supplementation is sometimes warranted in those with low-protein diets or who are trying to build muscle mass, but be advised that too much valine intake will make one’s skin feel like it is crawling, and may cause hallucinations. Supplements should always be taken responsibly.

Leucine

  • Three letter code: leu
  • One letter code: L

Leucine helps with blood sugar regulation, muscle repair, and energy production. It also helps burn fat located deep inside the body that is hard to reach through diet and exercise alone.

Leucine is a branched-chain amino acid (BCAA) along with valine and isoleucine, all of which help to promote post-exercise muscle recovery, leucine being particularly effective, as it converts to glucose the fastest of the three. That is also why leucine is closely linked with the regulation of blood sugar, and why a leucine deficiency causes symptoms like hypoglycemia: headaches, fatigue, dizziness, confusion, depression, and irritability.

Leucine promotes the recovery of skin, bones, and muscle tissue after injury or surgery. Natural sources of this essential amino acid are meat, nuts, soy flour, brown rice, beans, and whole wheat.

Isoleucine

  • Three letter code: ile
  • One letter code: I

An isolated form of leucine, isoleucine is prized by bodybuilders for its ability to increase endurance, help repair muscle tissue, and encourage clotting at sites of injury. Isoleucine is broken down for energy inside muscle tissue, and helps stabilize energy levels by aiding in blood sugar regulation. An isoleucine deficiency also produces symptoms that mimic hypoglycemia.

Isoleucine is an essential amino acid, and food sources include high-protein options like nuts, peas, lentils, seeds, meat, eggs, fish, and soy protein.

Methionine

  • Three letter code: met
  • One letter code: M

An essential amino acid that helps the body process and eliminate fat, methionine contains sulfur, a substance required for the production of the body’s natural antioxidant, glutathione. The body also needs methionine to produce two other sulfur-containing amino acids, cysteine and taurine, which help the body eliminate toxins, build tissues, and promote cardiovascular health.

Methionine helps the liver process fats (lipids), preventing accumulation of too much fat in the liver, which is essential for the elimination of toxins to stay functional. Methionine is needed to make creatine, a nutrient found mainly in muscle tissue and often taken as a supplement to boost athletic performance. Methionine is also needed for collagen formation, which is then used to make skin, nails, and connective tissue. One study suggested that taking 6 grams of methionine a day can improve memory recall in AIDS patients who otherwise show a marked methionine deficiency. Methionine may also help treat symptoms of Parkinson’s disease.

Methionine is an essential amino acid, and can be gained from eating garlic, beans, seeds, eggs, fish, lentils (in lower levels), meat, onions, soybeans, and yogurt.

Tryptophan

  • Three letter code: trp
  • One letter code: W

Tryptophan is an essential amino acid that helps balance nitrogen in adults and growth in infants. It also creates niacin, which is needed to create the “happy” neurotransmitter serotonin. In this way, tryptophan helps influence relief from depression and anxiety, managing pain tolerance and increased emotional well-being. Tryptophan is also associated with promoting deeper sleep.

You can get tryptophan through certain foods or a supplement in powder form. Natural food sources include cheese, milk, fish, turkey (famously), chicken, eggs, pumpkin and sesame seeds, chocolate, as well as tofu and soy.

Phenylalanine

  • Three letter code: phe
  • One letter code: F

Phenylalanine is an essential amino acid that is needed for the functioning of the central nervous system. It has been successfully used to help control feelings of depression and chronic pain, and other diseases linked to a malfunctioning central nervous system. Especially effective for treating brain disorders, phenylalanine is able to penetrate the blood-brain barrier, and only chemicals that are able to cross that barrier can directly influence brain function.

Phenylalanine is used to make epinephrine, dopamine, and norepinephrine, neurotransmitters that control how you perceive and interact with the world around you. Phenylalanine supplementation can help you feel happier and more alert, and it also has been used to treat chronic pain and improve cognitive function. An essential amino acid, phenylalanine is normally obtained from high-protein foods like meat, fish, chicken, eggs, milk, dairy products, beans, and nuts.

Cysteine

  • Three letter code: cys
  • One letter code: C

Cysteine is an amino acid containing a sulfur atom, and is used to form healthy bones, skin, hair, and connective tissue. It is also needed to make glutathione, one of the body’s natural antioxidants that fight free-radical damage. Cysteine and glutathione work together to remove toxins from the liver, and cysteine is often used in emergency rooms to treat acetaminophen overdoses before they can cause liver damage. It also protects the brain and liver against toxins from alcohol and cigarettes, and may be useful in preventing hangovers.

Cysteine is a nonessential amino acid, which means the body manufactures it in-house, but foods such as meat, eggs, dairy products, and whole grains are also good sources of cysteine.

Nonpolar Knowledge

There you have the rundown of the amino acid nonpolar side chains, the nonpolar aminos that variously help form protein molecules in our bodies, and do so much to keep us alive and functioning at top form.

Top 16 Vegan Foods That Are High in Protein

Learn about 16 high-protein vegan foods, including their nutrient content, a few interesting facts about their origins and histories, plus some tasty recipe ideas.

One of the first struggles involved in maintaining a vegan diet is getting enough protein. Significant amounts of casual protein comes from animal sources, and so it takes a fair amount of effort to derive the body’s much-needed protein from plant-based foods. Below are 16 high-protein vegan foods, with their nutrient content, origins, and common recipe uses.

Top 16 vegan foods high in protein.

1. Tofu

One cup of the soy product tofu contains 10 grams of protein. A valuable resource for iron, calcium, the mineral manganese, and vitamin B1, tofu is what’s known as a whole protein, meaning that it contains an adequate amount of the nine essential amino acids necessary in the human diet.

Where It Comes From

Made by pressing soymilk curds into a firm tofu slab, this high-protein source is invaluable. Tempeh and edamame also originate from soybeans, edamame from immature soybeans, which gives them a grassy taste, and tempeh from fermented soybeans, which has a more nutty flavor.

How to Eat It

Formed into cubes or balls, tofu can be grilled, fried, marinated, baked, or thrown into a vegetable stir fry. With a very light nutty flavor, tofu can be easily seasoned with a multitude of flavors, and because it’s such an especially pliable substance (tofu texture can span the range from silken to extra firm), it can be formed into mimicking types of meat like chicken strips, hamburgers, and meatballs.

2. Lentils

One of the great vegan protein sources, lentils are edible legumes, and 1 cup of lentils has approximately 18 grams of protein. Lentils are also high in fiber, folate, and iron.

Where It Comes From

Lentils are widely cultivated throughout Europe, Asia, and North Africa but very little is grown in the Western Hemisphere. An annual plant, its seeds grow two to a pod.

How to Eat It

From soups to salads to a wide variety of side dishes, lentils promote gut health, provide a significant source of dietary fiber, and contain important antioxidants.

3. Seitan

Seitan is a high-protein food made from cooked wheat gluten and is a fantastic meat substitute. One cup has over 75 grams of protein, making it one of the richest plant protein sources, and also a good source for the minerals iron, calcium, and phosphorus.

Where It Comes From

Made from gluten, seitan is the main protein of wheat, which is why it’s sometimes called “wheat meat.” Seitan was coined in Japanese, and roughly translated means “made of proteins.”

How to Eat It

Unlike many soy-based products, seitan actually resembles the look and texture of meat when cooked, and makes for a fun pizza topping. It can be sautéed, pan-fried, and grilled, meaning it’s easy to include in a variety of recipes. Though not for those with celiac disease or a gluten sensitivity, this meat-like plant-based protein is a favorite of many vegetarians and vegans.

4. Wild Rice

An aquatic grass with edible grains, wild rice contains nearly 1.5 times the amount of protein of other long-grain rice varieties like basmati and brown rice. A cooked cup of wild rice contains 7 grams of protein, along with B vitamins, fiber, manganese, copper, and phosphorus. Wild rice is not stripped of its bran (unlike white rice).

Where It Comes From

Wild rice is one of only two cereal grains that are native to North America, and it happens to be the state grain of Minnesota.

How to Eat It

In a soup, as a side, or combined with any dish to add a healthy yet filling dimension to a meal. There are many vegan dishes that include a bed of wild rice as a base.

5. Ezekiel Bread

Ezekiel bread can be made from wheat, barley, millet, spelt, soybeans, and lentils. A single slice of Ezekiel bread contains approximately 4 grams of protein.

Where It Comes From

Ezekiel bread is made from sprouted whole grains and legumes. Because it doesn’t contain added sugars, it is an organic, healthy alternative to other commercial breads. Sprouting also appears to increase the bread’s beta-carotene, vitamin C, vitamin E, and folate content.

How to Eat It

You can eat Ezekiel bread the same as you would eat any other bread: toast, French toast, sandwiches, and so on. It’s easier to digest for people with a gluten sensitivity due to a slightly reduced gluten content, and sprouted grain breads have an enhanced protein and nutrient profile over traditional breads.

6. Hemp Seeds

One tablespoon of hemp seeds (approximately 30 grams) contains 9.47 grams of protein, 50% more than chia seeds and flax seeds. Hemp seeds also contain calcium, magnesium, iron, and zinc. They’re even a good source of omega-3 and omega-6 fatty acids.

Where It Comes From

A variety of the Cannabis sativa plant, hemp seeds do belong to the same family as the marijuana plant but contain only small trace amounts of THC. Hemp seeds may help reduce inflammation, and for women may diminish symptoms of PMS and menopause.

How to Eat It

Hemp seeds can be easily added to a diet by including them in smoothies, oatmeal cookies, homemade salad dressings, and protein bars. This valuable plant-based vegan protein is also highly digestible.

7. Chia Seeds

Speaking of chia seeds, though lower in protein than hemp seeds, chia seeds are quite high in fiber (28 grams of chia seeds delivers 11 grams of fiber). Chia seeds also contain iron, calcium, selenium, magnesium, omega-3 fatty acids, and antioxidants.

Where It Comes From

An important food for the ancient Aztecs and Mayans, chia seeds are an annual herb from the mint family and native to Mexico and Guatemala.

How to Eat It

Chia seeds have a bland taste and are able to absorb water until they reach a gel-like consistency. This makes them easy to include in a variety of recipes, from baked goods to smoothies to their own chia seed pudding.

8. Green Peas

A cup of cooked green peas contains 9 grams of protein (a little bit more than a full cup of milk), and provides more than 25% of your daily fiber requirements.

Where It Comes From

The pea is a small green seed eaten as a vegetable; the field pea was one of the very first crops cultivated by humankind.

How to Eat It

Often served as a side dish, sweet green peas can be stuffed in with ravioli filling, made into pea soup, or added to salads for delightful taste and texture. Mashed peas can be used even more creatively, as part of or an alternative to traditional avocado guacamole, as a spread for bread or crackers, or folded into other dishes for their valuable health content.

9. Pumpkin Seeds

A 100-gram serving of organic pumpkin seeds contains 15 grams of carbohydrates and 5 milligrams of protein.

Where It Comes From

From the pumpkin fruit (named after the Greek word pepon meaning “large melon”), pumpkin seeds have been found in Mexico dating back to the period between 7000-5500 B.C.

How to Eat It

You can flavor and roast pumpkin seeds in your oven, and enjoy them as a quick snack between meals. Whether plain, sweet, or salty, they can help curb your hunger during the day while adding a little extra protein to your stores.

10. Spelt

Spelt is an ancient grain, along with einkorn, barley, teff (also particularly high in fiber and gluten free), sorghum, and farro. One cup of raw spelt has 25 grams of protein and is an excellent source of complex carbs, fiber, iron, magnesium, phosphorus, and manganese.

Where It Comes From

Spelt is a type of wheat that contains gluten. A member of the farro family of grains, it was originally cultivated in what is now present-day Iran.

How to Eat It

Spelt can be prepared and eaten much like rice, but can also be included in a variety of recipes, from baked goods to pizza, from polenta to risotto.

11. Chickpeas

Also known as garbanzo beans, chickpeas are a legume that contain about 5 grams of protein per cooked cup. They are also an excellent source of complex carbs, iron, fiber, folate, phosphorus, and potassium.

Where It Comes From

An annual plant of the pea family, chickpeas were likely domesticated as a crop in what is currently southeastern Turkey and Syria about 11,000 years ago.

How to Eat It

Chickpeas are a staple of Middle Eastern, African, and Indian cuisines. Often made into hummus, chickpeas can also be added to stews, mashed to form pancakes and fritters, or flavored for taste and eaten on their own.

12. Nutritional Yeast

Nutritional yeast is a deactivated form of yeast. Fortified nutritional yeast is a great source for all the B vitamins, as well as the minerals zinc, magnesium, copper, and manganese. It also provides 14 grams of protein and 7 grams of fiber per ounce.

Where It Comes From

Nutritional yeast is derived from the single-cell organism Saccharomyces cerevisiae, which is grown on molasses before being harvested and heat-dried to deactivate it. Due to its being inactive, unlike baking yeast, nutritional yeast does not froth or grow, and thus has no leavening ability.

How to Eat It

Nutritional yeast can be enjoyed as a savory topping for popcorn thanks to its cheesy flavor, or sprinkled over pasta or pizza in lieu of Parmesan. It is also a popular ingredient for adding into dishes like mashed potatoes or scrambled tofu, both for its taste as well as its health benefits.

13. Quinoa

Another of the ancient grains, quinoa is gluten-free and considered a pseudocereal because it does not grow quite like other cereal grains do. One cup of cooked quinoa has 8.14 grams of protein.

Where It Comes From

A member of the goosefoot family, quinoa was widely cultivated in the Andes for its edible starchy seeds.

How to Eat It

Quinoa can be used in a powder form for adding protein content to baked goods. Otherwise it can be treated much the same as a rice dish: used as a base, a side, or eaten on its own with whatever preferred seasoning you’ve got.

14. Oats

With a good amounts of folate, magnesium, zinc, and phosphorus, oats are a cereal plant cultivated in cool climates and used for animal feed as well as human consumption. Although not considered a complete protein, 1 cup of cooked steel-cut oats has 10 grams of plant protein.

Where It Comes From

Originally considered a weed that afflicted wheat and barley, oats have since become a staple food in Western diets.

How to Eat It

Oats can be eaten in oatmeal, of course, and oatmeal cookies, but oats can also be included in veggie burgers, homemade protein bars, and mixed with yogurt for a pleasing and nutritious texture.

15. Edamame

Edamame is a green soy bean, and has 18 grams of protein per cup (a significant amount of protein).

Where It Comes From

Translated from Japanese, edamame literally means “beans on a branch,” and appears regularly in and alongside Japanese cuisine (though edamame’s roots are actually in China).

How to Eat It

You’ll recognize edamame at sushi restaurants, but it doesn’t have to stay there. In their pods, edamame can be boiled or baked and eaten as a snack. Shelled edamame can be added to salads, stews, basically any dish you want.

16. Peanut Butter

There are 65 grams of protein in 1 cup of peanut butter. Nuts and nut butters are a great source of protein, fiber, vitamins, and minerals.

Where It Comes From

Dr. John Harvey Kellogg (of Kellogg’s cereal) patented a process for creating peanut butter in 1895. He noted that it was a healthy protein substitute for patients without teeth.

How to Eat It

Spread it, blend it, bake it into cookies, roll it into balls with other high-protein ingredients, literally go nuts!

High-Protein Vegan Foods

While it is important to be cognizant of the protein and amino acids often missing from a vegan diet, these vegan sources of protein show that removing animal products from your diet isn’t a loss. Instead, it’s a healthy alternative that leads to a rich variety of plant-based foods.

How to Use Amino Acids for Bodybuilding

Amino acids have become some of the most popular types of bodybuilding supplements across multiple disciplines. Both BCAAs and EAAs can be used on their own or in the form of “stacks”—specialized blends of multiple supplements that work together synergistically to provide even greater benefits than when taken on their own.

Bodybuilding usually refers to increasing and sculpting muscle mass for appearance as well as strength. In a more general sense, bodybuilding can refer to increasing muscle mass and function for the purpose of competing in sports such as football or power sports (e.qg., shot putting, discus throwing, etc.). It is a given that bodybuilding requires resistance training. If bodybuilding is for the purpose of improving competitive performance in a specific sport there are likely to be training requirements unique to that sport. This discussion on amino acids for bodybuilding will, therefore, not focus on the specific aspects of training. Regardless of the goal of training, amino acids play a key role in bodybuilding.

The Impact of Nutrition on Bodybuilding

Training tends to be the first factor most consider when seeking to build lean muscle, however, the nutrients we provide our bodies with can be equally influential—or more so—in determining how quickly we progress toward our goals. No matter how intensely you train, you will not be able to achieve the results you desire if you’re lacking certain crucial nutritional elements.

Obtaining all the nutrients you need from your diet alone in the quantities necessary for maximal bodybuilding results can be challenging. That’s where workout supplements come in.

By taking targeted sports nutrition supplements, you can ensure you get all the nutrients you need to build muscle, speed recovery time, decrease muscle soreness, amp up energy levels, and more.

Bodybuilding Supplements Then and Now

Depending on how broadly you interpret the idea of dietary supplementation, the idea of bodybuilding supplements can be traced back to ancient Greece.

According to Professor Andrew Dalby and other experts, Greek and Roman athletes consumed large quantities of meat and wine as well as herbal concoctions and tonics with the goal of increasing their strength and stamina.

In the early 1900s, Eugen Sandow, a pioneering German bodybuilder whose legacy earned him the honorific “father of modern bodybuilding,” advised all who wished to maximize their muscle growth to adhere to the dietary rules he himself followed. Bodybuilder Earle Liederman, who rose to prominence in the 1920s, recommended drinking what he called “beef juice” or “beef extract” (a substance the luminaries of today’s wellness landscape call “bone broth” and chefs simply refer to as “consommé) in order to speed muscle recovery.

In the 1950s, protein powders entered the picture as recreational and competitive bodybuilding became ever more popular with ever-broader audiences in the United States and elsewhere. Irvin P. Johnson, who operated a bodybuilding gym in Chicago, was one of the first to market egg-based protein powder. According to an article he published in Iron Man with the title “Build Bigger Biceps Faster with Food Supplements,” his specialized line of protein powders fueled serious strength gains. According to the article, he went from only being able to leg press 165 pounds for 10 repetitions to 660 pounds for 12 repetitions!

The bodybuilding supplement industry grew at an exponential rate throughout the 1970s and 1980s, fueled both by increased interest in recreational bodybuilding as well as advancements in advertising. Then, in October of 1994, Congress passed the Dietary Supplement Health and Education Act, a piece of legislation that transferred responsibility for determining the safety of dietary supplements such as protein powders and other mainstays of sports nutrition from the government to the manufacturers of the products. Unless they added a new dietary ingredient, manufacturers were no longer required to provide the U.S. Food and Drug Administration (FDA) with evidence to substantiate the safety or efficacy of their products. Legal experts believe this opened the door for the supplement industry to sell even more of their products. According to a Consumer Reports publication, annual sales of sports nutrition supplements hit $2.7 billion in 2010. And according to the “Sports Nutrition and High Energy Supplements – Global Market Outlook (2017-2026)” report sports nutrition and high energy supplements made $44.58 billion in 2017 with an outlook of $124.85 billion by 2026.

Defining the Term “Bodybuilding Supplements”

Just as the term bodybuilding can encompass both physique-focused and performance-focused endeavors, so too can the term “bodybuilding supplements” encompass a multitude of dietary supplements utilized by individuals engaged in bodybuilding as well as weight lifting, mixed martial arts, and other athletic pursuits to increase lean body mass as well as bring about other desirable outcomes such as:

  • Decreased body fat
  • Sharper muscle definition
  • Enhanced athletic performance

Amino acids have become some of the most popular types of bodybuilding supplements across multiple disciplines. Both branched-chain amino acid supplements (BCAA supplements) and essential amino acids (EAAs) can be used on their own or in the form of “stacks”—specialized blends of multiple supplements that work together synergistically to provide even greater benefits than when taken on their own.

Making the Most of the Building Blocks of Protein

Amino acids have earned the nickname “the building blocks protein” because of the vital role they play in creating muscle tissue. While it’s certainly possible to obtain all the amino acids you need simply by eating high-protein foods like eggs, lean meats, legumes, vegetables, and pseudo-grains like quinoa, amino acid supplements can be a convenient and efficient way to maximize the benefits of amino acids.

One of the most compelling reasons to use supplements can be captured in a single word: bioavailability. Bioavailability refers to how efficiently a substance can be metabolized and the percentage of what’s ingested that’s utilized for its intended purpose inside the body.

Several factors determine the bioavailability of each amino acid. For example, when taking in amino acids from a food source, the amount of fat contained in that food influences the length of time it takes for amino acids to be put to use. The way you cook food can also impact the amino acids it contains. Some heat-sensitive amino acids can even decompose when cooked. And not all amino acid supplements are metabolized at the same rate. The physical nature of the supplement will have the most significant influence on its bioavailability. A BCAA powder, for instance, will be digested differently than a supplement in pill or liquid form. The extent to which a supplement is pre-digested as well as whether it contains any fillers or binders impact its overall bioavailability.

Understanding Muscle Protein Turnover

Muscle protein turnover is the metabolic basis that powers increased muscle mass, strength, and function.

Muscle protein turnover refers to the constant breakdown of older muscle proteins that are no longer operating at peak efficiency and their replacement with newly synthesized, more efficient muscle protein fibers. The balance between protein synthesis and breakdown determines whether a muscle is growing or shrinking.

Muscle function is accomplished by the contraction of muscle protein fibers. Muscle strength and function are determined by how many muscle protein fibers you have and the efficiency with which they contract. Increasing muscle protein mass and contractile efficiency is accomplished by optimizing muscle protein turnover.

For bodybuilding, the goal is to make the rate of muscle protein synthesis exceed the rate of protein breakdown. Further, the increased balance between muscle protein synthesis and breakdown should optimally be accomplished mainly by stimulating synthesis, not lessening breakdown—protein breakdown gets rid of muscle proteins that are not functioning efficiently, so it is good to keep that process functioning at full speed.

The Mechanics of Muscle Protein Synthesis

Muscle proteins are composed of a series of amino acids hooked together in a specific order determined by the messenger RNA (mRNA) in the cell for each specific muscle protein. The sequence of the mRNA is dictated by the DNA in the cell. There is a specific molecule for each amino acid (tRNA) that delivers it to the mRNA as required for incorporation into the protein that is being produced.

A simple, conceptual way to think about the process of muscle protein synthesis is to compare it to the construction of a building. The DNA is basically the idea for the design of the building. The RNA is the written plan or blueprint, and transcription of the mRNA from the DNA is the process of writing up the plan. The tRNA molecules that bring the amino acids to the mRNA for incorporation into protein are like trucks that bring bricks to the building site, and the hooking of amino acids together in the proper order on the mRNA corresponds to the builder putting the bricks together according to the blueprint. The protein is the final product, or completed building, ready to serve its function.

The details of how muscle protein is made are important only so that it is clear why all the amino acids must be available in abundance. If the mRNA dictates that the next amino acid in the chain making up the protein is a particular amino acid that is deficient, then the process is halted and no muscle protein is produced.

How Amino Acids Impact Muscle Protein Synthesis

We must derive certain amino acids, as I touched on earlier, from dietary protein. However, the human body can synthesize other amino acids through chemical reactions that occur in the liver and select sites throughout the body.

The amino acids that must be obtained from the diet are called essential amino acids, or EAAs, while the amino acids that can be made in the body are called nonessential amino acids, or NEAAS.

The nine essential amino acids are leucine, isoleucine, valine, phenylalanine, lysine, methionine, phenylalanine, threonine, and tryptophan. Three of the EAAs, leucine, isoleucine, and valine, have been subcategorized as branched-chain amino acids (BCAAs), a descriptor which refers to their chemical structure. We typically put the number of nonessential amino acids at 11, as that’s how many NEAAs can be found in human protein, though other NEAAs like citrulline and ornithine can be found elsewhere in the body.

Since your body can produce NEAAS and they are available in abundance, the availability of EAAs serves as the limiting factor for setting the rate of muscle protein synthesis.

Using Essential Amino Acids to Stimulate Muscle Growth

Consuming essential amino acids, either as dietary protein or supplements, is the most potent stimulus of muscle protein synthesis. Consuming nonessential amino acids, either alone or with EAAs, has no impact.

EAA supplements have been shown to trigger muscle protein synthesis and increase muscle mass, strength, and physical function in at least 25 clinical trials. The muscle-building response to EAAs is 2 to 4 times greater than the muscle-building response to the same amount of a whey protein supplement. The muscle-building response to EAAs is even greater than the response to hormonal treatment with testosterone, growth hormone, or insulin.

There is one very big must when it comes to EAA supplementation, however. In order to be effective, all the EAAs are required. That being said, there are varying degrees of importance among the EAAs.

Leucine, which is both an EAA and a BCAA, is particularly important. Leucine is the most abundant EAA in muscle protein, so it should comprise the highest proportion of an EAA supplement. Beyond its role as a component of muscle protein, leucine can signal the molecular mechanisms within the cell to initiate the process of protein synthesis. Important as leucine may be, however, it cannot function alone. All the other EAAs are required as well, roughly in proportion to their relative content in muscle. It is not possible to make muscle protein from leucine alone.

The Role of Essential Amino Acids for Bodybuilding

It is clear from the above discussion that making sure you consume enough essential amino acids is an important part of bodybuilding. Even when using EAA supplements, the main source for your essential amino acids intake will likely be dietary protein. Therefore, the place to start is with your diet.

Protein is the key dietary component of the basic bodybuilding diet. It will increase your muscle mass. You should set a goal of eating approximately 30% of your caloric intake as high-quality protein.

When I say high-quality protein, I mean a protein that contains a high abundance of essential amino acids. High-quality proteins are generally animal-based proteins. These protein food sources also have a significant amount of non-protein calories. Therefore, eating a sufficient amount of high-quality protein to supply all the EAAs you need is difficult through normal diet alone.

You will most likely run into issues with the flexibility of your diet when eating this amount of high-quality protein food sources because of the non-protein calories. Therefore, EAA supplements can play a vital role in helping you meet your dietary goal for EAA intake.

While the focus of your basic diet should be high-quality protein, you must remember that energy substrates (carbohydrates and fat) are important too. As an example, in a tightly controlled study, subjects drank the same amount of protein in the form of milk. In one case, it was skim milk, and in the other case whole milk. The stimulation of muscle protein synthesis was greater with the whole milk. Under these study conditions, the additional calories provided by the fat in the whole milk helped to fuel muscle building.

You must be in a positive energy balance to gain a significant amount of muscle mass. Carbohydrate is of less importance for resistance training than it is for endurance training, but you should eat enough fruit and vegetables to meet the RDAs for micronutrients. Also, carbohydrate intake will stimulate insulin release, and insulin is an anabolic hormone that will increase the amount of muscle protein made from your EAA intake.

Fat intake will also amplify the anabolic effect of EAAs, and therefore you can eat animal-based, high-quality protein foods without worrying about eating too much fat.

What you do want to keep in mind with your bodybuilding diet is that the more you eat, the bigger you will get. If you do eat a lot while lifting heavy weights and consuming EAA supplements as recommended, a significant part of the weight gain will be muscle.

You will also gain fat with this dietary approach, so you need to carefully monitor your body composition to be sure that the extra fat you put on does not counteract the benefits of the muscle gain. In a sport like powerlifting, that is not likely to be the case, but if you are bodybuilding for appearance, you must reach a balance between muscle and fat gains. This can be accomplished by incorporating aerobic exercise into your training program.

How to Use Essential Amino Acids for Optimal Bodybuilding Results

amino acids for bodybuilding

The research documenting the optimal use of amino acids for bodybuilding is extensive. Experts can provide precise guidance on the effects of taking EAAs both pre-workout and post-workout.

Consuming 15 grams of EAAs 30 minutes before starting your workout will elevate blood concentrations of essential amino acids throughout your workout and stop the muscle breakdown that would otherwise occur. A 15-gram dose of EAAs achieves a greater response on muscle protein synthesis than either casein or whey protein can, without creating the fullness that can hinder a workout.

Then immediately after your workout, take another 15 grams of EAAs. One hour later, take another 15-gram dose.

These recommendations stem from the assumption that you will be working out every day. When you do take off days, you should still consume the same amount of EAAs. Instead of using your workouts to determine the timing, however, take your EAAs between meals.

Between the completion of dinner and breakfast the next morning, you may go for 12 hours or more without food. During this post-absorptive time, muscle tissue breakdown transpires in order to supply amino acids to tissues and organs that have no protein reserve. Therefore, to fuel maximal muscle-building response around the clock, you should consume another 15 grams of EAAs before bedtime. If you have wholly committed to maximizing muscle gain, you can even set your alarm for a final dose at about 4 am.

Alternatively, you can take 20 grams of casein protein at bedtime. Because casein coagulates in the stomach, your body digests it at a slower rate, meaning the amino acids it contains are then absorbed over many hours. While the anabolic effect will be less than if you take the EAAs, this approach will save you the trouble of getting up in the middle of the night.

The total amount of supplemental EAAs you ingest should be in the range of 60 grams per day. Consuming this amount of EAAs will stimulate the production of new muscle protein without you having to also take in a significant amount of non-protein calories. The result will be a lean body with increased muscle mass and minimal increase in fat mass. Sixty grams of EAAs in addition to what you eat as part of your bodybuilding diet is needed to drive protein synthesis past what may be your normal genetic limit.

Do EAA Supplements Have Side Effects?

This a reasonable question, because bodybuilding requires a much higher than average EAA intake. An important caveat to state up front is that I am focusing exclusively on side effects from EAA supplements.

When your EAAs come from an unusually high amount of dietary protein intake, that will increase the rate of amino acid oxidation and as a result, burden the kidneys to excrete the ammonia and urea that are natural byproducts of NEAA oxidation.

The great thing about EAA supplements, however, is that there is no such increased oxidation of NEAAs when EAAs are consumed. This is because NEAAs are not also being consumed but are rather being produced in the body. In fact, the oxidation of the NEAAs actually goes down, since they are being incorporated into protein at an increased rate.

Consequently, there is no reason to worry about the side effects of EAA supplements. The FDA has determined EAA supplements to be Generally Regarded as Safe (GRAS), while the Food and Nutrition Board of the National Academy of Science has determined that there is no upper limit of consumption beyond which would not be safe.

Unlock Lasting Weight-Loss Results by Understanding Hunger Control

Weight loss and maintenance depend on a number of factors, one of which is controlling the desire to eat. Dietary proteins and amino acids play key roles in hunger control. Learn how to maximize their effect.

Weight loss and successful long-term weight maintenance depend on a number of factors, one of which is controlling the desire to eat. While there are numerous approaches to weight management, reducing your caloric intake will almost certainly play an important role in helping you achieve your desired body weight. No matter how dedicated you are, if you’re dealing with persistent feelings of hunger, it’s highly likely that you will deviate from your mindful eating intentions. Fortunately, there are scientifically validated ways to keep your hunger levels in check. Researchers have found that dietary proteins, as well as amino acids, play key roles in hunger control.

Studies Show Eating More Protein Can Curb Hunger

Increasing satiety by choosing the right foods to eat is essential to achieving successful weight loss and weight maintenance.

Scientists have known for more than 50 years that when you eat a high-protein meal you end up consuming fewer calories. In 1956, a research team composed of Sherman Mellinkoff, Marjorie Frankland, David Boyle, and Margaret Greipel found a clear link between amino acid concentration in the blood and hunger levels. The more amino acids were circulating in a subject’s blood, the lower their reported level of hunger…and the fewer amino acids, the higher their level of hunger. The researchers noted that the same relationship appeared to exist between blood sugar levels and hunger—when blood sugar levels dropped, participants’ appetites soared. Since that pioneering study, it has been repeatedly shown that dietary protein elevates amino acid concentrations in the blood and that high-protein meals function as appetite suppressants.

Several studies conducted on healthy subjects have shown, too, that long-term adherence to a high-protein diet can increase feelings of fullness in an enduring way. Some of these studies carefully controlled energy balance by having the subjects live in a chamber for several days so that their total energy expenditure could be accurately measured. The level of energy expenditure was matched with the same amount of caloric intake. This approach ensured that the only variable was the level of protein intake, so there was no doubt that the effect on appetite control stemmed from the higher intake of dietary protein.

Why Eating High-Protein Meals Makes You Feel More Satiated

There are a few theories as to why a high-protein meal makes you feel fuller.

One potential pathway has to do with hunger hormones such as peptide YY (PYY), sometimes referred to as the fullness hormone. Research shows that peptide YY helps control hunger and food intake. Scientists have found that when you eat protein, your gut releases these hunger hormones.

According to a study published in Cell Metabolism, eating a high-protein diet increases your body’s production of hunger-fighting PYY.

“We’ve now found that increasing the protein content of the diet augments the body’s own PYY, helping to reduce hunger and aid weight loss,” said Rachel Batterham of University College London, a Medical Research Council clinician scientist and the study’s lead author.

Batterham and her fellow researchers found that eating high-protein meals stimulated the body to release more PYY than either high-fat or high-carbohydrate meals. Consequently, both normal-weight and obese participants who ate the high-protein meals reported fewer food cravings and less overall hunger.

The research team conducted follow-up studies with mice in order to eliminate other factors that could influence the results. They discovered that mice on high-protein diets had higher PYY levels and ate fewer calories than those who ate the usual amount of protein. They also had lower body fat levels.

So, what is it about high-protein foods specifically that produces this effect on fullness signals?

One hypothesis, which I introduced above, has to do with amino acids. Proteins are made up of amino acids, so when we eat a high-protein meal the plasma concentrations of their component amino acids spike. Some researchers, including the team behind that groundbreaking 1956 study, believe that this elevation of plasma amino acid levels can promote feelings of fullness.

Dietary proteins and amino acids play key roles in hunger control.

Amino Acids: The Key to Quelling Many Types of Hunger

A review of studies conducted to date provides indisputable evidence that amino acids on their own, separate from other compounds found in protein, can lower hunger levels.

The satiating effect of increased plasma amino acids was proven in an experiment in which amino acids were infused intravenously. This study demonstrated that intravenous amino acid infusion increased the satiety rating and feeling of fullness, even though nothing was ingested into the gastrointestinal tract. The suppression of appetite was due to elevated plasma amino acid concentrations. When the infusion stopped and plasma amino acid concentrations returned to the basal level, the effect on satiety was eliminated.

As with the question of exactly what biological mechanisms underlie the clear connection between protein intake and increased satiety, there is no single, succinct answer to the question of why their component amino acids have such a pronounced effect on hunger control.

One possibility is that a greater availability of amino acids, particularly the essential amino acids that cannot be produced in the body, stimulates protein synthesis. The stimulation of protein synthesis increases energy expenditure. Recent research proposed that the extra use of oxygen associated with stimulated protein synthesis results in increased satiety.

Another possibility is that the actions of amino acids in the brain stimulate satiety. When amino acids were infused into the intestines of cats, either as a mixture or independently, researchers recorded increased signaling from the part of the brain responsible for satiety. Early amino acid studies that identified the brain receptor that influences satiety are supported by the more recent identification of a chemosensor for dietary essential amino acids in the brains of rats. This area of the brain projects signals to other brain areas that are associated with the control of food intake.

Do All Amino Acids Help Control Hunger?

The short answer is, no. While all amino acids have health benefits and can be valuable components of dietary supplements, scientists have found that only some amino acids increase satiety. Other amino acids have been shown to have either no discernible effect on appetite or, in some cases, to stimulate the appetite.

The results of one study showed that while tryptophan and lysine increased satiety, proline and threonine had no effect and arginine decreased satiety.

The results of another study in which essential amino acids were directly injected into the cerebroventricular area of the brain found that injections of all three of the branched-chain amino acids (BCAAs) or leucine individually led to a suppressed food intake. Ultimately, the study’s authors determined that the effect of the BCAA injection was entirely due to leucine, as individual injections of the other BCAAs, isoleucine and valine, had no effect.

Not only does an augmented supply of certain dietary essential amino acids including leucine, lysine, and tryptophan induce satiety, but the reverse is also true. When your body lacks amino acids, that spurs your appetite.

Research consistently indicates that a low-protein diet drives increased food intake—in fact, there is a brain receptor that identifies a diet deficient in essential amino acids! A low-protein diet causes an increase in food intake in order to correct the amino acid deficiency, which can easily result in weight gain. This phenomenon was demonstrated by a study published in Physiology and Behavior. Increased food intake occurs when intake of all the essential amino acids drops, not just leucine or other amino acids directly linked to fullness signals.

How You Can Use Scientific Findings to Achieve Real-World Weight-Loss Results

So, you may be asking yourself, what does this all mean for my personal weight-loss journey?

As I have mentioned, understanding the precise biological mechanisms that affect hunger control can be challenging. Satiety is difficult to quantify objectively in humans. A number of factors come into play, and we do not have access to the complete workings of the brain. Consequently, we must rely extensively on data obtained from rats, which differ from humans in obvious ways. That being said, there are important findings obtained from studies on rats that are relevant to human nutrition.

With regard to amino acids, a rat’s brain can sense when essential amino acids are available and modify dietary intake accordingly. Elevated levels of certain essential amino acids—namely leucine, lysine, and tryptophan—can increase satiety, while a deficiency of essential amino acids increases the amount of food eaten. Following this science, a low-protein diet increases food intake and causes weight gain, and a high-protein diet reduces food intake.

In addition to ensuring an adequate intake of dietary protein, you may find it beneficial to consume a balanced mixture of free essential amino acids. Essential amino acids produce the same effect as high-protein foods but contain far fewer calories.

Taking a complete essential amino acid supplement with all the essential aminos has been shown to be the most low-calorie way to improve hunger control. While not all amino acids directly affect your hunger levels, it appears that supplementing with individual amino acids does not have the same effectiveness as optimizing your intake of all the essential amino acids.

What Is the Keto Diet—and Can Amino Acids and Other Supplements Really Improve Results?

Consistently following a ketogenic diet, or keto diet, is an effective way to lose weight and keep it off. Taking amino acids along with following a keto diet can expedite the metabolic processes responsible for ketogenic weight loss.

People diet for different reasons, such as preventing or treating infection, managing diabetes, gaining muscle mass, or maintaining a healthy weight. Weight loss is the most popular reason for dieting, but weight loss can be quite difficult to achieve depending on the type of diet you follow. If you’re interested in how the foods you eat can impact your weight and well-being, chances are, you’ve encountered the phrase “keto diet,” but you may still be wondering: “What is the keto diet?”

The ketogenic diet, often shortened to the keto diet, is an extremely low-carbohydrate diet approach (even sticter than the infamous Atkins diet) that proponents state can train your body to burn fat more efficiently. Many individuals have shared their experiences using the keto diet to lose weight, improve their overall health, and enhance physical and mental performance, leading to increased interest in the diet. Some of the benefits of the keto diet have been validated by scientific studies and a growing number of medical professionals recommend it as a means of addressing lifestyle-related chronic conditions.

As more and more people adopt a keto diet, often with the goal of losing weight and keeping it off, some have begun exploring whether certain supplements can improve their results. It appears that amino acids show particular promise as a means of enhancing metabolic processes responsible for ketogenic weight loss.

In this article, we’ll provide an introduction to the keto diet, cover some of the most common benefits associated with the keto diet, and then share the best keto diet supplements to take and how those supplements can help accelerate your keto diet results.

What Is the Keto Diet?

The ketogenic diet was developed in the 1920s as a treatment for epilepsy. Traditionally, it was used to treat children, but in recent years, it has been used to treat adults with epilepsy that does not respond to other interventions. And, of course, its use has expanded far beyond that initial medical context.

After the fat-free diet craze went bust, researchers turned their attention to carbohydrates. Ironically, diets that discourage fatty foods often encourage the consumption of low-fat, fat-free, or trans-fat options loaded with highly processed ingredients that the body stores as fat. Low-fat diets tend to place less emphasis on monitoring the intake of carbohydrates, which can greatly jeopardize calorie-burning processes at the cellular level.

Carbohydrates come in many food forms; sugars, complex carbohydrates (starches), and fiber are the three main types. Regularly consuming carbohydrates over time has been linked to higher risk of developing chronic illness, especially cardiovascular disease.

How the Keto Diet Encourages Your Body to Burn More Fat

The foundational principle of the keto diet is rigid carbohydrate restriction. Carbohydrates are the body’s preferred source of fuels; however, your body can also run off of fat. When you keep your carb intake below a certain threshold while adhering to a high-fat diet, your body switches from burning carbs for fuel to burning fat.

The “keto” in ketogenic refers to small fuel molecules called ketones that your body runs off of when it does not have access to significant quantities of glucose (blood sugar) from carbohydrates.

When you eat carbohydrates, your body quickly converts them into glucose via a process called glucogenesis. Excess protein can also be converted to glucose. The glucose produced from carbohydrates and protein can be used to power your body, but any that’s not immediately needed gets stored as fat.

If your body does not have a ready supply of glucose, it switches over to a process called ketogenesis. The liver converts loose fatty acids into ketone bodies that cells use for energy while the body metabolizes fat and burns calories at a high rate. Ketosis, a term that pops up frequently in reference to the keto diet, describes the moment when the body enters the metabolic state in which it’s running off of fat rather than carbohydrates.

The quickest way to enter a state of ketosis is to fast, but that short-term approach has its limitations. Adopting the keto diet allows you to enter and stay in ketosis for a sustained period of time.

Consistently following a comprehensive ketogenic diet, otherwise known as the keto diet, is an effective way to lose weight and keep it off. Taking amino acids along with following a keto diet can expedite the metabolic processes responsible for ketogenic weight loss.

The Basics of the Keto Diet

Entering a state of ketosis does require some number crunching to track nutrient intake, something many other diets involve too. The basic ratios of the keto diet are:

  • 70% to 75% fat
  • 15% to 25% protein
  • 5% carbohydrates

The most crucial aspect of these ratios is carbohydrate intake. Most individuals will need to limit their carb intake to 50 grams or fewer of net carbs per day. Some experience even greater benefits with a daily carb intake below 20 grams.

For the best keto diet results, you will also need to pay attention to how much protein you consume. The bulk of your calories should come from high-fat, moderate-protein foods, since excess quantities of protein can be converted into glucose.

Athletes or individuals who engage in high-intensity activity should monitor their performance when on the keto diet and may require more protein and carbohydrates for peak metabolic function. One to two days of carbohydrate refueling followed by ketogenic dieting the remaining days of the week is a common dietary program for high-endurance performers.

But if you decrease the intensity of your workouts, plan accordingly. A more precision-based model for carbohydrate intake may work best in this instance. Eating easily digestible natural carbohydrates, like honey, 30 minutes prior to a moderate to vigorous workout can offset potential energy deficiencies created by a keto diet meal plan.

7 Health Benefits of the Keto Diet

The time that it takes for you to achieve ketosis depends on how well-adapted your body is to the ketogenic process. The most reliable way to determine whether you have entered a state of ketosis is to use a blood ketone meter, which can gauge ketone levels in your blood.

Optimal ketosis—the point at which you begin to experience the health benefits of the keto diet, such as weight loss—typically begins when blood ketone levels reach between 1.5 mmol/L and 3.0 mmol/L.

For most people, it takes 2 to 3 weeks to reach optimal ketosis. During this time, you may experience symptoms of “keto flu” as your body acclimates to this new metabolic state. Some common side effects people experience during this entry phase include:

  • Mood swings
  • Drowsiness
  • Fatigue
  • Intestinal discomfort

Once you reach ketosis, however, any initial unpleasantness you experienced will clear up and you will begin to reap the health benefits. Here are seven of the most common benefits associated with the keto diet.

1. Sustainable Weight Loss

The keto diet, in essence, turns your body into a fat-burning machine. As you might anticipate, this can have significant benefits when it comes to weight loss. Strong scientific evidence shows that the keto diet dramatically increases the body’s fat-burning capacity while decreasing levels of insulin, a hormone that encourages fat storage.

2. Decreased Hunger

Researchers have also found that the keto diet supports body fat loss while decreasing appetite, making it easier to stick to the meal plans you set up for yourself.

One reason for this is likely that when your body uses fat as its primary fuel source, it has round-the-clock access to weeks or months of stored energy. This eliminates the hunger attacks many experience when their blood sugar spikes and then plummets after a high-carb meal.

3. Balanced Blood Sugar Levels

Adopting a keto diet can help you gain control over your blood sugar levels. For this reason, medical practitioners may recommend the keto diet to patients with type 2 diabetes. The keto diet can not only lead to better management of this condition, but also, as studies have shown, to a reversal of the disease.

Though no randomized, controlled trials have examined whether the keto diet can help prevent or reverse pre-diabetes, its impressive effect as a treatment for full-blown type 2 diabetes along with anecdotal evidence makes a strong case for its likely success.

4. Reduced Risk of Heart Disease

Multiple studies have shown that adopting a low-carb diet, like the keto diet, can positively influence several key risk factors for the development of heart disease, including cholesterol levels. Levels of high-density lipoprotein (HDL) cholesterol and triglycerides consistently drop while low-density lipoprotein (LDL) levels remain fairly stable.

It’s also common for people who switch from, for instance, the standard American diet (aptly abbreviated to SAD), to the keto diet to see decreases in blood pressure numbers.

5. Heightened Cognitive Skills and Mental Clarity

While weight loss and improved physical health rank high among the reasons people try the keto diet, some seek it out for its beneficial impact on cognition.

When the body enters ketosis, your brain activity no longer depends on glucose stores. Instead, it runs off a steady supply of ketones. This can eliminate frustrating issues related to blood sugar swings, such as brain fog and difficulty focusing.

6. Boosted Energy and Endurance

By allowing you to access the vast amounts of energy in your body’s fat stores, the keto diet can keep your vitality high.

While stores of glucose only contain enough energy to fuel you through a few hours of physical exertion, your fat stores could theoretically last for weeks.

7. Better Digestion and Nutrient Absorption

Many find that adopting the keto diet can relieve symptoms of digestive distress associated with IBS and other conditions.

This benefit often sets in rapidly. Within days of following a keto meal plan, individuals report improvements and fewer instances of bloating, gas, and stomach cramps and pain. Consistently following a comprehensive ketogenic diet, otherwise known as the keto diet, is an effective way to lose weight and keep it off. Taking amino acids along with following a keto diet can expedite the metabolic processes responsible for ketogenic weight loss.

It generally takes 3 to 6 months to train your body to reach optimal ketosis at a fast rate.

Once you reach that milestone, you can begin to gradually re-introduce plant-based carbohydrates from fruits and vegetables into your diet. At this stage, it’s particularly important to continue to monitor your protein intake. Protein surges can cause insulin levels to rise in the blood, which can hinder ketosis.

While transitioning into ketosis, it can be beneficial to engage in high-intensity workouts, as doing so will accelerate glycogen depletion. Many find that when they are in a state of ketosis, they feel best when participating in low-impact exercise, such as jogging or speed walking, yoga, swimming, or dancing.

Using Supplements to Improve Your Keto Results

Those who commit to a keto-friendly, low-carb foods centered approach to eating long term often find that adding specific supplements can maximize the benefits of the keto diet while minimizing any less-than-pleasant side effects.

Some supplements help fill in possible deficiencies that can result when personal preferences are overlaid on top of the restrictions built into the keto diet. Others help counteract symptoms of keto flu experienced while the body adapts to a state of ketosis, or enhance athletic performance.

Here are three supplements that can enhance the positive effects linked to the keto diet and offset any unwanted ones.

1. Amino Acids

Amino acids are the building blocks of proteins. Proteins consist of single- or long-chain amino acids and are necessary nutrients for most cell and organ functions. Consuming measured proteins in correct proportion to nutrient fat can facilitate ketosis. Ketogenic amino acids can convert to acetyl-CoA, a precursor of ketone bodies, whereas glucogenic amino acids degrade to glucose.

Lysine and leucine function exclusively as ketogenic amino acids. Isoleucine, phenylalanine, threonine, tryptophan, and tyrosine function both as ketogenic and glucogenic amino acids.

Lysine, leucine, phenylalanine, and tryptophan are all considered essential amino acids—meaning the body cannot synthesize them on its own and they must be acquired through food or supplements. Leucine, for example, can be found in abundant quantities in cheese, soybeans, chicken, nuts, seeds, and seafood.

The branched-chain amino acids (BCAAs)—leucine, isoleucine, and valine—have particular relevance for keto dieters engaged in physical training, as they can help reduce exercise-related muscle damage, muscle soreness, and fatigue during exercise. However, many studies show that the most benefit can be derived from a well-formulated essential amino acid supplement rather than individual amino acid supplements.

For more information on the best amino acids to take to complement a keto diet, check out this article.

2. Beta-Hydroxybutyrate (BHB)

Beta-hydroxybutyrate (BHB) supplements, sometimes referred to as exogenous ketones, may be able to elevate ketone levels, among other desirable benefits.

As we’ve discussed, your body naturally produces ketone bodies through a process called ketogenesis. Some experts believe that exogenous ketones from an external source can increase your blood ketone levels, helping you reach a state of ketosis more quickly.

There’s also some evidence to show that BHB supplements can counteract the fatigue and mood swings that some experience when they start the keto diet. Once you’ve entered ketosis, studies show that these same supplements may help to enhance athletic performance, decrease recovery time between training sessions, and lower appetite levels.

Some general guidelines for a starting dosage for BHB supplements would be to take either 2 BHB oil capsules daily or 1 scoop of BHB oil powder on an empty stomach between meals with 16 ounces of water. You should limit yourself to three such doses per day.

Some individuals experience stomachaches when taking BHB supplements. If you experience digestive upset, try lowering your intake, then gradually increase to the ideal dose.

3. Medium-Chain Triglycerides (MCTs)

Medium-chain triglycerides (MCTs) can be an ideal tool for keto dieting. These fatty acids are used to form ketones in the liver, and supplementing with MCT oil can help you feel more satiated during the ketosis transition.

Keto-friendly coconut oil is a rich natural source of medium-chain triglycerides, although it provides a far less concentrated dose of MCTs than expressly manufactured MCT oils.

MCTs and amino acids work together synergistically. The presence of amino acids in the body supports the essential metabolic process by which the fatty acids are transformed into ketones, and a study published in the journal Comparative Biochemistry and Physiology determined that dietary fat, especially medium-chain fats, helps to regulate amino acid transport.

As researchers study these unique compounds found in healthy dietary fats, they continue to add to the long list of health benefits associated with an increased intake of MCTs, including:

  • Increased fat burning during athletic activity
  • Bolstered growth of good gut flora
  • Lowered cardiovascular risks
  • Protection against neurodegenerative disorders such as Alzheimer’s disease
  • Increased antibacterial, antiviral, and anti-fungal activity

As with BHB supplements, MCT oil supplements, such as these softgels, should be taken with water—in this case, at least an 8-ounce glass. Only one daily dose is needed.

Consistently following a comprehensive ketogenic diet, otherwise known as the keto diet, is an effective way to lose weight and keep it off. Taking amino acids along with following a keto diet can expedite the metabolic processes responsible for ketogenic weight loss.