Foods That Are Rich in Sulfur and Why You Should Be Eating More of Them

A diet that contains sulfur-rich food is necessary for keeping connective tissue flexible and helping the body detox and metabolize food. Get enough sulfur by eating a protein-rich diet that includes Brussels sprouts, kale, meat, and eggs.  

As an essential mineral found in proteins and the amino acids cysteine and methionine, sulfur is a critical nutrient for the human body. Sulfur is most likely known best for its sulfur compounds, which give garlic its distinctive aroma, cause tears when chopping onions, and lend a funky smell to urine, but sulfur does so much more. The mineral stabilizes and shapes some protein structures, aids in metabolism and detoxification, and keeps connective tissue and cartilage supple, making it essential that our diets contain sulfur-rich foods.

Good Sources of Sulfur-Rich Foods

Sulfur doesn’t discriminate by diet. Whether you’re a meat lover or a plant-based eater, there’s a wealth of sulfur-rich foods to choose from.

Meat, Fish, Poultry, and Other Proteins

Building and maintaining healthy skin, nails, and hair depend on protein-rich foods, such as fish, poultry, meats, nuts, and legumes. Packed with protein, eggs are also an optimal source of sulfur, which is found in both the egg yolk and the white, although sulfate content is higher in egg whites.

Protein-rich foods contain sulfur in the form of the amino acids cysteine and methionine. These amino acids provide the amounts of sulfur our cells need to function properly. In addition to helping make protein, sulfur serves as a cofactor for enzymes that result in chemical reactions.

Cruciferous Vegetables

Many fibrous, often green and non-leafy vegetables fall into the category of sulfur-rich vegetables. Cruciferous vegetables, such as wasabi, horseradish, cabbage, kale, bok choy, Brussels sprouts, and cauliflower, pack a punch when it comes to nutrients.

Brussels sprouts, asparagus, and legumes also are very high in methylsulfonylmethane (MSM), which provides a major source of sulfur. Additionally, these cruciferous veggies provide healthy doses of fiber, vitamins C, E, and K, folate, and carotenoids, as well as the sulfur-containing chemicals known as glucosinolates. Thank these chemicals for the bitter flavor and distinctive, pungent aroma that set cruciferous vegetables apart from so many others. When glucosinolates break down, for example during digestion, they form compounds, including indoles and isothiocyanates. Researchers have studied these specific compounds most often for their anti-cancer effects. Studies have shown that the compounds, indoles, and isothiocyanates can have antiviral and antibacterial effects, as well as anti-inflammatory properties.

Alliums

Other foods high in sulfur include allium vegetables, like leeks, garlic, chives, and onions. They contain organic compounds that contain sulfur, and studies in animals have shown that these vegetables may help prevent esophagus and colon cancers. Though more clinical trials need to be performed to determine their efficacy in humans, this research shows that the cancer-fighting potential of alliums warrants further exploration.

Stay healthy with a sulfur-rich diet.

Understanding Amino Acids

Most commonly referred to as the building blocks of protein, amino acids assist in many biological functions. There are 20 amino acids in protein. Nine of them are essential, which means we must get them through nutrition because our bodies don’t produce them on their own. Since our bodies do not store them, adults need to eat healthy diets to get these nine essential amino acids: valine, leucine, lysine, isoleucine, methionine, phenylalanine, tryptophan, threonine, and histidine.

The other remaining amino acids fall into the categories of nonessential and conditionally essential. Nonessential amino acids are naturally occurring in our bodies, and we can also get them from the foods we eat. Alanine, asparagine, and aspartate are examples of nonessential amino acids.

Arginine, glutamine, tyrosine, cysteine, glycine, proline, serine, and ornithine are both nonessential and conditionally essential. This means our bodies synthesize them, but during times of sickness or stress, we may not be able to produce the amount we need. In those instances, we must ensure our amino acid needs are met through our diets or with supplementation.

Only two amino acids, methionine and cysteine, contain sulfur. Methionine is critical for good health because it is required to build proteins and produce many molecules in the body, including SAM, which is used to modify DNA. Methionine also plays a critical role in many cell functions and helps prevent liver damage in acetaminophen poisoning.

Why the Consumption of Sulfur Foods Matter

In addition to providing strength and resiliency to hair, sulfur assists in many other biological processes.

Sulfur is needed to synthesize the tripeptide glutathione, which is a chain of three amino acids that is joined by two peptide bonds. Not only is glutathione a key antioxidant, but it also regulates a number of cellular processes. It helps to control the rapid production of cells, aids in the detoxification of foreign organisms and free radicals, and influences immune function.

Sulfur is integral in binding together the two chains of amino acids that form the hormone insulin, which regulates our bodies’ sugar use. Taurine synthesis also depends on sulfur. Taurine is an organic compound that contains sulfur and plays an important role in metabolizing fats, restoring insulin sensitivity, and supporting the general functions of muscles and the central nervous system.

How Much Sulfur Do We Need?

The recommended dietary allowance set forth by the Food and Nutrition Board of the National Research Council/National Academy of Sciences for methionine plus cysteine is 14 mg/kg of body weight per day. Regardless of age or sex, a person weighing 70 kilograms would need to consume about 1.1 grams per day.

Who Suffers from Low Sulfur Levels

Though sulfur is one of the most abundant minerals in our bodies and many foods contain the mineral, we can suffer from low sulfur levels. First, the American diet often includes many processed foods and carbohydrates, and not many high-protein foods. A low-protein diet can result in low sulfur levels. Sometimes, those who eat little or no protein from animals, such as vegetarians and vegans, also may have lower amounts of sulfur in their systems.

Even when we eat balanced diets, we may not have the sulfur content levels we expect. Overcooking sulfur-rich foods can compromise their nutrition, negatively impacting the amount of the mineral our bodies get. Also, industrialized farming practices impact the levels of sulfur in the soil where crops grow. The bottom line is that if we are not buying and consuming local, organic produce or acquiring our meat and produce from grass-fed animals, there’s a very great chance we are not getting the essential vitamins and minerals our bodies need.

Top 24 Vegetarian Protein Sources

The top 24 vegetarian protein sources, including a list of valuable complete proteins, and information on the unique health benefits each food provides to the human body.

The quest for vegetarian protein sources is an important one. Protein and amino acid deficiency can lead to muscle loss, delayed healing, difficulty concentrating, and increased levels of depression and anxiety. When your body’s lacking what it needs, you won’t feel right, and you’ll know it.

This is why it’s important to make sure you get the protein intake you need from a vegetarian diet. Incomplete proteins like whole grains, produce, and nuts can do the job in concert with one other, but there are some foods that contain all nine essential amino acids required for proper human functioning: complete proteins.

We’ve assembled a list of the best vegetarian proteins below. Any of these foods will help ward off the symptoms of protein deficiency, but the complete protein foods listed at the end are for those who want to do some one-stop shopping when it comes to their amino acids intake.

Top 24 vegetarian protein sources.

Nuts and Seeds

We’ve compiled some of the healthiest and handiest snacks around.

1. Hemp Seeds

Rich in omega-3 fatty acids, hemp seeds are a protein source that can aid against obesity, metabolic syndrome, and heart disease. Hemp seeds are small sources of fiber that can be easily added to just about any food—stirred into oatmeal, blended into a protein shake or smoothie, or even sprinkled onto a salad. With 3.3 grams of protein per tablespoon, this is an easy ingredient to include in the foods and meals you already eat.

2. Almonds

Full of the amino acid arginine, almonds as a snack can contribute to healthy weight loss and fat burning, reduce the risk of heart disease, and curb hunger. With 6 grams of protein per ounce, almonds are also a source of nutrients that contribute to brain health, like vitamin E, folate, and carnitine, known for its neuroprotective benefits.

3. Cashews

Another conveniently healthy snack, cashews are an excellent resource for minerals like copper, manganese, magnesium, and phosphorus. With a fair amount of vitamin K, cashews also contain biotin, which is used for hair and nail health, and they have 5 grams of protein per ounce.

4. Pumpkin Seeds

Pumpkin seeds contain magnesium, phosphorus, zinc, antioxidants and 9 grams of protein per ounce. Containing the amino acid arginine, pumpkin seeds can help in situations of hair loss, and can be eaten raw or baked with added flavors like honey (for sweet) or garlic powder (for savory).

Beans and Legumes

Here are some hardy foods to add substantial protein to your diet.

5. Lentils

Lentils are a complete protein, but there’s a catch: they contain all nine essential amino acids, but they don’t contain sufficient methionine to meet ideal amino acid intake. Just 1 cup of lentils has 18 grams of protein, the same amount as three eggs. With a high-fiber content, lentils are filling when eaten and slow down digestion in a way that could help blunt spikes in blood glucose (a contributing factor to the development of type 2 diabetes).

6. Black Beans

With 39 grams of protein per cup, black beans are a heavy hitter in the protein department and a terrific way to meet your copper, manganese, vitamin B1, phosphorus, magnesium, and iron needs. Black beans are a great way to add valuable density to a pot.

7. Chickpeas

Chickpeas, also known as garbanzo beans, are legumes high in the amino acid lysine as well as fiber, iron, folate, zinc, phosphorus, and B vitamins. Just 1 cup of chickpeas has 39 grams of protein. Extremely popular in the form of hummus, when eaten with pita bread, that combined snack can become a complete protein.

Protein-Rich Grains

These modern and ancient grains are the staff of life.

8. Amaranth

An ancient grain that is naturally gluten free, amaranth offers up digestive fiber and calcium. Porridge-like when cooked, it is a particularly healthy replacement for or addition to morning cereal and oatmeal. It provides 9 grams of protein per cup.

9. Teff

A lesser-known ancient grain from the Ethiopian region, Teff is full of essential amino acids, vitamin C (quite unusual in a grain), and calcium. With 10 grams of protein per cup, again it could replace or enhance a bowl of oatmeal, a helping of grits, or a side of rice.

10. Triticale

Triticale is another whole grain (wheat-rye hybrid) with 24 grams of protein per cup and rich in iron, potassium, magnesium, and fiber. Triticale can be used instead of traditional baking flour in recipes.

Fruits and Veggies

Vitamin-rich vegetables and even some fruit can provide protein.

11. Spinach

With 5 grams of protein per cooked cup, spinach has almost the equivalent amount of protein as a hard-boiled egg (at half the calories). Eating spinach raw or steamed maintains the maximum amount of nutrients, namely high amounts of carotenoids, vitamin C, vitamin K, folic acid, iron, and calcium.

12. Tomatoes

Tomatoes contain lycopene, an antioxidant that may reduce your risk of bladder, lung, prostate, skin, and stomach cancers, as well as your risk of coronary artery disease. With 6 grams of protein per cup, tomatoes provide fiber and calcium and make a refreshing addition to many salads, sandwiches, and salsas.

13. Guava

This high-protein fruit has more than 4 grams of protein per cup. Along with fiber, guava has over 600% of your daily recommended vitamin C (about seven oranges worth). A brightly colored and delightfully zesty treat to include in any diet.

14. Artichokes

Artichokes are a good source of niacin, magnesium, potassium, copper, vitamin C, vitamin K, and folate. With about 10 grams of plant protein per cup, it has one of the highest protein yields among vegetables, and the artichoke has nearly twice the fiber of kale.

15. Peas

A high-protein food with 8 grams of protein per cup and nearly 100% of the daily recommended amount of vitamin C, peas add a tantalizing texture to salads and mashed potatoes. Of course, they’re also enjoyed as a side dish all on its own. You can even mash them up for baby food, or flavor that mash and use it as a veggie spread for your morning toast.

Complete Proteins

Here’s the good stuff, the protein sources that contain all nine essential amino acids needed in your diet.

16. Quinoa

With 8 grams of protein per cup, quinoa is an ancient grain with wide modern popularity, included in over 1,000 products on the market and regularly showing up in strange places (like wrapped around a sushi roll or pressed into a veggie burger). With a mild flavor, quinoa can be seasoned to a variety of taste preferences and is an excellent source of unsaturated fats and fiber. Along with the nine essential amino acids, quinoa also contains the amino acid L-arginine, shown to promote muscle over fat gain in animal studies (let’s hope that proves true for the most dangerous game animal of all: humans!). In fact, quinoa contains about a dozen amino acids, making it a wonderful alternative to carbs like couscous or rice.

17. Soybeans

Soybeans and soy products like tofu and soy milk all contain protein: steamed soybeans have 8 grams per cup, tofu 20 grams per cup, and soy milk 4 grams per cup. Soy foods offer cardiovascular benefits, help prevent prostate and colon cancer, decrease hot flashes for women in menopause, and guard against osteoporosis. Tofu particularly can be formed and flavored to fit a variety of recipes.

18. Buckwheat

With 6 grams of protein per cup, buckwheat is a gluten-free seed full of fiber (more than the amount found in oatmeal) and magnesium, a mineral that’s important to metabolism. Buckwheat is not a wheat but a versatile cousin of rhubarb that can nevertheless function as a pancake mix, be formed into Japanese soba noodles, or be eaten as porridge.

19. Ezekiel Bread

Sprouted bread or Ezekiel bread has 4 grams of protein per slice and is made with the sprouted grains and legumes wheat, barley, lentils, beans, spelt, and millet. It contains 18 amino acids, including all 9 essential amino acids, which is not even close to true for most bread products. With one sandwich on Ezekiel bread you can gain 8 grams of protein during lunch alone.

Fun fact: Ezekiel bread is named after this passage in the Bible from Ezekiel 4:9: “Take wheat, barley, beans, lentils, millet, and spelt, put them in one vessel and make them into bread for yourself.” Intended as a last resort to make bread when a besieged Jerusalem was running low on supplies, it turned out to be a fantastic recipe fit for modern times, and an extraordinarily nutritious food.

20. Spirulina

Used as a whole food or dietary supplement, the vibrantly green spirulina is a biomass of cyanobacteria that can be eaten by humans and other animals. With 4 grams of protein per powdered teaspoon, it also provides the B vitamins B1 (thiamine), B2 (riboflavin), and B3 (niacin), along with copper, iron, magnesium, potassium, and manganese. An odd taste at first, spirulina can nevertheless be added to a variety of foods for the bevy of benefits it provides.

21. Quorn

Developed in the U.K. in the 1980s from a fungus relative of mushrooms and truffles, Quorn is often used as a faux meat in the form of tenders, burgers, and lasagna filling. With over 20 grams of fiber per cup, this product contains all nine essential amino acids.

22. Peanut Butter

With 65 grams of protein per cup, peanut butter is a tasty protein source that can be made into cookies, sandwiches, included in smoothies, and used as a spread on crackers or celery (add some raisins to make the classic “ants on a log” snack). Peanut butter also contains healthy fats and could prevent both cardiovascular and coronary artery disease. Choose the unsalted kind, with no hydrogenated oils or sugars added, and have a guilt-free treat!

23. Chia Seeds

With 2.5 grams of protein per tablespoon, chia seeds don’t contain that much protein, but they can easily make up for it by providing all nine essential amino acids. Chia seeds can absorb moisture and become gel-like, making them a fun addition to pudding and smoothies, and the omega-3s in chia seeds can help reduce the risk of heart disease. They can be sprinkled over soups and salads, made into a chia seed pudding for dessert, and used as an egg replacement in vegan cooking recipes once they are fully hydrated.

24. Eggs

Speaking of eggs, this last item is for the ovo-vegetarians only, but too important to leave off the list entirely. Eggs are one of the most nutrient-filled protein sources around. With 6 grams of protein per egg, they contain the disease-fighting nutrients lutein and zeaxanthin and are a classic breakfast food whether they’re prepared scrambled, sunny side up, baked into a quiche, or separated to make an egg white omelet. Along with being versatile as their own main ingredient (egg salad, deviled eggs, etc.), eggs are also a great binding element for cauliflower pizza dough or egg-washing cookies before baking.

Plentiful Vegetarian Protein Sources

A protein deficiency doesn’t have to be a concern for those keeping to a vegetarian diet, and in fact, since plant-based sources of protein are so abundant, protein deficiency in vegetarian and vegan diets is actually quite rare. There are many ways to add enough protein to your diet that will support healthy weight loss, increase muscle mass, and improve your overall health and well-being.

On a deeper level, choosing complete proteins to include in one’s diet gets down to the cellular level of wellness, providing the nine essential amino acids that only come to humans via dietary intake. The more you know about what your food truly provides to the human body, the more precise your choices (and recipes) will become.

While animal proteins are higher quality in that they contain an adequate balance of the essential amino acids our bodies need, some plant proteins are low in essential amino acids such as methionine, tryptophan, lysine, and isoleucine. If you’re adhering to a plant-based diet, it’s a good idea to supplement with an essential amino acid blend to improve the balance of essential amino acids and nonessential amino acids, especially if you don’t want to have to think so hard about mixing and matching plant-based proteins to make them more complete.

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.

What Are Polar Amino Acids?

There’s more to amino acids than first meets the eye. There are actually two types: polar and non-polar. Here we uncover the polar amino acids and what they mean for you and your health.

When most people think of amino acids, they probably have a vague memory of their high school science teacher discussing the building blocks of protein. But did you know there are actually two types? Known as non-polar and polar amino acids, each group is classified according to its side chains—the shorter chains of atoms attached to the main chain, or backbone, of a molecule.

When amino acids join together to form proteins, only their side chain groups are exposed and able to interact with each other and their surroundings. And the shape of the protein—yes, proteins really do have shape—is determined mainly by the sequence of amino acids in that chain.

The non-polar groups are hydrophobic amino acids, which means they have side chains that are repelled by water. These amino acids are thus located in the protein core, safely tucked away from any contact with water.

In contrast, polar amino acids have hydrophilic side chains, which means they’re actually attracted to water and participate in hydrogen bonding with the highly polar water molecules. Because of this water-loving characteristic, these amino acids are generally located on the surface of proteins, in contact with the aqueous cell environment.

Interestingly, although the hydrophilic nature of polar amino acids means that they readily dissolve in water, they actually have the opposite reaction when placed in oil. In this case, instead of dissolving, the presence of the oil results in the amino acids being attracted to each other.

Which Amino Acids Are Polar?

There are many different amino acids, with over 300 known forms listed in the Practical Handbook of Biochemistry and Molecular Biology. However, only 20 are used to synthesize proteins.

These 20 amino acids are known as the common amino acids. Of these, 10 are considered polar. Including their three-letter codes, these amino acids are:

Arginine (Arg)
Histidine (His)
Asparagine (Asn) Lysine (Lys)
Aspartate (Asp) Serine (Ser)
Glutamine (Gln)
Threonine (Thr)
Glutamate (Glu)
Tyrosine (Tyr)

Contrast these with the non-polar amino acids, which are:

Alanine (Ala)
Phenylalanine (Phe)
Glycine (Gly) Proline (Pro)
Isoleucine (Ile) Tryptophan (Trp)
Leucine (Leu) Valine (Val)
Methionine (Met)

What Are the Properties of Polar Amino Acids?

The polar amino acids can be further broken down into neutral, basic, and acidic groups. And each of these categories functions in a different way.

1. Neutral Polar Groups

As the name suggests, neutral polar amino acids are neither basic nor acidic. This means that their side chains contain exactly one amino group and one carboxyl group (hence the name “amino acid”). The majority of amino acids, both polar and non-polar, are in fact neutral. Of the polar amino acids, asparagine, glutamine, serine, threonine, and tyrosine are neutral.

2. Acidic Polar Groups

If the side chain contains an extra element of carbolic acid, the amino acid becomes acidic. Aspartate and glutamate are acidic amino acids. These forms are also known as aspartic acid and glutamic acid, respectively. The aspartate and glutamate types are the anions, or negatively charged ions, of these substances.

3. Basic Polar Groups

If the side chain contains an extra nitrogen group, the amino acid becomes basic. Arginine, histidine, and lysine are basic amino acids and have a positive charge.

Group Polarity

The degree of polarity is also determined by the functional groups—the groups of atoms that dictate the chemical behavior of a compound—contained in the side chains. In the case of polar amino acids, this refers to the various combinations of amide and carboxylic acid groups that interact to create the neutral, acidic, and basic forms.

What Role Do Polar Amino Acids Play?

Like the rest of the common amino acids, the neutral, acidic, and basic polar groups all perform important functions in the body. Some of these include:

Polar amino acids for optimal health.

More to Learn

You may have noticed that we mentioned 20 common amino acids earlier but listed only 19. While it may have looked like we were bad at math, we promise we really knew what we were doing when we left cysteine (Cys) out of our lists.

You see, cysteine is classified as only slightly polar and thus doesn’t fit well into either the polar or non-polar category.

In fact, where amino acids are concerned, researchers continue to disagree on several points, including whether certain forms should be considered polar or hydrophilic.

So, as you can see, even though we’ve come a long way in our understanding of amino acids and the important roles they play in the human body, we still have more to learn before we can say we’ve truly mastered all the intricacies of these essential building blocks of life.

Aromatic Amino Acids Explained

Everything you need to know about the three aromatic amino acids—the science and history behind the aromatic amino acids that are essential to your health.

Aromatic amino acids: what are they exactly? What makes them aromatic? (Do they smell good, like perfume or brewing coffee? Quick answer: no.) How were they discovered and why do they matter to your health? Find the answers to these questions and more in this article.

Amino Acids: The Basics

We’ll start by outlining the basics of amino acids: how they were first detected, when they became understood as important components to the chemistry of the human body, and what we know (and continue to discover about them) today.

The History of Amino Acid Discovery

The history of the discovery of amino acids dates back to the 19th century. In 1806, French chemists Louis-Nicolas Vauquelin and Pierre-Jean Robiquet identified what they called asparagine, the first known amino acid, which they’d isolated from asparagus (thus the name).

Cystine was next recognized and isolated by English physician and chemist William Hyde Wollaston in 1810, as he studied patients with bladder stones: cystine comes from the Greek kystis, meaning “bladder pouch.” While this amino acid was found early in the century, cystine was not recognized as a major protein component until the very end of the 1800s. Even later than that, scientists further broke down its composition and designated the amino acid cysteine (two cysteine molecules bound together form cystine).

According to the Historical Encyclopedia of Natural and Mathematical Sciences, Volume 2, these major units of the molecular protein structure were discovered in the following order: glycine (1820), leucine (1820), tyrosine (1849), serine (1865), glutamic acid (1866), aspartic acid (1868), phenylalanine (1881), alanine (1888), lysine (1889), arginine (1895), histidine (1896), cystine (1899). By the 20th century, experts had a pretty good understanding of amino acids.

The building blocks of protein, 20 amino acids make every protein your body needs, linking them together and folding them over in different chains and combinations. Just as the 26 letters of the alphabet can make every word in the English language, that is the level of ordered complexity with which our bodies organize amino acids.

It is interesting to note that two extremely rare amino acids have been newly discovered, selenocysteine and pyrrolysine. They are known as the 21st and 22nd amino acids in the genetic code, with selenocysteine discovered in 1986 (mainly responsible for selenium transport), and pyrrolysine discovered in 2002 (an ɑ-amino acid used in the biosynthesis of proteins and not present in humans).

While scientific advancement carries on, the main 20 amino acids can be further categorized for our purposes as essential vs. nonessential.

Amino Acids: Essential vs. Nonessential

Let’s quickly name, explain, and clarify the 20 standard amino acids that are hard at work in the human body.

Nonessential

Nonessential amino acids are amino acids you absolutely still need, but because they are produced naturally in the body, you don’t have to eat or otherwise acquire them. Of the main 20 amino acids, there are 12 nonessential amino acids. They are as follows (with descriptions sourced from PubChem):

  1. Alanine: used for protein construction and metabolizing tryptophan and vitamin B6 (pyridoxine).
  2. Asparagine: a carrier of residual ammonia to be eliminated from the body (in case you ever wondered why urine sometimes smells like asparagus).
  3. Aspartate: found in animals and plants (especially sugar cane and sugar beets), it may be a neurotransmitter.
  4. Cysteine: an important component of hair, skin, and nails.
  5. Glutamate: the most common excitatory neurotransmitter of the central nervous system.
  6. Glutamine: involved in many metabolic processes, it’s the main carrier of nitrogen throughout the body.
  7. Glycine: a fast inhibitory neurotransmitter.
  8. Proline: synthesized from glutamic acid, an essential component of collagen important for the proper functioning of joints and tendons.
  9. Serine: involved in the biosynthesis of purines, pyrimidines, and other amino acids.
  10. Tyrosine: synthesized in the body from phenylalanine, also the precursor of epinephrine, thyroid hormones, and melanin.
  11. Arginine: a semi-essential amino acid, boosts the production of nitric oxide, also an important intermediate in the urea cycle and the detoxification of nitrogenous wastes.
  12. Histidine: an essential amino acid, necessary in the production of the neurotransmitter histamine.

Semi-Essential

Now might be a good time to discuss semi-essential or conditionally essential amino acids, such as arginine. Arginine is only essential for juveniles, but is nonessential at later stages of development, unless the body is under siege from stressors such as illness and surgery, which can compromise the production of conditionally essential amino acids like arginine.

Tyrosine too is considered semi-essential. It is synthesized only from phenylalanine, which is itself an essential amino acid. However, a lack of the enzyme phenylalanine hydroxylase (which is used in tyrosine synthesis) can cause phenylketonuria (PKU), also known as phenylalanine hydroxylase (PAH) deficiency. It is a disorder that causes a buildup of phenylalanine in the body. Without the necessary enzyme to process phenylalanine (and thus gain tyrosine), people with PKU must limit the foods they eat that contain protein, as well as the artificial sweetener aspartame. If the buildup of phenylalanine is not properly managed, it can lead to severe health problems including mental and behavioral issues, intellectual disabilities, and seizures. PKU patients have low levels of tyrosine as a result, and will sometimes need to take a tyrosine supplement. If there is an issue with processing the essential amino acid phenylalanine—which under ideal circumstances would naturally produce tyrosine—that is the condition under which tyrosine would become an essential amino acid for the individual.

Essential

The nine remaining amino acids are essential, meaning they need to be acquired from outside the body in order for the human body to function. If not by food, then possibly by supplement, but whatever the way, they must be taken in to gain their benefits.

  1. Isoleucine: an isomer of leucine, important in hemoglobin synthesis and regulation of blood sugar and energy levels.
  2. Leucine: important for hemoglobin formation and an initiator of muscle protein synthesis.
  3. Lysine: required for growth and tissue repair and supplied by foods such as red meats, fish, and dairy products.
  4. Methionine: a sulfur-containing essential L-amino acid that is important in many body functions like tissue repair, detoxification processes, protecting cells from pollutants, preventing excess fat buildup in the liver, and the tone and pliability of skin, hair, and nails.
  5. Phenylalanine: used in the biosynthesis of dopamine and norepinephrine neurotransmitters.
  6. Threonine: an important residue of many proteins, such as tooth enamel, collagen, and elastin that is found in eggs, milk, gelatin, and other proteins.
  7. Tryptophan: necessary for normal growth in infants and for nitrogen balance in adults.
  8. Valine: promotes muscle growth and tissue repair, also a precursor in the penicillin biosynthetic pathway.

That’s the rundown of amino acids, so now: which ones are aromatic, and what makes them so?

Aromatic Amino Acids: The Specifics

Out of all the above listed amino acids, which ones are aromatic, and why does that matter? Let’s start with what “aromatic” means in this biological context.

Aromatic Defined

To a layperson, this word means “having a pleasant and distinctive smell.” Fragrant, sweet-scented, perfumed. In chemistry however, it speaks of an organic compound, a large class of unsaturated compounds characterized by one (or more) planar rings of atoms joined by covalent bonds of two different kinds.

The Aromatic Amino Acids

There are three aromatic amino acids (AAA): phenylalanine (Phe); tyrosine (Tyr), derived from phenylalanine; and tryptophan (Trp).

Everything you'd want to know about aromatic amino acids.

You’ll notice the distinctive aromatic ring on the side chain of each of these three amino acids. Each of those rings has three double bonds, a clear characteristic of aromatic amino acids. What’s even more distinctive about them is that while amino acids don’t absorb light in the visible region of the electromagnetic spectrum, they do all absorb light from the infrared region thanks to their double bonds. And the aromatic amino acids specifically? They absorb ultraviolet radiation, or UV light.

Ultraviolet Rings

To a different degree, all aromatic amino acids absorb ultraviolet light.

Measured in wavelengths via nanometers (nm), tryptophan has the highest absorption of ultraviolet light (280 nm) by proteins, with tyrosine high as well (above 250 nm), and phenylalanine the lowest (but still significantly above 210 nm).

This absorption ability is used to quantify the concentration of proteins in an unknown sample. It causes the electron of each to enter an excited state, and when that electron returns to its ground state, it will either release energy or emit light. If the molecule emits light, it is called a fluorescent molecule. Tryptophan is a widely used fluorescent molecule.

Tyrosine further distinguishes itself as the only one of the aromatic amino acids with an ionizable side chain. Seven out of the 20 amino acids contain ionizable side chains, meaning that their side chains can exchange a hydrogen atom with some other biomolecule in certain circumstances.

Not Just for Humans

Animals (including us humans) get our essential aromatic amino acids from the food we eat, but plants and microorganisms (like fungi, bacteria, algae, and some protozoans), must synthesize them through the shikimate pathway.

Found only in microorganisms and plants, the shikimate pathway is a seven-step aromatic amino acids and carbohydrate metabolism route. It was studied extensively via the Arabidopsis thaliana plant (commonly known as thale cress or mouse-ear cress), the findings of which were detailed in a paper titled “The Biosynthetic Pathways for Shikimate and Aromatic Amino Acids in Arabidopsis thaliana,” published in The Arabidopsis Book.

The shikimate pathway begins with the formation of chorismate in plants, the precursor of tyrosine, tryptophan, and phenylalanine. As it is for us, the aromatic amino acids are essential to a plant’s biological functions. In fact herbicides often inhibit the enzymes involved in the plant’s biosynthesis of aromatic amino acids, which is what makes those poisons toxic to the organism’s biological functions.

What Do the Aromatic Amino Acids Do for You?

You may be saying to yourself, having read or skimmed this far, “That’s all well and good, but now that I know what they are and how they’re classified, what do the three aromatic amino acids actually do for me?”

That’s a great question! Let’s take an in-depth look at each one:

Phenylalanine

Phenylalanine exists naturally in two forms: L-phenylalanine and D-phenylalanine (there is also a laboratory-made mixture called DL-phenylalanine or DLPA). Nearly identical save for their shape (you might guess they are shaped more or less like an L and a D), the L-form is the essential amino acid found in food and used for protein-building in the body. The D-form is a non-protein amino acid still being studied for its uses and effects, particularly in the areas of pain, stress, and mood disorders like depression and anxiety.

Phenylalanine is found in soy foods, cheese, seeds, nuts, lean meats, poultry, and seafood. While it’s dangerous for people with PKU or PAH deficiency (as discussed previously in this article), it is so essential to human life that phenylalanine supplements might be recommended to people in need of a therapy for depression, or to curb the effects of drug and/or alcohol withdrawal. That is because phenylalanine is the key to producing dopamine, the molecule in your brain that allows you to feel pleasure and form memories.

Phenylalanine has been studied in connection with the therapeutic treatment of Parkinson’s disease, as a possible treatment for children with ADHD, and as an alternative treatment for vitiligo. Vitiligo is a disorder characterized by the patient losing pigmentation on patches of their skin, a condition that theoretically could be helped by phenylalanine’s connection to proper melanin production.

Perhaps the best part about phenylalanine as a potential treatment is that, because it’s an essential amino acid already irreplaceable in the human body, experimenting with it causes little-to-no side effects or adverse reactions. It’s like oxygen or water—yes, it’s still possible to have too much of any one, but it takes a very unusual or drastic circumstance to bring about harm, and the rest of the time there is simply no life without it.

Speaking of a bare necessity for life, phenylalanine is also crucial for the production of epinephrine and norepinephrine, the vital components of the body’s “fight-or-flight” response mechanism—it could literally save your life in a crisis.

As the first ingredient for the creation of tyrosine, phenylalanine is in essence the key to two important amino acids in the body. We’ll delve further into tyrosine’s uses next.

Tyrosine

Tyrosine is derived naturally in the body from phenylalanine, and thus is usually considered nonessential as long as there is no issue with phenylalanine processing. However, tyrosine can also be ingested, and is found in eggs, dairy products, meats, fish, beans, nuts, and wheat.

From the Greek word tyros, meaning “cheese,” which is where it was first discovered, as a supplement it is most commonly used to treat PKU, and also in situations to improve alertness, memory creation/retention, and learning ability. That is because tyrosine produces chemicals for the brain that help nerve cells communicate with one another. Tyrosine may even have a hand in regulating mood, improving focus, and influencing other facets of cognitive functioning.

Tyrosine is also a key player in protein synthesis, the fundamental function that keeps us alive. Like phenylalanine before it, tyrosine has been studied in the management of stress, the improvement of mental performance during times of stress, and issues of sleep and wakefulness.

Tyrosine also has a huge role to play with the thyroid gland, which extracts iodine from the foods we eat, combines it with tyrosine, and thus produces the two primary thyroid hormones thyroxine (T4) and triiodothyronine (T3). Those hormones are important for maintaining the body’s metabolic rate, heart and muscle function, brain development, digestion, and the maintenance of bones. Supplementation with tyrosine can sometimes be used in the treatment of hypothyroidism, a condition cause by an underactive thyroid, but should not be taken casually or without expert advice from a doctor or trusted medical professional.

The benefit of tyrosine being a natural inhabitant of the body is that it’s often a safe therapy for a variety of clinical conditions, including hypertension and chronic pain, but as with any supplementation or treatment, it’s important to seek medical advice before experimenting independently on oneself.

Tryptophan

Tryptophan is needed in infants to facilitate normal growth, and in adults for ensuring there is a balance in the breakdown and synthesis of protein. It can be found in seeds, spinach, salmon, poultry, eggs, soy products, and nuts.

Tryptophan is well known as being a precursor of serotonin, the neurotransmitter that helps regulate anxiety, reduce depression, heal wounds, and maintain bone health. Serotonin is also a component of digestive health (and indeed is largely found in the digestive system), as well as being the chemical that stimulates the parts of the brain that control wakefulness and sleep.

Tryptophan’s connection to food and sleep is so famous that it was even the topic of a Seinfeld episode, where feeding someone turkey is so effective at inducing slumber, the person falls asleep immediately after she finishes eating turkey for dinner.

There is a disorder that particularly affects tryptophan too: Hartnup disease, also known as Hartnup disorder or pellagra-like dermatitis. It is a metabolic disorder that disrupts the absorption of nonpolar amino acids (which include tryptophan and phenylalanine). Often the only sign of this disorder is aminoaciduria, or a high level of amino acids in the urine, since they are not being properly absorbed by the body. However in more extreme cases, people with Hartnup disease will exhibit possible skin rashes (hence the dermatitis designation), difficulty in coordinating their movements, and even psychiatric symptoms like depression or psychosis. Those extreme reactions are usually flare-ups caused by stress, poor diet, or illness, but it is otherwise a manageable condition. The worst symptoms could very well be due to the inhibition of tryptophan—an upset to serotonin levels in humans can lead to quite precarious mental states, and as a result, sometimes terribly dire depressive outcomes.

The Bouquet of Life

The metabolism of aromatic amino acids phenylalanine, tyrosine, and tryptophan is essential to human life. While it’s tempting to know that elements so important are so easy to get access to, when seeking to boost one’s intake of these amino acids, it’s even more important to be well-informed and carefully balanced. Not only do all of the amino acids work in concert with one another, but the resulting byproducts and response they produce are not to be trifled with lightly.

It’s been posited (mostly in jest), that due to the way our brains work, dopamine and serotonin are the only two things we truly enjoy. Everything we love doing, we love because of the chemical reaction it causes in our brains. Because the aromatic amino acids specifically are direct keys to our dopamine and serotonin, we must love them too.

Is Quinoa a Complete Protein? It May Just Be the Missing Link in Your Diet!

It can be hard for vegans and vegetarians to find complete proteins that meat and fish eaters source with ease. Enter Quinoa (KEEN-wah), a complete protein that some hail as a supergrain.

Vegetarians, vegans, and even the meatless Monday crowd crave the same quality nutrition that the carnivore next door gets without breaking a sweat. Which leaves many of us wondering, is quinoa a complete protein? While it’s not difficult to get garden-variety nutrients in a plant-based diet, it can be a challenge to source the complete proteins found in animal products. Enter quinoa (KEEN-wah), a complete protein source that some hail as a supergrain.

We need 20 amino acids in different combinations to create the proteins that fuel our cells and power our lives. For instance, your heart is made of 95% amino acids. But our bodies alone can only create 11 of them. The other nine essential amino acids must come from what we eat, and quinoa is one of the plant sources that supplies each of these “building blocks of life.”

Is Quinoa a Complete Protein?

Quinoa is technically not a grain, but a seed. Regardless of classification, it’s enjoyed much like other grain-based foods.

While most whole grains have some amino acids, they tend to lack the amino acid lysine or contain only trace amounts of it and don’t deliver enough protein to sustain our essential amino acid requirements. The amino acid profile of quinoa, however, can be considered complete.

Quinoa offers up a good amount of lysine and the other eight essential amino acids to help support our bodies’ amino acid needs. And research shows that the digestion of quinoa protein is comparable to that of other high-quality protein foods.

Here’s the possible catch: quinoa appears to be a high-quality protein, but that is in terms of quinoa protein isolate, which is actually of low quantity in quinoa seeds. The amino acid profile of quinoa is, for instance, significantly inferior to specially formulated essential amino acid mixtures. So, by all means, add quinoa to your diet to feed your body the essential amino acids it craves, but, if you are concerned that you aren’t meeting your protein needs, then consider supplementing with essential amino acids according to your nutritional needs.

Is quinoa a complete source of protein?

The protein in quinoa far surpasses the protein content of its grainy competitors. Take incomplete proteins such as rice and barley, for example. One cup of quinoa contains 8 grams of protein, while brown rice has only 5 grams, and barley less than that at 3.5 grams.

Is quinoa a complete protein?

On par with rice and couscous, quinoa has a nutty taste with a slight toothsomeness. For a savory approach, some toss in bay leaves, thyme, garlic powder, and other herbs and spices, while the breakfast crowd might like it a bit sweeter, boiling it with milk, stirring in fruits and nuts with a dash of cinnamon or nutmeg. You can add quinoa to soups, salads, and stir-fries, or pop it like popcorn. Here are some recipes to try.

Harvest from an Ancient Table

A seed that comes to us courtesy of Peru, Bolivia, and Chile, quinoa means “the mother grain” in its original South American tongue, and dates back thousands of years. It was also called  “The gold of the Incas” because, with a belly full, warriors as old as 50 had the fortitude to scale the Andes, fight amid the harsh terrain, and vanquish their enemies.

Though this superfood remained a secret tucked away in a distant land for millennia, word has gotten around. These days quinoa crops are sprouting up in North America, China, France, and India with production picking up in Africa and the Middle East. There are 1,800 types of quinoa in a rainbow of colors, but only a few made the leap to the U.S. The white variety is milder, while the red and black boast more nutrients. The harvested seeds of Chenopodium quinoa undergo processing to remove natural saponins, a bitter-tasting husk that acts as a natural pesticide to the maturing plant.

A Cornucopia of Nutritional Goodies

Apart from being one of the best sources of protein, quinoa has small amounts of omega-3 essential fatty acids, is non-GMO, and is usually organically grown, which makes it a good find. Astronaut Samantha Cristoforetti took a selfie with her pouch of quinoa aboard the International Space Station. She chose this plant protein as one of her “bonus foods,” pairing it with mackerel. Quinoa’s also held in lofty esteem by NASA scientists, who’ve explored growing it in outer space, as it reproduces and stores well, while offering nutritional bang for the buck. Aside from protein, which supports muscle, hair, collagen, enzymes, and antibodies, and fiber that helps our bodies absorb nutrients, quinoa is a strong source of:

  • Manganese (58% of the RDA): A friend to the brain, nerves connective tissue, bones, blood, hormones, and metabolism.
  • Magnesium (30% of the RDA): Gets the biochemical party started and helps with energy production.
  • Phosphorous (28% of the RDA): Teams up with calcium to give strength and structure to bones and teeth.
  • Folate (19% of the RDA): A B vitamin that hooks up with your DNA chain and percolates other genetic material.
  • Copper (18% of the RDA): Links up with iron to help form red blood cells and keep blood vessels, nerves, immune system, and bones ticking like the Swiss.
  • Iron (15% of the RDA): Important for healthy blood and transfer of oxygen from lungs and tissues.
  • Zinc (13% of the RDA): Big on cell division, cell growth, wound healing, and the breakdown of carbohydrates. If you can smell and taste, thank zinc.
  • Vitamins B1, B2, and B6 (more than 10% of the RDA): The Bs power energy level, brain function, and cell metabolism.
  • Potassium (9% of the RDA): Regulates fluid balance, muscle contractions, and nerve signals. A diet rich in potassium may help reduce blood pressure and water retention, and help prevent stroke, osteoporosis, and kidney stones.

Is quinoa a complete source of protein?

 

Fighting Disease Like an Incan Warrior

There’s a saying: Fruit doesn’t fall far from the tree. And while quinoa is mainly known for the ways it supports body function, it’s increasingly becoming appreciated—in the never-say-die spirit of its Incan ancestry—for its warrior-like attributes and health benefits.

Antioxidants? Check!

Quinoa ranks high in antioxidants, which help neutralize free radicals in the body. Free radicals are believed to contribute to aging and certain diseases. A study looked at antioxidant levels in five cereals, three pseudo-cereals, and two legumes, and found quinoa to have the highest antioxidant content of them all. When added to gluten-free goods, quinoa enhanced their polyphenol content, helping to stave off certain cancers, osteoporosis, and other unwanted health effects.

Quinoa May Boost Metabolism

A study published in the European Journal of Nutrition showed that using quinoa instead of typical gluten-free breads and pastas significantly reduced blood sugar, insulin, and triglyceride levels. And research with rats indicated that quinoa in a diet high in fructose almost completely inhibited the negative effects of the fructose.

Good for Low Glycemic Diets

The glycemic index measures how foods raise your blood-sugar levels. Foods that are high on the glycemic index can stimulate hunger and lead to overeating and obesity. Obesity can be a culprit in type 2 diabetes and heart disease. Quinoa has a glycemic index of 53, which is considered low and can be an ally in blood sugar control.

Feel Fuller, Eat Less

Quinoa has been associated with weight loss by boosting metabolism and reducing appetite, possibly because its high-fiber content may increase feelings of fullness, causing one to eat less, though more research is needed to help scientists better understand quinoa’s effects on metabolism.

A Hedge Against Diabetes

Studies of Peruvian grains and legumes found that quinoa, its cousin kañiwa, and other traditional crops from Peru’s Andes have the potential to manage type 2 diabetes and associated hypertension.

Putting the Kibosh on Cholesterol

High in soluble fiber, quinoa can help bring down blood sugar levels, lower cholesterol, and increase a sense of fullness, which can, potentially, help with weight loss.

Highly Regarded, but No Halo

Quinoa attributes are undisputed, but even with a glycemic index of 53, it is somewhat high in carbs, and not as well-suited to a low-carb diet.

Another potential hitch is quinoa’s naturally occurring phytic acid, which can make it harder for the body to absorb all of its rich minerals. Soaking and/or sprouting the seed prior to cooking can reduce that effect. Other than that, though, it’s pretty hot stuff. In fact, leaders are looking at mass-produced quinoa as a way to feed the world as the effects of climate change take hold. Given its high level of genetic diversity, quinoa crops are highly resilient to extremes in soil, rainfall, temperature, and altitude, and tolerant to frost, drought, and salinity, according to a 2016 report.

So, if you haven’t already, maybe it’s time to up your protein intake and add some quinoa to the menu.

What You Should Know About How Amino Acids Benefit Liver Health

Before we dive into the fascinating ways that amino acids benefit liver health, let’s provide some context on just how dire the consequences of not paying attention to the health of your liver can be.

There are more than 4.9 million diagnosed cases of chronic liver disease in the United States, based on statistics shared by the Centers for Disease Control and Prevention (CDC). Of those cases, 40,545 end in death.

According to the American Liver Foundation, “Anything that keeps your liver from doing its job may put your life in danger.” There are many different factors that can interfere with liver function, such as…

  • A viral infection
  • Chemical injury
  • A misfiring immune response

Regardless of the underlying cause, the central danger is the same: that your liver will become too damaged to function at the level necessary for you to remain alive. And no matter what set it off, liver damage and disease tends to progress along a familiar path.

Learn about how amino acids benefit liver health.

What Causes Liver Disease?

One of the factors that spurs the progression of liver disease is that a protein called Bcl-xl begins to malfunction, failing to control the release of a second protein called cytochrome C, which occurs when a liver cell dies.

The release of cytochrome C triggers a cascade reaction in the liver which ultimately results in liver scarring—what medical professionals refer to as “hepatic fibrosis”—and instigates the development of chronic liver disease.

When it comes to uncovering methods for preventing liver disease and protecting the health of the liver, finding ways to ensure the Bcl-xl protein functionally regulates cytochrome C is a major priority. And exciting new research indicates that branched-chain amino acids (BCAAs) may be able to do exactly that.

In order to understand how amino acids protect your liver, it’s important to understand how the liver processes amino acids.

How the Liver Processes Amino Acids

Did you know that your liver is the largest organ in your body? Given that, it’s hardly surprising how many essential functions the liver carries out. Not only does your liver detoxify your blood, but it also processes nutrients and produces lipids, carbohydrates, and amino acids.

Your liver produces a variety of proteins, such as albumin and fibrinogen, two of the major plasma proteins that are responsible for many vital tasks. Albumin keeps your blood volume balanced and transports essential amino acids throughout the body, while fibrinogen ensures your blood clots properly.

One of the primary functions of the liver is to process the amino acids your body absorbs through protein digestion. Your liver uses enzymes called deaminases and transaminases to transform the amino acids into the forms most useful to your body.

The deaminase and transaminase enzymes can add nitrogen to synthesize nonessential amino acids, or remove nitrogen to leave intact carbon structures that can then be utilized for the production of glucose or, less frequently, converted into fatty acids.

When these processes involve the release of nitrogen, a potentially toxic compound called ammonia is generated. Your liver then converts the ammonia to urea, allowing it to be safely flushed from your body.

Prolonged, excessive exposure to alcohol or other drugs as well as nutritional deficiencies can compromise your liver’s ability to carry out these key jobs. Altered amino acid metabolism is one of the hallmark symptoms of liver disease, and studies indicate that supplementing with amino acids—and BCAAs in particular—can improve the health of your liver.

Investigating the Ways Amino Acids Benefit Liver Health

Some of the most exciting research on how amino acids benefit liver health was done by a team of scientists based in Kyoto, Japan. The team hypothesized that BCAA supplementation could slow down, or possibly even halt, the progression of chronic liver disease.

After inducing liver disease in a group of rats, the researchers then split the rats into two groups. One group received a diet supplemented with three BCAAs: valine, leucine, and isoleucine. The other was the control group. Over the course of the 11-week study, weekly blood samples were taken from both groups of rats. At the study’s conclusion, the researchers took liver samples.

The results of BCAA supplementation were quite dramatic. Blood levels of a liver enzyme called AST, which rises as liver damage intensifies, were an average of 22% lower for the group given BCAAs than for the control group. And levels of the CTGF protein, a marker of liver scarring, were an average of 75% higher in the control group.

Perhaps most significant of all, levels of an enzyme called caspase 3 and a protein called albumin, which indicate rates of cell death, were respectively 100% and 80% higher in the control group.

Based on these changes, the researchers concluded: “Supplementation with branched-chain amino acids delays the progression of chronic liver disease” and that it does so specifically by slowing liver cell death.

Learn about how amino acids benefit liver health.

Rates of Liver Disease Are Rising

Concerningly, rates of liver disease fatalities in the United States are rising, according to an analysis of data collected from across the nation. Lead author Zobair M. Younossi, MD, MPH, attributes this largely to a spike in nonalcoholic fatty liver disease (NAFLD).

“I believe it’s all related to a big increase in obesity and type 2 diabetes in this country,” Dr. Younossi said in an interview in advance of the annual meeting of the American Association for the Study of Liver Diseases. “Those two risk factors drive NAFLD and its progressive type, nonalcoholic steatohepatitis (NASH). That accounts for at least part of the increase in mortality related to liver disease.”

Dr. Younossi and his colleagues analyzed findings from 838,809 chronic liver disease-related deaths. They found that the overall fatality rate for chronic liver disease rose by 1.3% for men and 2.5% for women.

Nonalcoholic liver disease was the most common cause of chronic liver disease-related deaths (34.7%), followed by alcoholic liver disease (28.8%) and chronic hepatitis C (21.1%). Between 2007 and 2016, fatalities caused by NAFLD increased from 7.6 to 9.0 per 100,000.

One of the most important takeaways from the analysis, Dr. Younossi said, is that NASH—the most severe form of NAFLD—is quite common in the United States. “These patients are under-recognized and underdiagnosed because they are asymptomatic.” But fatty liver disease can progress to full-blown cirrhosis. Younossi believes it’s vital to identify treatments that can help to tackle this disease.

Using Amino Acids to Treat Liver Disease

Studies done with humans have confirmed that amino acid supplements can naturally and effectively treat both nonalcoholic fatty liver disease and alcoholic liver disease, the top two causes of liver disease-related deaths.

A clinical trial found that essential amino acids reduce liver fat as effectively as fenofibrate, a top pharmacological treatment. And the amino acids caused no adverse reactions. Fenofibrate, on the other hand, can cause unpleasant side effects such as fever, hives and other skin rashes, muscle aches and pains, stomach pain, and vomiting.

Learn about how amino acids benefit liver health.

Scientists are still working to understand the metabolic shifts that cause fat to accumulate in the liver, which then disrupts liver function and results in damage and disease. Many people show no symptoms of fatty liver in the early phases, but some potential warning signs include:

  • Fatigue
  • Weakness
  • Nausea
  • Difficulty concentrating
  • Pain in the upper right abdomen, where the liver is located

It is possible to mitigate the damage associated with fatty liver disease, and in some cases, to fully reverse it. Nutrient therapies that improve fatty acid metabolism in the liver, like essential amino acids, can go a long way toward safeguarding or restoring liver health.

Muscle Strains, Sprains and Pulls: How to Heal Quickly and Protect Yourself with Amino Acids

Muscle strains are common injuries—especially for athletes and individuals with jobs that require heavy lifting. Muscle strains in the back cause significant pain and stiffness and may affect your quality of life. How long does it take for a pulled muscle or a muscle strain to heal? It depends on the severity of the injury and how you choose to treat the injury.

Severe muscle injuries, including muscle sprains and strains, limit your range of motion, depending on where the injury occurs. For example, a muscle strain may require time off work or time away from the gym to allow the muscle tissue to heal properly. Conventional muscle strain treatments, as well as natural remedies such as physical therapy, amino acid supplements, massage, and other techniques, can hasten recovery time.

The best advice? Avoid muscle injuries by warming up before exercising and by lifting heavy objects correctly (use those legs!).

What Is a Muscle Strain?

Muscle strains occur when muscles are overstretched to the point of tearing muscle fibers. Muscle injuries that involve torn muscle tissue can range from mild to severe. Mild cases, for example, only affect a few of the muscle fibers in the group while the surrounding muscles remain intact. On the other side of the scale, severely strained muscles are torn to the extent that the muscle is unable to function correctly.

According to Harvard Medical School, there are three grades of muscle strains defined by the severity of the damage:

  • Grade 1 strain: A grade 1 strain is the mildest of the three grades, causing the muscle to be painful and tender, but to retain its normal strength. Typically, only a few muscle fibers have been damaged and the surrounding fibers continue to function appropriately, allowing for full range of motion and weight-bearing activities.
  • Grade 2 strain: This grade of strain is considered moderate and causes muscle pain and tenderness. The surrounding area may swell and bruise. In a grade 2 muscle strain, a significant loss of strength and range of motion may occur.
  • Grade 3 strain: If a muscle tears all the way through, separating the muscle into two pieces, it is considered a grade 3 strain. Grade 3 strains cause complete loss of muscle function, significant pain, a visible dent under the skin, discoloration or a bruise, and swollen tissue. A grade 3 muscle strain is considered a serious injury and needs to be evaluated by a healthcare professional.

Delayed-Onset Muscle Soreness, or DOMS, presents similarly to a grade 1 muscle strain. DOMS is the result of exercise—or overexercise—and the pain typically appears within 48 hours after exercising and lasts for a few days. Rubbing the muscle and gentle stretching will help the injury heal and relieve pain and tightness.

Muscle Strain Symptoms

Muscle strain symptoms depend on the location of the injury and severity. Recognized signs of a muscle strain may include:

  • An audible “pop” at the time of injury, indicating a grade 3 strain
  • A gap or visible change in the normal outline of a muscle, suggesting a grade 3 strain
  • A decrease in muscle strength, indicating a grade 2 strain—with complete loss of muscle function signifying a grade 3 strain
  • Swelling, bruising, or both at the site of injury
  • Muscle cramps or spasms
  • Generalized muscle pain and tenderness that increase with movement
  • Charlie horse-type pain
  • Painful muscle knots

Certain areas of the body may present with slightly different symptoms of muscle damage including:

  • Low back strain: If you have a low back muscle strain, the back pain will likely radiate into the buttocks. A low back strain causes stiffness and often restricts the range of motion. The injury may cause spasms, poor posture, and significant pain, even while at rest.
  • Forearm muscle strain: When you experience problems flexing the fingers or wrist, or pain, swelling, and muscle spasms, you may have a forearm muscle strain. A forearm muscle strain is often caused by physical trauma, overuse, or repetitive movements.
  • Hamstring strain: Hamstring strains are very common injuries for competitive athletes. According to the Mayo Clinic, this type of muscle injury often is related to poor flexibility, muscle imbalance, or a prior hamstring injury.
  • Neck strain: Necks are incredibly susceptible to injury. There are over 20 muscles connected to the neck that facilitate the movement of the shoulders, upper back, jaw, neck, and head. Neck strains may cause sharp localized pain that aches or throbs, stiffness, muscle spasms, and inflammation, and the pain often worsens with movement.

NOTE: An Achilles tendon rupture can cause an audible “pop” like a grade 3 strain, as well as immediate sharp pain in the lower leg and ankle. The Achilles tendon is not a muscle, and if you experience significant pain or the inability to bend your foot or stand on your toes, see your doctor immediately for evaluation and treatment.

 

Did you just pull a muscle?

Diagnosis and Muscle Strain Treatment

If you believe you have a grade 2 or a grade 3 muscle strain, see your sports medicine healthcare team as soon as possible. Your doctor will physically examine the area, testing range of motion, pain, flexibility, and strength. If your symptoms are moderate to severe, X-rays or an MRI may be required to determine the extent of the damage to the muscle so the best treatment for your muscle strain can begin.

If you have a minor muscle strain, your doctor may recommend the R.I.C.E. method:

  • Rest: Allow the muscle to repair by minimizing use for a few days or until pain abates.
  • Ice: Apply ice for 10 to 15 minutes every hour for the first 24 hours, and then every 3 to 4 hours, or as necessary.
  • Compression: Wear a compression wrap or undergarment for the first few days after you’ve injured your muscle to relieve pain.
  • Elevation: For the first few days after injury, elevate the muscle above the heart to reduce swelling.

For minor muscle sprains, your physician will likely suggest an over-the-counter anti-inflammatory medication like ibuprofen and encourage you to begin stretching the muscle after a few days of healing. If the stretching causes pain, give yourself a few extra days to allow the injured muscles to repair.

Grade 2 and grade 3 strains may require prescribed pain relievers and muscle relaxants to relieve discomfort. Severe strains may require a trip to an orthopedic specialist. Depending on the location and severity of the strain, immobilization for a few weeks may be necessary. In severe cases, surgery and physical therapy may be required.

When healing from a sports injury, even a minor muscle strain, it would be wise to consult with a physical therapist who can design a customized recovery and exercise program for you. The last thing you want to do is cause further damage or re-injure your muscle. A sports medicine-minded physical therapist can teach you to exercise properly to spur healing and to create muscles that are strong and flexible, so reinjury of the muscle is less likely.

Amino Acids and Muscle Recovery and Health

For all grades of muscle tear damage, taking a full-spectrum amino acid supplement spurs healing of muscle damage when consumed in the days following injury according to a study published in the International Journal of Sport Nutrition and Exercise Metabolism. Researchers from Australia investigated a supplement that contained the nine essential amino acids as well as three nonessential amino acids. Findings support the use of an amino acid supplement 30 minutes prior to working out and immediately upon completion of the workout to reduce muscle soreness and delayed-onset muscle soreness.

Amino acids are required for muscle growthmuscle building, and pain management. If you are looking to heal a muscle strain or other muscle injury—an amino acid supplement is a must. According to an article in the journal Practical Pain Management, amino acids are responsible for three key pain-modulating neurotransmitters, and balanced amino acid supplementation can reduce pain and even reduce the dose of prescription painkillers that are necessary for severe pain. The article further explains that the human body’s entire pain-relief system is fueled by amino acids and the hormones they produce.

4 Essential Tips to Prevent Muscle Strains and Sprains

Preventing injury is always better than treatment! Use these four tips to help prevent muscle injuries including pulls, tears, and sprains.

  1.  Warm up your muscles properly before exercising or moving heavy objects. Just 5 minutes of light stretching can protect you from injury.
  2. Take an amino acid supplement 30 minutes before you exercise and immediately following the workout to protect your muscles and improve performance.
  3. Learn how to lift heavy objects safely by squatting down instead of bending over to prevent mild strains or more severe lower back injuries.
  4. Under the guidance of a physical therapist or sports medicine professional, create a balanced exercise routine that includes aerobic activity, stretching, balance work, resistance exercise, and weight lifting.