Serrapeptase: The Science Behind the Supplement

Mostly used by health care professionals in Japan and Europe for reducing inflammation after trauma, surgery, or in other inflammatory circumstances, serrapeptase is also available as a dietary supplement for its various health benefits. Find out what serrapeptase is, how it was discovered, and which of its supposed benefits have the strongest evidence backing them.

Serrapeptase, also known as serratiopeptidase, serratia peptidase, or silk worm enzyme, is an isolated enzyme from bacteria found in silk worms. Mostly used by health care professionals in Japan and Europe for reducing inflammation after trauma, surgery, or in other inflammatory circumstances, it is also available as a dietary supplement for its various health benefits. This article will explore the science behind those health claims, discuss the potential side effects of serrapeptase, and help you decide whether this anti-inflammatory is right for you.

What Is Serrapeptase?

The serrapeptase enzyme is a proteolytic enzyme, which means it has the ability to break down proteins into their building blocks, amino acids. It’s an enzyme produced by the bacteria living in the silk worm’s digestive tract, and specifically it’s the enzyme that allows an emerging moth to dissolve and digest its own cocoon. If you’re the kind of person who finds bugs and worms to be skin-crawlingly gross, it might do you well to think less about where this enzyme comes from, and more about what it and other proteolytic enzymes like bromelain, chymotrypsin, and trypsin can do to benefit you.

Discovered throughout the 1950s, these enzymes were used in the United States to relieve the inflammation caused by ulcerative colitis, rheumatoid arthritis, and post-surgical swelling. By 1957, the Japanese were using serrapeptase in the same manner, and in the 1990s these different enzymes were compared and it was found that serrapeptase was the most successful at reducing inflammatory responses. Since then it has become more widely used in Europe and Japan for its anti-inflammatory benefits.

The Benefits of Serrapeptase

Though serrapeptase is relatively new to the medicinal scene, there have nevertheless been many studies done to document its effectiveness and safety. Here are some of the benefits that have been observed from the use of serrapeptase.

Serrapeptase supplements: the science and the speculation.

May Reduce Inflammation

This is the health benefit serrapeptase is best known for, reducing inflammation in instances like tooth removal or post-surgery recovery. It’s thought that serrapeptase works by decreasing inflammatory cells at the site of injury. The anti-inflammatory effects of serrapeptase were shown in a clinical trial on the surgical removal of wisdom teeth, and serrapeptase was found to be more effective at improving lockjaw than more powerful drugs like ibuprofen and corticosteroids.

Though corticosteroids improved facial swelling more effectively on the first day post-surgery, the differences on the second day were insignificant. While more research is still needed to define the best uses of serrapeptase going forward, the researchers in the study did note that serrapeptase had a better safety profile than the other drugs analyzed, which may make it particularly useful in cases of drug intolerance in patients, or those who have adverse side effects with stronger drugs.

May Prevent Infections

There is evidence that serrapeptase may decrease the risk of bacterial infection by acting as a “biofilm buster,” so-called because bacteria have the ability to join together and form a protective barrier or film around themselves. The biofilm shields them from antibiotics long enough that their rapid growth can take place and cause infection. Serrapeptase can inhibit the formation of biofilms, increasing the efficacy of antibiotics in cases like Staphylococcus aureus (Staph. aureus), or staph infection, one of the most common opportunistic dangers associated with hospital stays.

Both animal and test-tube studies have shown that serrapeptase combined with antibiotics was more effective than treating Staph. aureus with antibiotics alone, including those strains that have become drug-resistant. An example of a drug-resistant form of staph infection is MRSA (methicillin resistant Staph. aureus), an especially dangerous infection to those who are already hospitalized in immune-compromised states.

May Reduce Pain

Pain being a symptom of inflammation, serrapeptase has been known to reduce pain by inhibiting certain compounds. For example, in one double-blind study that examined the effects of serrapeptase in about 200 people with inflammatory conditions of the ear, nose, and throat, researchers found that those who took a serrapeptase supplement had significant reductions in mucus production and pain severity than did those who took a placebo.

Another study found that serrapeptase reduced pain significantly compared to a placebo in 24 participants following the removal of their wisdom teeth. More research is needed for scientists to be sure of serrapeptase’s effects, but these findings show promise for those hoping to avoid nonsteroidal anti-inflammatory drugs (NSAIDs) after medical procedures.

May Help Dissolve Blood Clots

It is thought that by acting to break down fibrin (a protein formed in blood clots) as well as damaged and dead tissue, the serrapeptase enzyme could help treat atherosclerosis. Atherosclerosis involves plaque buildup inside your arteries, which leads to a hardening and narrowing of the arteries and an increased danger from blood clots.

If serrapeptase is successful at dissolving plaque or blood clots, it could reduce a person’s risk of stroke or heart attack. However, not enough studies have been done showing a direct effect, and so while there is potential that serrapeptase has a role in treating blood clots, more research is warranted.

May Be an Aid Against Chronic Respiratory Disease

Chronic respiratory and chronic airway diseases affect the lungs and breathing apparatuses of the body. Serrapeptase’s potential to clear mucus and reduce inflammation in the the lungs could help improve breathing in those with asthma, chronic obstructive pulmonary disease (COPD), and pulmonary hypertension, which is a form of high blood pressure in the vessels of your lungs.

These chronic conditions are ongoing and incurable, and yet managing the symptoms effectively (as with increased mucus clearance and better dilation of air passages) can greatly improve a person’s quality of life. One month-long study of 29 participants with chronic bronchitis involved a test group that was given 30 milligrams of serrapeptase per day, which resulted in less mucus production than the control group, better lung-clearing ability, and greater ease of breathing.

May Treat Endometriosis

Due to the potential serrapeptase has for targeting dead tissue and scar tissue throughout the body, some believe there is potential in using serrapeptase for endometriosis treatment. Endometriosis occurs when endometrial cells grow outside the uterus, in the tissues surrounding the pelvic area, causing pain and often issues with fertility.

Likewise with conception issues arising due to ovarian or uterine cysts, serrapeptase for fertility is another natural therapy that currently has more anecdotal evidence than scientific research done on it, though that does not mean the research won’t be done, nor that it wouldn’t be a safe supplement to try in consultation with a qualified health care professional.

May Help Relieve Alzheimer’s Disease

One study on rat models revealed that the proteolytic enzymes nattokinase and serrapeptase may have a therapeutic application in the treatment of Alzheimer’s disease, modulating the different factors that characterize the disease. Oral application of these enzymes provided a decrease in transforming growth factor, acetylcholinesterase activity, and interleukin-6, all of which are found in high levels among patients with Alzheimer’s disease. While more research still needs to be done, Alzheimer’s is a medical condition that needs any relief options available.

Potential Serrapeptase Side Effects

Because it’s such a new commodity, people are rightly concerned that there could be potential serrapeptase dangers. There are not many published studies touching on potential adverse reactions to taking serrapeptase, however some studies have reported the following side effects.

As there is a lack of data on the long-term safety and tolerability of this enzyme, should any side effect occur after you take it, you should stop immediately and seek medical advice. What works for some may not work for all, and so your judgement is paramount when it comes to whether you’re getting the benefits you want.

How to Take Serrapeptase

It’s advised against taking serrapeptase with any sort of blood thinner, or other dietary supplements like turmeric, garlic, or fish oil which could increase a risk of bruising or bleeding. For serrapeptase dosage, it’s recommended to take between 10-60 milligrams per day (the range used within the various studies) on an empty stomach, and to avoid eating for at least 30 minutes afterwards.

When purchasing the supplement, choose a product in an enteric-coated capsule to prevent your stomach acid from neutralizing the enzyme before it reaches your intestine. Without a strong enough capsule, the enzymatic activity could be deactivated before it has a chance to work.

How long does it take serrapeptase to work after you take it? For pain and swelling it can have immediate effects post-surgery, but for more gradual or ongoing treatments, the effects might be felt over a period of weeks. It truly depends on your condition, your health, and how you’re using the supplement.

The Secrets of Serrapeptase

Our understanding of serrapeptase is far from comprehensive at this moment. There is one study linking it to treatment of carpal tunnel syndrome and anecdotal evidence suggesting serrapeptase for weight loss (albeit temporary). There are far more clinical studies on the use of serrapeptase for reducing inflammation, fighting infections, and preventing blood clots, but researchers are still exploring its uses. Should you be interested in seeing what serrapeptase supplementation can do for you, we only ask that you do so wisely, and with a willingness to consult a medical professional about any results you find, be they bad or good.

Unexplained Weight Loss: What Could It Mean?

Unexplained weight loss could be due to dangerous underlying causes, from infections, to disorders, to conditions as serious as congestive heart failure and cancer. 

Under normal circumstances, people have to work hard to control their weight, whether they’re trying to slim down or bulk up. Sudden, noticeable, weight loss is often a symptom of an underlying health concern, and unexplained weight loss is even more worrying, as it could be an indication that something is wrong with your body, but is currently undiagnosed. This article will detail some of the usual suspects behind unintentional weight loss, so you can better understand how important it is to identify the underlying cause.

How Much Weight Loss Is Concerning?

It’s common to fluctuate between 1-3 pounds per day according to your scale; those are just the vagaries of water weight. However, a loss of 10 pounds or more (or 5% of your body weight) over a 6-12 month period with no known reason warrants concern. If you’ve changed your habits, changed your diet, or undergone a change in life that could explain the reduction in weight, then it may not be that unusual, but you may benefit from asking yourself some questions.

  • Did you start a new job?
  • Did you move to a new area?
  • Are you under some known form of stress (whether happy or unfortunate—i.e. planning a wedding or caring for a sick loved one).
  • Has there been a change in your relationship status?

It’s important to know, because while this sort of steady weight loss would be welcome if you’d changed your diet with the intention to lose weight (by transitioning from processed to whole foods for example), if no alterations to your diet or lifestyle have been made and your weight has still gone down this dramatically, there may be some serious underlying reasons.

Losing Weight Without Trying: Am I Sick?

Unexplained weight loss could be the first sign of sickness, yes. You should contact a doctor or health care professional right away to seek evaluation, as the causes for unexplained weight loss can be quite serious, from infections, to thyroid issues, to the terrifying prospect of cancer (but please don’t go to the extreme scenario…just go to a doctor!).

The good news is that doctors quickly find the cause of abnormal weight loss in over 75% of cases. In fact, even if you think you know the cause, something like general stress and anxiety could be masking a physical health problem, and you should make an appointment to be sure this weight loss isn’t caused by a combination of issues or that it isn’t taxing your health in other ways.

If the first examination isn’t thorough enough, seek a second opinion to rule out other causes. Blood tests, a urinalysis, a thyroid panel, liver and kidney function tests, a blood sugar test, or imaging studies may need to be done to make sure there are no red flags in your health profile.

Your doctor may ask:

  • Have you made any changes in your exercise or diet recently?
  • Has this sort of weight loss ever happened to you before?
  • Do you have any dental problems or mouth sores that could impede your ability to eat normally?
  • Is there a history of any particular illness that runs in your family?
  • Do you have any other concerning symptoms (palpitations, excessive thirst, sensitivity to heat or cold, a persistent cough, shortness of breath)?

Consider your overall health as you prepare for your appointment, so you can make sure your doctor is informed of any symptom that might be relevant to your condition.

Why Diagnosis Is Important

There are many medical conditions that might lead to unintentional weight loss. The American Cancer Society points out that 50% of all cancer patients have a form of cancer cachexia, a wasting syndrome that involves unintentional weight loss and brings on the death of about 20% of cancer patients.

It is the same with cardiac events. One study explicitly states, “Unintentional weight loss was an independent predictor of poor outcomes.” Unintentional weight loss brings about higher morbidity, mortality, and bodes ill for anyone already battling a disease. That is why identifying and treating unexplained weight loss is so important, especially in older adults (above age 65), who are all the more at risk of serious consequences from any sudden change in health.

Possible Causes of Unexplained Weight Loss

We’ll now run down some of the common causes of unintentional or abnormal weight loss.

Unexplained weight loss: possible underlying causes.

Endocrine Conditions

Endocrine conditions include hyperthyroidism (an overactive thyroid), hypothyroidism (an underactive thyroid), diabetes, and Addison’s disease (wherein the adrenal glands don’t produce enough hormones). The thyroid gland is located in your neck, is somewhat butterfly-shaped, and controls your metabolism. An issue with the thyroid gland could be accompanied by heart palpitations, and if type 2 diabetes is at play, you’re likely to experience increased thirst and excessive urination as your body tries to expel all the glucose it can’t absorb.

Infections

Infections include anything from parasites, bacterial infections, and viruses (which HIV/AIDS patients are more susceptible to), along with conditions like endocarditis (an infection of the heart valves), or tuberculosis (an infection of the lungs). In these instances, your body is losing weight because it is using all of its resources to fight off an invasion.

Cancer

Weight loss can sometimes be one of the earliest symptoms of cancer, such as from lung cancer, ovarian cancer, colon cancer, pancreatic cancer, or blood-related cancers like lymphomas and leukemias. About 40% of cancer patients report having experienced weight loss around the time of their diagnosis, and studies have shown that unintentional weight loss is the second highest predictor for certain cancers. Weight loss often occurs as a result of cancer due to the body’s nourishing efforts being hijacked to support an abnormal tumor growth. Doctors will often check first for tumors in the bowels, colon, and esophagus, which can impede swallowing and quickly contribute to unintentional weight loss.

Intestinal Conditions

Conditions like celiac disease, peptic ulcer disease, Crohn’s disease, ulcerative colitis, and pancreatitis can lead to unexplained weight loss in those who have yet to be diagnosed.

Celiac disease is an autoimmune disorder wherein the small intestine is damaged by gluten intake, leading to GI symptoms like diarrhea and bloating. According to the Mayo Clinic, when the immune system sees gluten as a threat, it reacts, and that reaction means your body doesn’t have a chance to absorb its nutrients properly. Likewise, in an inflammatory bowel disease like Crohn’s, the body’s reaction leads to malabsorption and unexplained loss of weight.

Those with chronic pancreatitis lose weight due to the fact that their body cannot produce enough digestive enzymes to properly break down food (and this may come with nausea, particularly from eating fatty foods).

Heart Failure

Congestive heart failure may cause weight loss due to a lack of sufficient blood flow to the GI tract. In a 2014 study researchers observed that those who had the most dramatic unintentional weight loss were indeed those who had the lowest blood flow to their intestines. Inadequate blood flow makes it harder to absorb nutrients, and the nausea and fatigue associated with congestive heart failure could lead to a loss of appetite.

Eating Disorders

Eating disorders like bulimia and anorexia nervosa can cause dangerous weight loss, and while it might not be a completely unknown cause to the person suffering from the condition, it can be an indicator to a loved one or parent that something is wrong. Moreover, because of the nature of body dysmorphia, those coping with these eating disorders may not fully realize just how significant their weight loss is until it starts causing other health symptoms due to malnutrition.

Psychological Conditions

Depression and anxiety disorders often come with loss of appetite as a side effect, and can be an underlying cause of unexplained weight loss. It often goes unnoticed until the weight loss is significant enough, and will involve a different sort of diagnosis, as these are not conditions that can be found via imaging scan or blood test.

Drug Abuse

Be they extralegally obtained drugs or prescription medications, drug dependence can alter your body’s metabolic and digestive processes, and change your eating habits. Side effects from medications could lead to nausea, loss of appetite, or laxative effects that can contribute to unintentional weight loss as well.

Neurological Conditions

Unintentional weight loss is frequently seen in those with Parkinson’s disease and Alzheimer’s. This is possibly due to the increased energy expense of rigidity, tremors, or dyskinesia (involuntary movements) associated with Parkinson’s, or the reduced energy intake due to poor health, stress, or the side effects of medication.

Rheumatoid Arthritis

When the immune system causes inflammatory reactions in healthy tissues, as in those with rheumatoid arthritis, it can also lead to a loss of appetite or an inflammation of the gut that interrupts nutrient absorption.

Reproductive Issues

Unexplained weight loss during menopause is unnatural, as it’s more common that menopause cause weight gain in women experiencing the change. Unintentional weight loss surrounding menopause could indicate that the changes in hormones has caused or made you susceptible to some other condition (stress, diabetes).

Likewise, unexplained weight loss during pregnancy is the opposite of the normal course of order. In the first few months, a loss of appetite due to morning sickness could be the culprit behind unintentional weight loss, but excessive weight loss could be a sign of a thyroid dysfunction or hyperemesis, a pregnancy complication that entails vomiting, severe nausea, dehydration, and weight loss. Your obstetrician should be made aware of any such symptoms.

An Explanation Is Necessary

Unknown causes of weight loss include a lot of scary and potentially life-threatening concerns. It’s normal for your weight to fluctuate by a few pounds here or there throughout the course of the year, but if you cannot determine a cause for sudden, steady weight loss, it’s important to consult with a medical professional and investigate: in fact, it could save your life.

Autophagy and Fasting: What Does the Science Say?

Autophagy is the body’s recycling program, which can be triggered by intermittent fasting. Autophagy is key in removing the toxins associated with neurodegenerative diseases, reusing residual proteins for energy and repair, and prompting the regeneration of cells throughout our bodies.

This article will discuss what autophagy fasting is, how it works, and whether or not the science backs up this practice.

What Is Autophagy?

We’ll start with the definition of autophagy: “auto” meaning “self” and “phagy” meaning “eats” tells you that the literal translation of autophagy is “self-eating.” That sounds scarier than the reality—we’re not talking about some flesh-eating bacteria or even the more common sort of self-cannibalization that our bodies do to our muscles when in need of energy, catabolizing.

Autophagy is more like a recycling program, or cutting your hair to keep it healthy and free of split-ends. It’s the body’s process of clearing out damaged cells so that it can regenerate new and healthier cells in their place. It’s almost like the internal equivalent of the exfoliating we do outside to keep our skin healthy.

The Details of Autophagy

Autophagy is a highly regulated process that delivers cellular waste material to lysosomes to be degraded, recycled, and then used to generate molecules to fuel cellular metabolism. For the specifics: scientist and Nobel prize winner Christian de Duve coined the term autophagy in 1962, when researchers discovered an increased amount of lysosomes in rat liver cells after an infusion of glucagon. It was also discovered that autophagy is regulated in part by the kinase mammalian target of rapamycin (mTOR), which promotes or represses autophagy as needed.

Autophagy and fasting: your body's recycling program.

What Does Autophagy Do?

The normal process of autophagy impacts your body and your health in various ways.

Promotes Metabolic Efficiency

The dysregulation of autophagy may contribute to developing metabolic disorders like insulin resistance, obesity, diabetes mellitus, osteoporosis, and atherosclerosis. From the very cellular level, autophagy can be used to improve the efficiency of mitochondria. The mitochondria in cells are the energy-makers, and the process of autophagy feeds them proteins from damaged cells that would otherwise either go to waste, or clog up other processes in the body.

Assists Against Neurodegenerative Disorders

In cases of Parkinson’s disease, Alzheimer’s disease, and Huntington’s disease, selective autophagy can help clean up the specific proteins that form in and around the brain’s neurons and result in neurodegenerative symptoms. While autophagy was previously thought of as a nonselective process of digestion, it’s now understood that autophagy receptors make this a selective process, involving a cellular form of quality control.

Fights Infectious Disease

One of the central functions of autophagy is to control infections. It removes the toxins that create infections and helps your immune system adapt its response to infection. Viruses as well as intracellular microorganisms and bacteria can be removed via autophagy.

Improves Muscle Performance

The oxidative stress placed on our cells during exercise can trigger instances of autophagy to help remove some of the damaged cellular debris and support our energy needs. Autophagy is necessary for exercise-induced muscle adaptation and the improvement of physical performance.

Prevents Cancer Growth

This is a double-edged sword, because while autophagy can clean up the damaged DNA and chronic inflammatory aspects of cancer development, some forms of cancer will attempt to usurp the process and use it to a detrimental advantage. Regulating the autophagy pathway is important for inhibiting cancer growth.

What Is Autophagy from Fasting?

Autophagy via fasting occurs when you take the reins of autophagy by carefully controlling your dietary intake. This is usually done in an attempt to trigger safe yet fast weight loss. Here are two types of dieting that can bring about targeted autophagy.

Autophagy via Intermittent Fasting

Stressing your cells is a quick way to turn on the autophagy process in your body, but you don’t want to overly stress your body for too long lest the cure be worse than the cold. Intermittent fasting can create a useful nutrient deprivation in your cells, just as exercising will create a certain amount of oxidative stress to purposefully trigger your repair mechanisms into building muscle.

Intermittent fasting is not so much a diet as a pattern of eating, with daily short-term fasting of 16 hours, or longer fasts of 24 hours twice a week. How long until autophagy from fasting begins? It begins whenever your liver glycogen depletes, which occurs between 12-16 hours into a fast. This isn’t a deprivation so much as a return to the eating pattern humans evolved to survive under when we didn’t have supermarkets open 24/7. Intermittent fasting in that sense is more natural than eating three square meals a day, and can lead to long-term, sustainable weight loss, as well as better overall health when practiced…well, intermittently.

Autophagy via Ketosis

The ketogenic diet (or keto diet) is another way to get the benefits of fasting without actually fasting. This high-fat, low-carb diet breaks down to about 75% of your daily calories from fat, 20% from protein, and 5% from carbohydrates.

By putting a caloric restriction on carbs, you end up shifting your body’s go-to source of energy from quick glucose to fat. That fat burning starts first with the fat you eat, and then quickly turns to burning the fat stores already on your body for a reliable energy source. This produces ketone bodies that bring protective effects, and research suggests that ketosis can also bring about periods of autophagy, which has its own health benefits for the body.

Autophagy via Exercise

Exercise is a non-diet-related way of inducing autophagy. An animal study suggests that physical exercise may bring about autophagy in specific organs that are involved in metabolic regulation, namely the pancreas, liver, adipose tissue, and muscles.

Adding intermittent fasting and regular exercise to your lifestyle is an excellent way to stimulate autophagy in your body. To make sure you have the ability to build muscle while fasting or utilizing calorie restrictions, you may want to supplement with a full host of the amino acids necessary for protein synthesis. That way the required ingredients for new muscle are never out of balance.

The Potential Benefits of Autophagy

Autophagy is the body’s way of replacing old cells with new and younger ones, a regeneration effect that can help optimize our lifespans. As with any process in the body, autophagy declines as we age—waste accumulates and the regeneration rate decreases. This invariably leads to many symptoms of aging, which is why targeted autophagy fasting is so appealing.

Autophagy and Anti-Aging Potential

The benefits of autophagy are still being explored by scientists for its anti-aging potential, from the cellular level of the brain to the surface level of the skin. Those looking to employ autophagy via fasting to the loose skin left over after dramatic weight loss can find hope in studies suggesting that the slowing of natural autophagy is associated with a deterioration of dermal integrity, and that the fibroblasts that produce collagen (which keeps our skin youthful and pliable) suffer when autophagy decreases as we age. It stands to reason that if our collagen-producing fibroblasts get clogged due to a lack of autophagy, a targeted increase in autophagy frequency can free them up again, thus preventing and counteracting the aging of our skin.

Autophagy and Anti-Cancer Potential

The buildup of cellular waste affects our bodies from surface to core, as discussed previously with neurodegenerative diseases like Parkinson’s. Fasting and autophagy applied to cancer treatment have been shown to inhibit tumor growth. Autophagy fasting is still being fully explored by researchers hoping to prevent cancers from forming via the clean-up efforts of autophagy.

Some studies indicate that cancerous cells can be detected and destroyed through autophagy, before they can proliferate and start using the body’s processes against itself. Targeted use of autophagy, and keeping that process from being hijacked by cancers, may lead to new therapies for cancer treatment.

Fasting for Autophagy

Autophagy is our body’s recycling program, beneficial in removing the toxins associated with neurodegenerative diseases, reusing residual proteins for energy and repair, and prompting the regeneration of new and healthy cells throughout our bodies. On a cellular level, it’s like a regeneration episode of Doctor Who, but instead of science fiction, this process is science fact, and you have the ability to use it to your health’s advantage via targeted fasting.

Muscle Atrophy: Causes, Treatment and Prevention

Learn about what causes muscle wasting or muscle atrophy, and how best to prevent and treat this condition, including through the use of physical therapy, medical intervention, and staying active. 

Muscle atrophy is essentially muscle wasting: it’s what happens when your muscles waste away, frequently as a result of a lack of physical activity. This article will explore the causes and symptoms of muscle atrophy, as well as preventative steps people can take if they’re immobile or bedridden due to illness. Loss of muscle mass or muscle strength can be particularly devastating for those who are already in positions of compromised health, and so in an effort to help you maintain your quality of life, we’ve compiled the relevant information here.

Muscle Atrophy: Definition

Atrophy of the muscles occurs when a person is inactive for so long that their skeletal muscles (these are the muscles attached to your bones which literally make your skeleton move) begin to break down, and the muscle protein is cannibalized by the body. This can happen in small instances or large, catastrophic instances.

Muscle atrophy of the hand or forearm may occur if you spend weeks in a cast to heal a broken arm, which is why people in casts are given exercises to do while they’re immobilized to prevent protein degradation in their muscles and muscle wasting. Muscle atrophy of the legs or muscle atrophy of the thighs can happen on a much larger scale to those who become wheelchair-bound, either temporarily or due to becoming permanently paraplegic. In even more extreme cases, those who have been held as prisoners of war may have full-body muscle wasting due to confinement and malnutrition for significantly long periods, sometimes years.

Muscle atrophy is a decrease in muscle mass, either partial or complete, which is most commonly suffered when a person becomes disabled or their movements severely restricted. This makes it difficult or impossible to move the part of the body where the muscle has atrophied, and medical advice should be sought for solutions.

Muscle atrophy: causes, treatment, and prevention.

Muscle Atrophy: Causes

Significant decreases in activity levels can lead to muscle atrophy, and there are many situations where that can occur, causing what’s known as disuse atrophy. There are also instances of muscle atrophy due to medical conditions that inhibit the use of a body part, and even rarer causes like the muscle atrophy experienced by astronauts after relatively short periods (a few days) of weightlessness. Muscle atrophy in situations of being bedbound or ceasing intense physical training can come on in as little as 2 weeks. Some of the other causes of muscle atrophy are as follows.

  • Lack of physical activity
  • Advanced aging
  • Malnutrition
  • Stroke
  • Alcohol-associated myopathy
  • Burns
  • Temporary disabling injuries (broken bones, torn rotator cuff)
  • Permanently disabling injuries (severed spinal cord, peripheral nerve damage)
  • Prolonged corticosteroid therapy

Some of the diseases and medical conditions that can disrupt or restrict movement, thus leading to muscle atrophy, include:

  • Spinal muscular atrophy: A hereditary wasting disease of the limbs.
  • Osteoarthritis: Degeneration of bones and joint cartilage that leads to decreased movement.
  • Polymyositis: An inflammatory disease of the muscles.
  • Amyotrophic lateral sclerosis (ALS or Lou Gehrig’s disease): Compromises the nerve cells of the spinal cord.
  • Muscular dystrophy: A hereditary disease that causes muscle weakness.
  • Multiple sclerosis (MS): An autoimmune disease that destroys the protective sheathing of brain and spinal nerves.
  • Rheumatoid arthritis (RA): A chronic inflammatory disease of the joints.
  • Dermatomyositis: Inflammation of the skin and underlying muscle tissue.
  • Polio: A virus afflicting muscle tissue, which can lead to paralysis.
  • Cancer cachexia: The weight loss, lack of energy, and loss of appetite in someone undergoing cancer treatment.
  • Guillain-Barré syndrome: An autoimmune disease and form of polyneuritis, which leads to paralysis of the limbs.
  • Neuropathy: Nerve damage that results in loss of sensation or functioning.

Muscle Atrophy: Symptoms

Regardless of the cause, these are the symptoms that may alert you to possible muscle atrophy, after which a trusted medical professional should be sought for advice.

  • One of your limbs (arms, legs) appears markedly smaller than the other one.
  • You’ve spent a long time physically inactive (bedridden, hospitalized).
  • You’re experiencing noticeable weakness in one limb.

Not to be flippant about the subject, but there is some truth to the phrase “use it or lose it” when it comes to muscle. If you cannot move your muscles with regular physical activity, you will start to lose them.

Muscle atrophy pain may or may not be a symptom, as that depends on the cause of the atrophy. Many people will begin to lose muscle before they are aware it’s happening, and will have to rely on visual muscle size to realize they need medical attention.

Muscle Atrophy: Diagnosis

Once you’ve gotten in contact with a medical professional, the diagnosis may involve your full medical history, a review of any previous injuries, as well as an evaluation of your symptoms. Diagnosing the atrophy may also involve diagnosing the underlying medical condition, which may require blood tests, X-rays, MRIs, CTs, a nerve conduction study, or a muscle and/or nerve biopsy to find out what could be causing muscle atrophy if it’s not readily apparently (as it would be if you’d suddenly become bedbound).

Can Muscle Atrophy Be Reversed?

Depending on the cause, yes. There are some cases where a proper diet, exercise, and physical therapy can not only reverse muscle atrophy, but also prevent it from recurring. However, this will not be the case in some disease-related forms of atrophy, and it is important that you consult your doctor on what your expectations for muscle atrophy recovery should be in restimulating protein synthesis and rebuilding your muscles.

Muscle Atrophy: Treatment

Again, this will depend on the diagnosis of the cause, and also the severity of your muscle loss, but the treatments for reversible muscle atrophy may be as follows.

  • Physical therapy
  • Exercise
  • Ultrasound therapy
  • Dietary changes
  • Surgery
  • Electrical stimulation

If a lack of movement caused this condition, regaining movement will go a long way towards fixing it, and moderate exercise like walking, along with physical therapy, may be a way to regain muscle strength without needing surgery to fix skin, tendons, or ligaments too tight to begin moving again (as in cases of contracture deformity that could be caused by malnutrition or burn injury scar tissue).

Muscle Atrophy: Prevention

There are ways to prevent muscle atrophy before it happens, and ways to guard against it if you were fortunate enough to recover your musculature after one instance of muscle loss. If preventing muscle atrophy is in your control (and, of course, sometimes it will not be), here are a few ways to maintain muscle strength in adverse circumstances.

Stay Active

If you’re in recovery from a severe illness or have just come home from the hospital after a debilitating accident, it’s not as if you’ll take up jogging right away. However, movements as small as walking to your mailbox each day, or around the block, or up and down a single flight of stairs, can truly make the difference in the long run when it comes to maintaining your mobility.

Stay Nourished

Depending on your condition, this may be difficult, but when your body lacks the proper nutrition to stay running, it will start to catabolize your muscles for its needs, which is a form of self-cannibalization or destructive metabolism that literally eats away at your muscles. Make sure you’re getting proper protein, if not from whole foods, then in the forms of protein shakes or supplements, as every little bit may help.

In fact, supplementing with amino acids has been proven to help accelerate muscle recovery in times of sickness and illness and can help boost your muscle-building gains. To learn more about amino acid therapy for muscle atrophy, give this informative article, written by one of the world’s foremost amino acid researchers, a read.

Seek Physical Therapy

Physical therapy is particularly valuable for those with severe injury recovery (such as a car crash survivor) or a neurological condition, as therapists provide professional guidance on what, and how, and how often to stretch your body to build strength.

Try Passive Movement

Another way physical therapy can help you even before you have the strength to help yourself is with passive movement. Passive movement requires the therapist to gently move your legs and arms for you. This is how you can begin to recover from a very deep muscle deficit and build up strength and muscle again.

Preventative Measures

Not only will the above advice help prevent muscle atrophy, but it can also help discourage bedsores in those who are bedridden due to illness, and reduce the chances of developing dangerous blood clots in the limbs. Likewise, these movements may prevent muscle stiffness, retraction, and nerve damage. Consult a medical professional or licensed physical therapist for more advice.

Eliminate Atrophy

If you are in danger of muscle atrophy, take steps to make sure your protein intake and nutrients are sufficient, including the use of a supplement if necessary, like Amino Co.’s essential amino acid supplement, which contains all of the essential aminos required to build new muscle cells and structures. Also, make sure that you stay active, no matter in how small a way, to preserve your muscle function and prevent your muscles from falling into complete disuse. You cannot always control your body’s condition, but if the type of atrophy you fear is the type that’s preventable, it’s well worth the effort to maintain the quality of life and movement you’ve come to expect.

Acidic and Basic Amino Acids Explained

Discover the chemical differences between acidic and basic amino acids. Learn about the structure and nature of amino acids, the difference between acidic vs. basic substances, the pH scale used to measure them, and why these differences matter.

This article will quickly inform you of the difference between acidic and basic amino acids. We’ll provide the definitions and explanations you seek, including what are amino acids, what makes some of them acidic and some of them basic, and why that matters when it comes to the chemistry of the human body.

Amino Acids: Essential vs. Nonessential

Amino acids are the buildings blocks of protein in your body. In short, when it comes to protein synthesis and literally building new muscle, you cannot do it without your amino acids.

Nonessential Amino Acids

Your nonessential amino acids are the amino acids your body can create on its own as a byproduct of normal functioning. There are 11 of these amino acids, and they include the following:

  • Alanine (ala)
  • Arginine (arg)
  • Asparagine (asn)
  • Aspartic acid (asp)
  • Cysteine (cys)
  • Glutamic acid (glu)
  • Glutamine (gln)
  • Glycine (gly)
  • Proline (pro)
  • Serine (ser)
  • Tyrosine (tyr)

Essential Amino Acids

Your essential amino acids are the ones you need but cannot produce yourself, and so must be gained either from your diet or via supplementation. These amino acids include the following:

  • Histidine (his)
  • Isoleucine (ile)
  • Leucine (leu)
  • Lysine (lys)
  • Methionine (met)
  • Phenylalanine (phe)
  • Threonine (thr)
  • Tryptophan (typ)
  • Valine (val)

Now that you know the amino acids we’ll be talking about, let’s move on to an illustrative example of what an amino acid’s structure looks like.

Amino Acid Structure

To understand what differentiates amino acids, you’ll have to understand their structure and what they have in common. Each amino acid is made of a central alpha carbon atom (Cα), and attached to that central atom are three molecular structures, also known as functional groups: one is a carboxyl group (-COOH), the second is an amino group (-NH2), and the third is a single hydrogen atom (H). This is the same structure of all amino acids, until the last piece of the puzzle joins the rest: the R group side chain. The R group you can think of as the Radical group, as it is different and unique on each and every amino acid, of which there are 20 main ones in the human body.

Picture it, if you will, as a group of lava lamps. Each one is made up of a light bulb in the center, a power cord, a stand, and a cap. With a long row of 20 identical lava lamps, imagine that the only thing that would make any of them unique is the color combination inside its radical glass lava vessel. Maybe one vessel has blue water and green lava, while another one has purple water with yellow lava, while yet another has blue water combined with yellow lava. With 20 different color combinations, you have enough to represent all 20 amino acids. The light bulb in the center? That is your central alpha carbon. The power cord? The carboxyl group. The supporting stand? Your amino group. And the little decorative cap on top? Your single hydrogen atom.

We illustrate it this way because it’s that glass lava vessel that not only determines what kind of amino acid you have (i.e. what color your lava lamp is), but these side chains also determine whether or not an amino acid is basic or acidic. With that structure explained, let us next generally cover acid vs. base when it comes to a chemistry standpoint.

Acid vs. Base: The Basics About Acids

In chemistry, we’re talking about molecules (which are themselves made up of atoms). A base molecule or compound is the opposite of an acid. Acids are the compounds that donate a hydrogen ion (H+) to a base, while a base compound is one that can remove a proton (H+ is a proton) from an acid. A strong base molecule can deprotonate, or take the proton, of a weaker acid such as water.

Differences between acidic and basic amino acids.

Water, Acids, and Alkalis

Hydrogen molecules are why bases and acids are often measured in pH levels (pH stands for “potential of hydrogen”) as related to pure water. The pH scale goes from 0-14. The pH of pure water is 7, precisely in the middle.

When an acid is dissolved in water, it becomes a solution with higher hydrogen ion activity than water, making it more acidic, with a pH value less than 7. When a base dissolves in water, it creates a solution with lower hydrogen activity than water, giving a pH value greater than 7. Bases that dissolve in water are called alkalis. To summarize:

  • Pure water
    • pH level: 7
    • Pure water can be swallowed by humans, is neither corrosive nor caustic, and will not burn human skin.
  • Acids
    • pH level: less than 7 (<7)
    • Named from the Latin acidus or acere, meaning sour.
    • Acids are corrosive.
    • Acids lose their acidity when combined with alkalis.
    • Examples are: citric acid (lemon juice), acetic acid (vinegar), stomach acid, and battery acid.
  • Bases
    • pH level: greater than (>7)
    • Bases that can dissolve in water are also known as alkalis, or alkaline substances.
    • Alkalis are caustic.
    • When highly concentrated, a corrosive substance will cause a chemical burn.
    • Examples are: sea water, baking soda, ammonia, garden lime, and strong lye.

To recap: the further you get from pure water on the pH scale, the more corrosive or caustic a substance becomes, and thus the more harmful to human skin (for example). On the low end of acids, you can drink orange juice, and on the low end of bases, you can swim in sea water. On the high end of acids, you have battery acid, and on the high end of bases, you have bleach, drain cleaner, and lye, which you may remember from the 1999 movie Fight Club. It occurred when Brad Pitt’s character mixed human saliva with lye on Edward Norton’s character’s skin and stated, “This is a chemical burn. […] You can use water and make it worse, or use vinegar to neutralize the burn.” Vinegar is a 2 on the pH scale, an acid that can indeed neutralize a strong base like lye (a 13 on the pH scale).

Acidic and Basic Amino Acids

Of our amino acids, which are acidic, which are base, and why does it matter? First we’ll state which is which, while quickly pointing out that the acidity of amino acids is measured with a pKa number, obtained by applying a logarithm; simply put, pKa measures acid strength, while pH measures the hydrogen content of a solution.

As a further example, for acids that means the smaller the pKa number, the more acidic the substance, and thus the lower the pH value.

Acidic Amino Acids

The two acidic amino acids are:

  • Aspartate (aspartic acid)
  • Glutamate (glutamic acid)

Acidic amino acids are those with acidic side chains, specifically containing carboxylic acid groups with pKa measurements low enough to lose protons and become negatively charged. Acidic amino acids are also by their nature hydrophilic amino acids (meaning they like water, as opposed to hydrophobic amino acids), and polar amino acids (meaning they are positively charged, as opposed to nonpolar amino acids).

Basic Amino Acids

The three basic amino acids are:

  • Arginine
  • Histidine
  • Lysine

These basic amino acids are so classified because they have basic side chains containing nitrogen, which resemble ammonia (a base). The pKa values of basic amino acids are high enough to bind protons and give them a positive charge. By nature, basic amino acids are also polar amino acids, and are also hydrophilic, just like the acidic ones.

A for Acid, B for Base, C for Conclusion

In conclusion and to summarize: the difference between acidic and basic amino acids is the same as between any acid and base in chemistry and chemical substances. Their similarities still include being polar amino acids, as well as hydrophilic amino acids, and, of course, the biggest thing they have in common is that they’re all still amino acids, with the same basic structure.

Though some are essential and some nonessential, the reason amino acids matter, and the reason that all these tiny permutations matter, is because without each of them working together, our health and well-being would fail. We at Amino Co. have developed amino acid supplements specifically because we understand their vital importance to human life. The chemistry behind each person’s daily concert of amino acids is the science that drives our passion.

Are Beans a Complete Protein?

Find out whether beans are a complete protein, and also learn about the health benefits that beans have to offer for weight management, digestive comfort, heart health, and blood sugar control.

You’ve heard about complete proteins, and you know that beans are a great non-animal protein source, but you find yourself asking, “Are beans a complete protein?” We will provide you with that answer, as well as the specific definitions of what makes a complete protein, and whether or not so-called “complementary proteins” get the job done in providing you with all nine of the essential amino acids that keep your body growing and functioning.

What Is a Complete Protein?

When someone speaks of a “complete protein” they are referring to the amino acid content of a food. Amino acids are the building blocks of protein in the body, meaning they are involved in building muscle, repairing tissue, and so much more (like producing your much-needed hormones).

There are 20 different amino acids in the human body, nine of which are considered essential, meaning they must come from a food source because the body can’t create them in-house. A complete protein has all nine of these essential amino acids, not least because for protein synthesis and muscle creation in the body, all nine are necessary.

Examples of complete proteins are eggs, chia seeds, Greek yogurt, quinoa, and soybeans. These are all great sources of protein that are either non-meat or plant proteins, and thus are especially valuable for those keeping vegetarian diets as well as vegan diets (where it’s all the more difficult to get enough protein).

When talking about foods, complete proteins must have all nine essential amino acids in sufficient amounts. If a food is lacking in one or two amino acids, it needs to be eaten with a complementary protein to make for a complete protein meal.

What Are Complementary Protein Combinations?

When you have a food that has, say, eight out of nine essential amino acids, or you have a food with all nine but two of the amino acids are only present in trace amounts and, therefore, not enough for your body to effectively use, well… what then? Of course, it’s not as if an incomplete protein is suddenly trash food to be thrown to the wolves, so what can you do?

No worries: if a complete protein is what you’re after, then you might easily pair two foods in one dish, each of which have complementary amino acid profiles. What one food lacks, the other makes up for, and vice versa!

One of the best-known examples is hummus eaten with pita bread. The protein in whole wheat is almost complete, deficient only in the amino acid lysine. Meanwhile the protein in chickpeas does contain a significant helping of lysine, which together makes this Middle Eastern staple a complete protein snack. Combine one whole wheat pita and 2 tablespoons of hummus, and you net 7 grams of protein. Other easy combinations for complementary protein sources include a whole wheat bread and peanut butter sandwich, hemp seeds added to a dish with lentils, or non-Greek yogurt combined with almonds or sunflower seeds.

So… Are Beans A Complete Protein?

The answer is: not without rice! Most beans are high in lysine but low in the essential amino acid methionine. Whole grain rice on the other hand is low in lysine, but rather high in methionine. On top of that, rice and beans is one of the simplest and most affordable vegan meals around (for those who are only interested in plant sources of protein), and one of the easiest sources of protein you can make for dinner. In a 1-cup serving of rice and beans you can gain a complete protein content of 7 grams. This meal choice is also a great way to load back up on carbs and protein after a workout.

The Many Health Benefits of Beans

Beans are valuable not just as a source of protein for your daily protein requirements, but for many more of the nutrients your body needs. Check out the following nutrition facts about beans, and see if you don’t feel like making rice and beans a regular staple of your household.

Learn whether beans are a complete protein.

The Bean Family

Beans are seeds that come from the Fabaceae flowering plant family, and are technically classified as legumes (a member of the pea family). Other legumes are peanuts, lentils, and (of course) peas. The bean family includes the following varieties:

  • Black beans
  • Soybeans
  • Garbanzo beans
  • Pinto beans
  • Lima beans
  • Black-eyed peas
  • Kidney beans
  • Navy beans
  • Red beans

The Health Benefits of Beans

Outside of its protein and amino acid content, check out just what else beans can offer to your health and well-being with these six facts.

1. Nutrient Density

Beans are full of the vitamin folate, which is vital for pregnant women and for anyone in their early childhood or adolescence, which are periods of time when we are growing rapidly. Note here that dried beans have close to double the folate of canned beans. Though it may take an extra step in preparation, cooking your own beans from their dried form is better for you in the folate department. However, even canned beans contain more folate than so many other foods, so they’re still worthy of inclusion if they’re easier for you to work with. A lack of folate can lead to folate deficiency anemia, which can result in heart palpitations, fatigue, irritability, and loss of appetite.

Some other important nutrients in beans include zinc, iron, magnesium, and fiber, needed regularly in our diets for comfortable digestion and gut health.

2. Heart Health

Consuming beans on a regular basis shows a correlation in scientific studies to a reduced likelihood of death from stroke, heart attack, and other cardiovascular diseases. A multi-study analysis from 2013 showed a clear connection between the consumption of beans and a reduction in risk from coronary heart disease, while even more research suggests that beans have the potential to lower dangerous LDL cholesterol levels, another contributor to heart disease.

3. Antioxidant and Anti-Cancer Properties

Rich in the antioxidants known as polyphenols, which help combat the damage done by free radicals in the body, beans can help prevent certain forms of cancer according to the American Institute for Cancer Research, as well as unhealthy inflammation. There has been research showing that black beans specifically have the highest antioxidant effect, which you may want to take into consideration when you’re choosing between beans at the grocery store.

4. Glucose Metabolism and Diabetes

Because beans are high in fiber, they can help prevent diabetes and stabilize blood glucose levels. Beans are often considered a diabetes superfood, with the American Diabetes Association saying specifically that pinto, navy, kidney, and black beans are each full of important vitamins and minerals like potassium and magnesium. Soybeans are also contributors to pancreatic health, and the pancreas produces the insulin that regulates blood sugar in the human body.

5. Appetite Control

Not only do people often feel fuller after eating beans due to their starch and fiber content, which cuts down on their caloric intake each day, but these healthful aspects of beans can even help prevent food cravings in the first place. Appetite control means a greater ease at losing body weight, which is valuable for those struggling with obesity and the health concerns that accompany the condition.

6. Preventing Fatty Liver Issues

When fats accumulate in the liver, it could lead to the metabolic disorder that is fatty liver disease. Beans can contribute to the prevention of nonalcoholic fatty liver disease, another health benefit from this protein provider (even if it’s not at the golden ratio of a “complete protein”).

These Beneficial Beans: Are There Any Downsides?

The most common complaint about beans is that they can cause gas and increase intestinal discomfort as a result (beans, beans, the musical fruit…). Though it’s usually not dangerous, some may find having extra gas to be quite unpleasant. There is a way to better avoid the issue: by hot-soaking, boiling, or pressure-cooking beans, you can reduce the chance of having gas or intestinal issues as a result of your meal. This practice may also be of use to those with IBS or inflammatory bowel syndrome who may want to include the protein and nutrients of beans in their diet, but must be wary of the strong fiber content on the digestive tract.

Protein, Pro-Beans

Long story short: no, beans are not considered one of the independent sources of complete protein, but they can easily become complete when paired with whole grain rice or cornbread (which go together as well as red beans and rice in that they’re all complete proteins). When searching for complete protein foods, it’s vital not to limit yourself when complementary proteins combos are available as well. You should welcome beans into your diet not just for the sake of your health, but for the rich variety of flavors and textures that make living well both a pleasure and a joy.

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 Amino Acid Functional Groups?

What is an amino acid functional group? This article will answer that question with information on amino acid classification and how proteins (and possibly all life on Earth) are formed.

What are Amino Acid Functional Groups?

So you’ve heard of amino acid functional groups and you want to understand them better. This article will help to clarify the structure of amino acids, their functional groups, and what it all has to do with the creation of protein.

Some Basic Reference Definitions

Below are the names of the 20 common amino acids in the body, nine of which are essential amino acids, meaning humans must eat or otherwise consume them to get what we need to function. The essential aminos are designated with an asterisk (*). There are their names, their three-letter codes, their one-letter codes (as used in drawing models of molecular bonds), plus their bond type and properties. Polar vs. nonpolar bond types refers to their covalent bonds. We will start with those definitions for the bond type category—get ready for some high school clique metaphors to help you visualize all this organic chemistry.

Covalent Bonds

Covalent bonds form the base of the chemical reactions between atoms of different elements. The bonds form in only one way: when an electron becomes shared by two elements. That creates the connection that then results in a new substance. Covalent bonds can exist as polar or nonpolar compounds, and all bonds that are polar or nonpolar in nature are by definition covalent.

To visualize: think of these bonds like the bonds of friendship. Two students (atoms) come close to one another and share their lunch (electrons). This sharing means there is a bond of friendship (the covalent bond). Whereas before they had been two separate elements, strangers, now a new substance has formed: a friendship.

Polar Bonds

Polar bonds are bonds where the electrons are not shared equally between two atoms. These types of bonds are what designates polar molecules from nonpolar ones. This occurs when the two atoms bonding are from two different elements; atoms from the same element do not form polar bonds.

Just as bigger planets can hold bigger moons in their orbits, so it is with atoms: they pull electrons to the best of their ability, but when they come into the orbit of a better puller (a bigger planet), that atom will pull more electrons into its orbit (and steal the lesser planet’s moons).

When two atoms of the same element meet, neither is stronger than the other, and thus neither one is more attractive than the other regarding electrons, and so neither side exhibits the polar pull, and the bond is considered nonpolar. The negative charge end of the bond is the more attractive atom, because it can draw more negative (-) electrons.

To put this back into the context of our high school friends, let’s say the two atoms meeting and bonding are a vivacious theater student and a more reserved math student. In sharing lunch, somehow the theater student always gets more to eat because the math student is so transfixed and feels the need to be overly generous. This is true whenever the theater student meets someone with less personal magnetism, which means the theater student gets an overabundance of food (electrons), which is negative because the increased calories may cause the theater student to gain weight, or get a bad complexion from eating too much processed lunch food. Eventually the theater student will fill up to the brim with extra food, and won’t be able to accept any more.

Nonpolar Bonds

A nonpolar bond is formed when two atoms from the same element meet and share electrons equally and evenly with one another. Neither atom is a better electron puller than the other, and so there is no one side more polar than the other.

In our friendship metaphor, this is a bond between two theater students, or two math students, who pool all of their lunch food together in the middle of the table, and pull from the pile equally and in unison.

Hydrophobic vs. Hydrophilic

For the properties category, hydrophobic and hydrophilic refer to molecules and their reactions to water. Molecules that repel water, or are phobic of hydration, are hydrophobic. The molecules that can form an ionic or hydrogen bond with a water molecule are hydrophilic, they have a philia for water, they like the feel of it.

If atoms are students once again, the hydrophilic ones are either on the swim team itself, or part of a group that likes to swim and heads out to the beach or the lake every weekend. The hydrophobic ones either can’t swim or simply do not like it. Hydrophobic students will tell you that their friends and the community pool go together like oil and water: they don’t mix.

Your Amino Acids: Names and Designations

Amino-acid name: Alanine Amino-acid name: Arginine
Three-letter code: Ala

One-letter code: A

Bond type: Nonpolar

Properties: Hydrophobic

Three-letter code: Arg

One-letter code: R

Bond type: Polar, positively charged

Properties: Hydrophilic

Amino-acid name: Asparagine Amino-acid name: Aspartate
Three-letter code: Asn

One-letter code: N

Bond type: Polar, no charge

Properties: Hydrophilic

Three-letter code: Asp

One-letter code: D

Bond type: Polar, negatively charged

Properties: Hydrophilic

Amino-acid name: Cysteine Amino-acid name: Glutamate
Three-letter code: Cys

One-letter code: C

Bond type: Nonpolar, no charge

Properties: Hydrophilic

Three-letter code: Glu

One-letter code: E

Bond type: Polar, negatively charged

Properties: Hydrophilic

Amino-acid name: Glutamine Amino-acid name: Glycine
Three-letter code: Gln

One-letter code: Q

Bond type: Polar, no charge

Properties: Hydrophilic

Three-letter code: Gly

One-letter code: G

Bond type: Nonpolar, no charge

Properties: Hydrophilic

Amino-acid name: Histidine* Amino-acid name: Isoleucine*
Three-letter code: His

One-letter code: H

Bond type: Polar, positively charged

Properties: Hydrophilic

Three-letter code: Ile

One-letter code: I

Bond type: Nonpolar

Properties: Hydrophobic

Amino-acid name: Leucine* Amino-acid name: Lysine*
Three-letter code: Leu

One-letter code: L

Bond type: Nonpolar

Properties: Hydrophobic

Three-letter code: Lys

One-letter code: K

Bond type: Polar, positively charged

Properties: Hydrophilic

Amino-acid name: Methionine* Amino-acid name: Phenylalanine
Three-letter code: Met

One-letter code: M

Bond type: Nonpolar

Properties: Hydrophobic

Three-letter code: Phe

One-letter code: F

Bond type: Nonpolar

Properties: Hydrophobic

Amino-acid name: Proline Amino-acid name: Serine
Three-letter code: Pro

One-letter code: P

Bond type: Nonpolar

Properties: Hydrophobic

Three-letter code: Ser

One-letter code: S

Bond type: Polar, no charge

Properties: Hydrophilic

Amino-acid name: Threonine* Amino-acid name: Tryptophan*
Three-letter code: Thr

One-letter code: T

Bond type: Polar, no charge

Properties: Hydrophilic

Three-letter code: Trp

One-letter code: W

Bond type: Nonpolar, no charge

Properties: Hydrophobic

Amino-acid name: Tyrosine Amino-acid name: Valine*
Three-letter code: Tyr

One-letter code: Y

Bond type: Polar, no charge
Properties: Hydrophilic

Three-letter code: Val

One-letter code: V

Bond type: Nonpolar

Properties: Hydrophobic

It’s a lot of information, to be sure, but it’s provided as a reference point to help facilitate the following explanations.

What Are Amino Acid Functional Groups?

Amino acids are all made up of groups of atoms, and the functional groups are the important ones in each amino, it’s what makes them different and unique, deciding whether the amino overall is polar or nonpolar, acidic or basic.

Each of the above standard 20 aminos have one hydrogen atom, and two groups attached to its alpha carbon atom: an amino or amine group (~NH3+) and a carboxyl group (~COOH). They are each then distinguished from other types of amino acids by their third attached functional group: side chains referred to as R groups. When you ask what are amino acid functional groups, here they are, with the R group being the one with the most diversity. When you think of R groups, think R for radical, as it’s the variable part that makes each amino acid different from the rest.

What is the amino acid functional group?

About R Groups

Of the 20 standard amino acids that make up the building blocks of protein:

  • 6 of them have hydrocarbon R groups
  • 7 of them have neutral R groups
  • 6 of them have acid or base R groups

The simplest of the amino acids is glycine, which has just one hydrogen atom in the position of the side chain group (no R group at all, just an attached loner).

Some Quite Interesting Relevant Facts

  • In chemistry, organic compounds are generally thought of as any chemical compound that contains carbon, which includes amino acids.
  • All amino acids are soluble in an aqueous solution (water), even the hydrophobic ones (counterintuitive but true).
  • All naturally occurring amino acids are in the L-form; L for levorotatory, referring to the way you’d turn the amino acid to read the order of its attached groups (the opposite of is dextrorotatory or D-form).
  • As you can see in the above list, 50% of the amino acids have nonpolar side chains. The other half is designated polar, five of which have side chains that are not only polar, but charged.
  • Because the carboxyl group is an acid, it can form peptide bonds with the base amino groups of other amino acids, causing chemical reactions that create polypeptide chains and amino acid residues.
  • When two amino acids react and form a peptide bond, and that process goes on to be repeated, many amino acids may string together, which forms a protein structure.
  • This protein synthesis (though a little more complicated than just linking acid to base over and over again like links of a chain) is among the most fundamental of biological processes, an invaluable component of every cell. Proteins make our nails and hair, protein builds and repairs our tissues, protein is needed to make our hormones, our enzymes, and many other chemicals in the human body.
  • In 1953, Stanley Miller and Harold Urey conducted a simulation, to test a hypothesis about how life originally formed on Earth. They built a closed system that contained a heated pool of water under a mixture of gases that were thought to be present in the early atmosphere of Earth. They delivered an electric current to simulate lightning, and after a week analyzed the contents of the liquid pool. In there they discovered that several organic amino acids had spontaneously formed from inorganic raw materials. This leant support to the theory that the first life on Earth arose out of the primordial ooze through naturally occurring chemical reactions like a little flash of lightning.

Conclusion

The functional or R groups of amino acids are the groups that define the chemistry of proteins. They are the basis on which amino acids are classified, and according to the Miller-Urey experiment, possibly the start of all organic life on Earth. Not only is “What are amino acid functional groups?” a stimulating question to ask, but the answer to that question comes awfully close to revealing the true answers behind life, the universe, and…well…everything.

BCAA vs. Creatine: What You Need to Know

BCAA vs. creatine: a comprehensive look to help you decide which you should choose, or whether you’d rather utilize a product that combines the two supplements for better energy, muscle strength, and protein synthesis.

If you spend enough time in the gym, you will eventually run across this question: BCAA vs. creatine, which supplement do you prefer? Before you can answer that question, you’ll need the information behind both BCAAs and creatine: what are they? What are the upsides and downsides to each? How can they help build muscle? Can they both be taken together? You’ll find the answers to all of those questions here, plus learn about the one ultimate supplement that perfectly marries the two together, so you never have to compromise for imbalance in your muscle-building nutrients.

BCAA vs. creatine: a comprehensive look.

What Is BCAA? What Is Creatine?

We’ll start with the definitions, and then move on to the differences between these two supplement options.

BCAA: Branched-Chain Amino Acids

A BCAA supplement is made up of branched-chain amino acids, specifically the three amino acids leucine, isoleucine, and valine. There are a total of nine essential amino acids, essential because you must eat or otherwise consume them to get them (other amino acids are produced in-house by your body). Leucine, valine, and isoleucine are essential amino acids.

“Branched-chain” refers to the molecular structure of these three specific amino acids. The chemical bonds branch off of the main structure.

Studies have shown that BCAAs help reduce muscle damage and soreness in post-workout recovery.

While it’s possible to get a sufficient amount of the BCAAs from your diet, for those who work out intensively, and/or for those on specific diets aimed to lose weight, it might be difficult to get the right amino acid balance, which is why some will chose a BCAA supplement in the hope that it will round out their nutrients. However, it should be noted here that muscle synthesis cannot take place without all nine essential amino acids, so a complete essential amino acid (EAA) supplement is preferable to a BCAA one—you cannot build muscle with only a third of the necessary ingredients.

To cut calories without having a negative impact on protein intake for muscle mass is important, and BCAAs are often taken to try to ensure there’s no interruption to protein synthesis while dieting. Even if weight loss isn’t your goal, the BCAAs gained from taking a complete EAA supplement might still help in that department by contributing to appetite control.

BCAAs have similar benefits to a whey protein shake, but with fewer calories. Moreover, the amino acid leucine is one of the two specifically ketogenic amino acids, another way that BCAA supplements contribute to fat loss (the ketogenic diet is all about burning off fat, and doing it both quickly and safely).

BCAA supplements are perhaps best suited for CrossFitters, bodybuilders, or rowers, but again, they are only a third of the essential amino acids, all of which are necessary for muscle building.

BCAA Quick Facts

  • BCAAs provide three of the nine essential amino acid building blocks of muscle tissue.
  • BCAAs help protect lean muscle and guard against muscle wasting.
  • BCAA supplements are a source of longer-term energy, and can help reduce exercise fatigue.
  • BCAAs help promote fat loss via appetite suppression and increased metabolism for burning calories.
  • BCAA supplements provide higher strength gains than whey protein does.
  • There are no harmful side effects reported from BCAA supplementation.

Creatine: The Energy Protein

Creatine is creatine monohydrate, the protein found in animal sources of meat like fish, poultry, pork, and red meat. Creatine contains two different amino acids, arginine and methionine, of which methionine is essential.

Unlike the weight-loss potential in BCAA supplements, taking creatine can lead to initial weight gain, as it causes some water retention in the muscles. Likewise, if you’re not drinking enough water while taking creatine, cramping can occur, meaning it’s more important than ever to stay hydrated while working out.

Researchers have stated that creatine might help lessen the effects of osteoarthritis, slowing the loss of bone mass as you age. Another unique benefit of creatine is its ability to deliver the rapid energy that is needed during fast muscle contractions (when sprinting, for example). That means creatine gives you longer endurance, which means more reps, which means more muscle growth. This is why creatine is best suggested for powerlifters or sprinters, and why it’s a part of our unique EAA blend (see below for further details).

Creatine Quick Facts

  • Creatine breaks down into phosphocreatine (CP), which provides rapid energy for muscle contractions.
  • Creatine causes the release of the anabolic hormone IGF-1, used in promoting muscle growth.
  • Creatine is a quick source of muscle energy, allowing for more reps.
  • Creatine use aids long-term bone strength for weight trainers.
  • Creatine increases strength during resistance training by up to 20%.
  • Some water retention and cramping is reported with the use of creatine, but the effects are short term.

BCAA vs. Creatine: Which Should You Use?

If you’re here to make a choice, now’s the time to review your fitness goals and how each of these products might influence them. Research suggests that BCAAs help to increase muscle mass for those doing resistance training. If your diet is low on protein intake, say if you’re vegetarian or vegan, BCAA supplements are a great way to promote muscle protein synthesis, but remember that they are also only a partial supply of the amino acids you need for muscle building.

Likewise, a study also showed that muscle strength increased up to 8% for those using a creatine supplement while resistance training. Creatine can provide rapid energy when the usual muscle cell energy supply of adenosine triphosphate (ATP) is slow to regenerate, and it goes a long way towards the kind of strength building and increase to muscular force that might be preferred by powerlifters.

Both supplements aid muscle recovery, both contain at least one essential amino acid, both help drive protein synthesis, both of them are good to take as pre-workout supplements for their benefits, and honestly, unless you have a specific reason to not take one of them, you may be thinking that you want to take both. Well good news for you then, because you can! In fact, we recommend that you do.

BCAA and Creatine Together

You may have noticed that there was no overlap between the amino acids from BCAA supplements and creatine supplements, which means taking both will not overdose you on any one amino acid. Rather than think of them as enemies in some competition for supplement supremacy, BCAAs and creatine can be two valuable players on the same team: your team. Nothing bad will happen to you if you combine them (they’re not baking soda and vinegar in a third grader’s science fair volcano or anything), and since they both aid sports performance, boost muscle building, help with fat loss, and ease muscle recovery, when taken together you may see improved results in all of those categories.

However, if you’re after a full roster of the essential amino acids, there are amino acid supplements that include all three BCAAs, plus the other muscle-building EAAs. Whether you’re looking into supplementation because you’re lifting weights or attempting to lose body fat or both, a protein powder with only partial, unbalanced amounts of amino acids just won’t do the trick.

A Complete EAA Blend

When it comes to muscle-building supplements, our blended EAA formula not only contains eight of the nine essential amino acids, including the BCAAs, but it also supplies them with the energy of creatine and the steady amino acid digestion that comes from whey protein supplements (derived from milk).

This supplement is scientifically proven to increase human muscle growth and can help prevent muscle breakdown in the elderly. It was also designed to contain the exact ratio of amino acids needed to build muscles without overtaxing your body with excessive or unnecessary amounts of any one.

When building muscle, you don’t want to show up with a partial supply of the building blocks of protein. Instead, you want a comprehensive EAA supplement that helps all the work you do weight training at the gym to pay off. Instead of a dose of BCAAs here or a dash of creatine there, we recommend you get the most out of all of the above with our combination of EAAs with creatine and whey protein support. If the question is BCAA vs. creatine, the real answer is the Amino Company’s blends: for balance, for building, for the best of both worlds and more.

Most Popular Supplements for Muscle Growth

Learn the chemistry behind the traditional top supplements for muscle growth, and find out about the newest and most comprehensive supplement that’s about to revolutionize muscle building.

If you’re looking for supplements for muscle growth, you’ve probably already noticed that it’s a pretty crowded field. Different proteins and combinations and timing strategies get discussed, and before you know it you feel like you need about half a degree in chemistry just to build muscle at the gym! We’re streamlining the relevant information on muscle-building supplements, their pros and cons, so you can decide on the best supplements for your own fitness goals. If you’re in a rush, skip to the end, because there’s a new supplemental option that combines the best muscle growth nutrients you’ve ever known, all in one complete, balanced formula that will best all the rest. Read through to learn about the ideal muscle-building combo, a powerful protein trinity.

The First Steps Towards Muscle Building

Getting the most out of your workout involves taking a few first steps before you can start targeting muscle gain specifically. The first steps after taking up regular exercise are:

While supplements are not mandatory to reach these goals, they can be excellent aids to quicken your progress and maximize your protein intake without bringing unpredictable calories to your diet. Next up we’ll discuss the top supplements for muscle growth that you can choose from when attempting to gain muscle mass, and reveal a cutting-edge, scientifically-backed newcomer to the muscle-building supplement world.

Traditional Top Supplements for Muscle Growth

Over and above eating well and lifting weights, here are some protein and muscle-building supplements you can use to augment your workout goals, some of them more effective than others.

Top supplements for muscle growth and bodybuilding.

Carnitine

Carnitine is the general term for a group of amino acid compounds that include L-carnitine, acetyl-L-carnitine, and propionyl-L-carnitine. Carnitine is a transporter that moves long-chain fatty acids into mitochondria, where they’re oxidized or burned for energy.

A popular supplement for fat-loss, carnitine can also aid muscle growth by increasing blood flow to muscles, lessening muscle soreness, and increasing nitric oxide production, all of which improve your post-workout recovery. The combination of these benefits makes carnitine a strong asset for energy-boosting while you’re building muscles through exercise, especially when utilized in pre-workout and post-workout shakes. Though it doesn’t directly contribute to muscle building, it does provide valuable energy assistance, and improves performance during endurance athletics.

Pros

  • Aids athletic endurance by providing energy transport.
  • Helps ease muscle soreness and improve post-workout recovery.

Cons

  • Does not directly increase muscle, but instead aids in workout energy.
  • Carnitine is only a peripheral aid to individuals working to build muscle via exercise.
  • Carnitine would need to be taken alongside direct protein or amino acid supplements to be most effective.

Whey Protein Powder

A milk protein derived from whey, which is the watery part of milk that separates from the curd, whey protein is an excellent supplement affecting protein synthesis. With a high level of branched-chain amino acids or BCAAs, and including some amount of all nine essential amino acids (EAAs), this protein supplement digests relatively quickly and can help with rapid muscle building.

Whey protein can help increase blood flow due to its content of peptides, and is regularly consumed by bodybuilders immediately after their training sessions (within the hour). When choosing a whey protein, it’s recommended that you find a powder containing whey protein hydrolysates, which are proteins broken down for faster digestion.

Pros

  • Whey protein is a complete protein, containing all nine essential amino acids.
  • Whey protein is high in the branched-chain amino acids (BCAAs).

Cons

  • While whey protein is a fast-absorbing whole protein, free-form amino acids can be absorbed much more quickly.
  • Whey protein’s amino acid content is not optimally balanced, and a properly formulated essential amino acid supplement can have 3 times the effectiveness rate as a whey protein powder supplement alone.

Glutamine

Glutamine is an amino acid that not only helps build muscles by increasing the levels of the essential amino acid leucine in muscle fibers, but it also helps fight against muscle breakdown, and has been shown to play a significant role in protein synthesis.

Incidentally, glutamine can also be recommended for those with digestion issues (diarrhea or constipation), anxiety, cravings for sugar and/or alcohol, and those with poor wound healing.

Pros

  • Valuable as a precursor to the essential amino acid leucine.

Cons

  • Glutamine aids only one of the nine essential amino acids needed for muscle building, and so is far from being the most effective muscle-building supplement.
  • Glutamine is unnecessary if you’re taking a complete blend of essential amino acids.

Casein Protein Powder

Casein is the other milk protein that is derived from the curd of the milk and not the whey. Casein has a slower digestion rate than whey protein does, which makes it an excellent protein to take before bed, as it digests while you sleep and helps to prevent catabolism (which is to say destructive metabolism, a kind of self-cannibalism the body sometimes resorts to for energy).

Because increased calorie intake is also needed to build muscle, casein can help by being less filling than whey, allowing you to consume more alongside it. However, it’s also suggested that taking a combination of whey (or better yet free-form essential amino acids…read on!) and casein after a workout can help with muscle protein synthesis better than taking either one of them alone. Be advised that a casein protein product with micellar casein is the slowest-digesting form of casein readily available, and is your best bet when buying it as a supplement.

Pros

  • Casein protein has a slower digestion rate than whey, which can help prevent catabolism during sleep.

Cons

  • Works best when combined with stronger protein supplements like whey protein or free-form essential amino acids.

Beta-Alanine and Carnosine

Beta-alanine, an amino acid and key component of the dipeptide carnosine, aids in increasing carnosine levels and thus heightening muscle strength and muscle endurance. Higher levels of carnosine also increase the force of muscle contractions, and combining it with creatine (next on the list) has the greatest effect on losing body fat and gaining lean tissue, as was seen when the two were studied during a 10-week resistance training program conducted with collegiate football players.

Pros

  • Carnosine contributes to muscle endurance, leading to more powerful workouts, which can then translate to increased muscle.

Cons

  • Carnosine does not directly build muscle, but instead helps aid in workout endurance.
  • Carnosine is most effective in combination with proteins like creatine or free-form amino acids, and so is best as peripheral support for muscle building.

Creatine

Popularized as a workout supplement in the 1970s, creatine is made up of three amino acids—glycine, arginine, and methionine—and is vital for supplying the energy for muscular contraction. Creatine can be found in the forms reatine alpha-ketoglutarate (AKG), creatine monohydrate, and creatine malate. Creatine has been shown to increase the levels of insulin-like growth factor-1 (IGF-1) in resistance-exercise training, which is essential for stimulating muscle growth.

Creatine is converted to phosphocreatine (CP) in the body, which then provides energy for explosive exertions like heavy weight lifting or sprinting. The creatine-phosphocreatine system provides an increase in energy supplied to muscle cells when your body is using more ATP (adenosine triphosphate) than is being regenerated in the cells’ mitochondria. This increases your athletic endurance.

Pros

  • Provides energy for increased exercise performance, especially when you’re using more ATP than the mitochondria of your muscle cells can regenerate.
  • Creatine helps stimulate muscle growth.

Cons

  • Creatine is not most effective when taken alone, but is instead at its best when paired with an essential amino acid (EAA) supplement, where it will help provide the energy needed for increased muscle protein synthesis.

Nitric Oxide Boosters (Arginine)

Nitric oxide (NO) in the body serves to dilate blood vessels, thus allowing better blood flow to muscles, providing them with energy, nutrients, water, anabolic hormones, and oxygen—everything your muscles need to function, grow, and thrive. Nitric oxide boosters do not contain nitric oxide, but instead provide it via the amino acid arginine, which the body converts into nitric oxide.

Arginine supplements are often marketed based on their association with muscle growth, increased muscle strength, and loss of bodyweight. However, we recommend supplementing with citrulline to increase arginine, as arginine supplements don’t produce significant increases in blood arginine concentrations due to the liver’s effectiveness at clearing absorbed arginine. Citrulline, on the other hand, is converted into arginine by the kidneys, and the arginine is then released into the bloodstream; this more effectively increases your arginine levels. Additionally, there are no adverse effects associated with citrulline supplementation, while arginine consumption can sometimes lead to gastrointestinal discomfort.

Pros

  • Arginine in the bloodstream leads to more readily available amounts of nitric oxide, essential for muscle functioning.

Cons

  • Counterintuitively, arginine supplements are often ineffective at supplying useable arginine to the bloodstream.
  • Instead citrulline is recommended to supplement for an effective increase in arginine, and can be taken alongside or included in EAA and protein supplements for optimal muscle performance.

ZMA (Zinc, Magnesium Aspartate, Vitamin B6)

Supplementing the minerals zinc and magnesium aspartate along with vitamin B6 is sometimes important to bodybuilders because they become depleted during intense training and need to be specifically replaced. These nutrients are necessary for maintaining proper sleep and hormone levels, as testosterone particularly can be compromised by intensive training.

Athletes who take ZMA have been shown to have increased levels of IGF-1 and testosterone, both of which have an influence on muscle gains. ZMA is recommended to be taken before bed on an empty stomach, to allow for better uptake and to help improve sleep quality and the muscle recovery that sleep provides.

Pros

  • Can help correct vitamin and mineral deficiency caused by intensive weight training.

Cons

  • ZMA supplementation does not lead to direct muscle growth, but can be taken as needed alongside free-form amino acids or traditional protein contributions like whey or creatine, depending on your workout style and your body’s needs.
  • Not everyone will need the extra supplementation of ZMA.

HMB (Beta-hydroxy beta-methylbutyrate)

Beta-hydroxy beta-methylbutyrate or HMB is a molecule derived from the processing of the essential amino acid leucine, and helps protect against muscle protein breakdown. HMB is often recommended only for those who are beginning weight-training exercises, as the scientific results seen in those who are more experienced with muscle training are less significant. This is due to the fact that HMB is heavily reliant on a steady and abundant supply of EAAs to be effective. When the EAA supply dips down, so does the effectiveness of HMB; it cannot work alone.

Pros

  • HMB supplementation can be good for resisting extreme catabolic states, such as in individuals with critical wasting illnesses.

Cons

  • HMB without an excess supply of EAAs is only marginally effective.
  • EAA supplementation is also needed to derive maximum benefits from HMB supplementation.

Branched-Chain Amino Acids (BCAAs)

The branched-chain amino acids are a subcategory of essential amino acids, and are designated by the molecular structure of leucine, isoleucine, and valine. BCAAs make up 14% of the amino acids that reside in your muscles, and it’s been shown that taking a supplement of BCAAs during resistance-training exercise increases muscle strength, fat loss, and lean mass.

However, while research shows that leucine in particular stimulates muscle protein synthesis, and that together these three amino acids diminish cortisol (a catabolic hormone), increase energy, and reduce delayed-onset muscle soreness, BCAAs when consumed alone are not fully effective. All nine essential amino acids are needed to make new muscle, and in fact, the the rate of muscle protein synthesis is directly affected by the availability of all your essential amino acids—the more you have, the faster your rate of muscle synthesis, and the fewer you have, the slower the rate. Because of this, research actually shows that BCAAs when taken alone have little to no effect on the rate of muscle protein synthesis in humans.

Pros

  • BCAAs are valuable amino acids that can be taken to help some aspects of muscle building.

Cons

  • BCAAs are only three of the nine essential amino acids, and all essentials are needed to create new muscle.
  • BCAAs have little to no effect on muscle protein synthesis when taken alone.

An Essential Amino Acid (EAA) Blend: The New Top Muscle Growth Supplement

If BCAAs ever sounded good, you’ll probably be more interested in a complete EAA supplement. Our unique EAA supplement is an ideally proportioned blend that combines the strengths of whey protein, creatine, and the eight essential amino acids that contribute directly to muscle growth. With our EAA blend, you’ll not only get the BCAAs mentioned above, but also a full cocktail essential amino acid supplement. It contains the key factors that make whey protein and creatine effective too, giving you the best of every top effective traditional supplement on the market.

EAAs and Muscle Protein Synthesis

The human body is made up of about 20% protein, and amino acids are used to form our muscles, tissues, and organs (not to mention the hormones needed for cognitive and physiological function). The key to our muscle-building product that helps make it more effective than other supplements, and even some dietary sources of essential amino acids, is its absorption rate and digestibility.

The EAAs derived from dietary proteins have to be digested first and then absorbed, while free-form amino acids are absorbed more quickly and completely. With eight of the nine essential amino acids (minus tryptophan which is not necessary to supplement for muscle protein synthesis), the amounts of EAAs are maximized more than any naturally occurring protein can deliver.

EAAs with Whey Protein’s Support

While free-form EAAs provide faster absorption, an intact protein like whey provides for a longer absorption period, sustaining the supply of EAAs after the rapid absorption of the free-form EAAs. Designed to work in concert with one another, our muscle-growth supplement combines its EAA profile with a balanced inclusion of whey protein for steady, ongoing support of muscle protein synthesis.

EAAs and Creatine’s Energy

Because creatine-phosphate provides the energy for sudden bursts of physical activity like lifting heavy weights or sprinting, it’s included in the Amino Co.’s technology to provide the energy needed to convert EAAs into muscle via muscle protein synthesis. Instead of waiting for the mitochondria of muscle cells to metabolize ATP for energy, creatine covers the time gap when needed, completing the full circle required for ideal muscle building: the rapid essential ingredients, the long-haul supply, and the energy to put them to use.

The Amino Company Advantage

Our product is a unique, patent-pending blend of essential amino acids, whey protein, and creatine that outperforms all other supplements in increasing muscle mass. Good for increasing strength in the elderly and easy to include in drinks or smoothies, Amino Co. supplements are scientifically proven to be effective in muscle protein synthesis over any other supplement, food, or protein choice currently available.

The ABCs of Muscle Growth

On a first glance at muscle growth supplements, it looks like an alphabet soup of vitamins and molecules and chemistry notes, but the more knowledgeable you become about your own body’s strengths and needs, the closer you’ll approach a PhD’s level of understanding when it comes to which supplements best support your goals. Effectiveness is key, bolstered by practical results that can be not only felt, but also scientifically proven. In the end, you can see which supplement brings you the greatest value.

The strongest performers from the traditional list of muscle growth supplements have been brought forward to the new frontier: an EAA blend that brings the best of everything essential to building and maintaining new muscle. The Amino Company provides the full circle of quick, long-lasting, and energized EAAs for muscle building. When you take our unique blend, you’re guaranteed to have an optimally balanced formula designed specifically for human muscle growth (and not lab animals). With the Amino Co. on your team, you can reach higher heights of strength faster and more effectively than ever before!