The Most Complete Guide To Protein: Muscle Building & More
20 min read
- Plant-Based protein is the superior choice for any serious athlete looking to get the most out of their training and recovery.
- Whey protein supplements have nasty side effects that can negatively affect overall health and performance.
- The leucine threshold is an important factor in kickstarting muscle protein synthesis.
We're breaking down protein in it's entirety to help you understand how much protein you really need, how to choose the best sources, and the key to building muscle.
It’s no secret that you need to include protein in your diet in order to maintain or even gain muscle. Protein is something we all need. In fact it is one of the fundamental building blocks of life.
Protein, in the simplest definition, is one of the primary macronutrients that make up the human body. Everything from cellular structure to our bones, muscles, hair, skin, nails is made of protein. Even the enzymes that help break down and digest food and facilitate chemical reactions in the body require protein to function, grow, and thrive.
But protein is a lot more complex than what it seems, both in the molecular structure and in how it works with the human body.
And while it’s clear that we all need protein to thrive as humans, what isn’t so obvious is the protein requirements for us as individuals based on our fitness, performance, and health goals.
It’s no wonder that some of the most highly searched questions on the internet about nutrition relate to protein in some way, shape or form.
How much protein should you really consume each day? And why do we even need it in the first place?
And these are important questions. It doesn’t matter if you're an elite level athlete, a weekend warrior, or just an average joe trying to look and feel a little better, this post was written to uncomplicate macronutrient we’ve all grown to love and provide the insight you need to fuel your pursuit for optimal human performance.
With that said, let’s get started.
What Exactly Is Protein Anyway?
Protein is the most abundant molecule, apart from water, in our bodies. When most people think about protein, they usually connect it with muscle building. And rightfully so.
Protein does play an important role in building and maintaining lean muscle, but it’s not just protein that’s doing the heavy lifting here. In fact, it’s all the bits and pieces that protein is made of, known as amino acids.
These essential building blocks are found in every cell and tissue throughout the body and categorized into two groups: essential and non-essential amino acids. We’ll get into more details on the difference between these two in a bit. For now, all you need to know is that amino acids are the individual components that make up protein. The types and combination of amino acids is one important factor in assessing the quality and completeness of protein.
Protein facilitates the digestion and absorption of nutrients. It acts as a lock and key mechanism, providing access to shuttle nutrients into the interior of a cell, and facilitates the removal of waste and toxins. It even goes into the hormones our bodies use to balance and regulate hundreds of systems and functions, from blood sugar to emotions.
Protein combines with vitamins and minerals to do even more. Protein can move oxygen from the lungs and to cells that desperately need it to survive, act as antioxidants (cleaning up free radicals that do cellular damage and contribute to cancer and aging), and aid the immune system in recognizing and removing threats to our health and wellness.
What makes protein an essential nutrient?
Out of the three macronutrients (protein, carbs, and fats) only two are actually essential. Dietary fat provides essential fatty acids that the body cannot make on their own and protein provides essential amino acids. Carbohydrates, on the other hand, don't provide any specific mechanism that the body can do without.
That’s because the body can switch between the two for energy production. Using fat for fuel happens through a process known as ketosis and releasing stored glycogen from the liver via gluconeogenesis.
Without getting too far into the weeds of biochemistry, when it comes to macros, only protein and fat are actually essential because the body doesn’t actually need carbohydrates to function.
For a deeper dive on the full list of essential nutrients for humans click here
Now, we’re not suggesting that you should forego carbs altogether because they can help to facilitate muscle growth in combination with protein, but they simply aren't a requirement for human physiology. Additionally, carbs are the primary source of beneficial prebiotic plant fiber that the microbes in our gut need to flourish.
Finding the balance between fat and carbs is something that varies widely depending on your training goals, your willingness to give up certain foods, and a whole range of other considerations that are beyond the scope of this article.
Protein, on the other hand, plays an entirely different role which allows us to set some more concrete guidelines for meeting your daily optimal intake.
When it comes to protein, it’s not common to experience a deficiency. Most medically reported instances of a protein deficiency, known as kwashiorkor, occur only in extreme malnourishment conditions in third world countries within populations that don’t have access to basic human nutrition.
With protein deficiency not something that many of us will ever experience first-hand, it’s interesting to see so many queries wondering if we’re actually getting enough.
Sure, as a society, we eat enough protein to prevent deficiency, but you could certainly argue that many of us would be better off getting more than the basic requirements, which for some odd reason have been reduced over time.
If building lean muscle is anywhere on your list of goals, you’d be foolish to skimp on your protein intake.
Numerous studies suggest that a high-protein diet has major benefits for weight loss and metabolic health.
Here are 9 science-based reasons to eat more protein.
- Reduces Appetite and Hunger Levels
- Increases Muscle Mass and Strength
- Lowers Your Blood Pressure
- Boosts Metabolism and Increases Fat Burning
- Reduces Cravings and Desire for Late-Night Snacking
- Good for Your Bones
- Helps Maintain Weight Loss
- Helps Your Body Repair Itself After Injury
- Helps You Stay Fit as You Age
"How Much Protein Do I Need?"
The short answer: More than a food label will tell you. Maybe as much as double.
The U.S. government sets the recommended dietary allowance (RDA) for protein, as well as for vitamins, minerals, fiber, fats, and carbohydrates. The RDA starts at a low of around 0.8 grams per kilogram of body weight for sedentary adults 18 and over, or about 0.36 grams per pound of body weight. (The RDA for children is higher, at 1.5 grams of protein per kilogram of body weight.)
This translates into 60 grams per day for a 150-pound person. But that doesn't mean that's the target you should be aiming for. For most active people and athletes, these guidelines are considered by most experts to be too low.
Of course, getting all of those grams in a single meal would likely leave you with a stomach ache. For this reason (and another one we’ll get into later), we recommend spreading your protein intake out across several meals containing at least 20 grams, and as much as 40 grams. Once you calculate your ideal daily intake, you can work backward to plan out your meals.
Do You Need More Or Less Protein As You Age?
The simple answer? You probably need more protein than you think. In his article "How to Eat for Maximum Muscle at Any Age," researcher and world-class powerlifter Layne Norton, recommends aiming for these daily standards over the course of your life:
|Under 18 years
|0.6-0.8 grams per pound of body weight
|0.8-1.1 grams per pound of body weight
|1.1-1.3 grams per pound of body weight
|Over 65 years
|1.3-1.5 grams per pound of body weight
As we age, our bodies become less efficient at using dietary protein. Over time, this deficiency, or "anabolic resistance" as it is also known, can lead to decreased strength and loss of both lean mass and mobility.
But staying physically active and eating adequate protein foods can help you stay in shape well into your golden years.
A common problem among elderly people is sarcopenia, or loss of muscle tissue. Adequate protein intake can help reverse this natural process. A study published in the Journal of the American Medical Directors Association recommends that people over 65 years of age consume a minimum of 1-1.2 grams per kilogram of body weight per day to maintain and regain lean body mass. The same study recommends that older people continue to regularly perform endurance and resistance-type exercises, and notes that most older people with acute or chronic diseases need even more of the macronutrient each day.
Now that you know that you need protein, you also need to know that not all protein is the same. There’s a difference between complete and incomplete protein.
"Even if you don't measure it out to the gram, the lesson here is that as you age, you need more protein," — Layne Norton, Ph.D.
According to protein researcher Don Layman, Ph.D., it is recommended to aim for a protein intake of 1.2 – 1.8 g/kg. Additionally, as one ages, it is important for protein to make up a greater proportion of their overall calorie intake. (Refer to the section at 43:03 in the video linked below titled "Is the Protein RDA Sufficient").
What Is A Complete Protein?
A complete protein is one that contains all nine essential amino acids (EAA) that our bodies need: histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine. The keyword here being “essential” - meaning the amino acids we must get through dietary sources because the body doesn’t make them on its own.
Dietary protein is easily found in animal sources, such as fish, poultry, meat, dairy products and eggs. But, protein isn’t exclusive to just animals. In fact, many plants contain protein as well, the primary difference being that many are considered to be incomplete.
An incomplete protein is one that does not contain all nine essential amino acids. Beans, specific nuts, and tofu are a couple examples of incomplete protein sources, so eating those foods alone for protein will not give you all of the amino acids your body needs.
Though there are some complete sources of vegan protein, such as quinoa, soy, and lupini, it’s more common to mix different proteins together to ensure you’re getting all the essential aminos you need on a plant-based diet.
Trying to meet a high protein target as a vegan without protein powders can be challenging. Not because protein in plants doesn’t exist but because you’ll need to eat a much higher volume of food to get the protein you need, turning meal prep and eating into a full time job.
That’s where plant-based protein powders, meal replacement shakes, and nutritional supplements can come in handy. They make it easier to hit your protein targets and save you time while sticking to your dietary guidelines. And when formulated correctly, they provide a complete protein source with all the amino acids you’ll need.
What Are Amino Acids?
Amino acids are the building blocks of protein, and proteins are simply long chains of amino acids. Your body has thousands of different proteins that each have an important role to play in keeping you healthy and fit. And every protein has its own sequence of amino acids. The sequence in which the amino acids are “glued” together is what gives protein different shapes and have different functions in your body.
You can think of amino acids like the letters of the alphabet. When you combine letters in various ways, you make different words. The same goes for amino acids — when you combine them in various ways, you make different proteins.
In other words, amino acids are much, much more than just the tiny building blocks of your muscles. They are literally the fuel for nearly every process in your body.
- Sexual function
- Hormone production
- Blood sugar
- Immune system
- Immune system regulation
- Nitrogen balance
- ATP (energy) production
- Muscle protein synthesis
- And more…
So, if you want optimal health, cognitive functioning, and human performance, focusing on proper ratios and adequate intake of amino acids might get you further than any biohack, cutting-edge peptide, or fancy piece of gear you can ever buy.
Essential Amino Acids (EAAs)
EAAs are a smaller subcategory of the 20 amino acids. They’re classified as “essential” because your body can’t make them on its own, and you have to get them from diet or supplementation.
In fact, EAAs and essential fatty acids (omega-3) are the only macronutrient humans must eat to survive. So long story short, just like water, you would simply die without enough of them.
There are nine EAAs in total, each with critical roles in the body:
|Critical for protein synthesis, muscular growth, and repair.
|Supports muscular metabolism, immune function, and energy regulation.
|Stimulates muscle growth, regeneration, and energy production.
|Precursor to several important neurotransmitters that promote cognitive function and a balanced mood.
|Forms structural proteins (collagen and elastin) for healthy skin and connective tissue.
|Precursor to serotonin, a neurotransmitter that regulates mood, sleep, and appetite.
|Important for immune function and the absorption of nutrients.
|Plays a role in metabolism, detoxification, and the absorption of zinc and selenium.
|Precursor to histamine, and neurotransmitter vital for the immune system, digestion, sexual function, and sleep.
As you can guess, lacking in any one of the EAAs is a fast-track to a multitude of health issues—hence why these amino acids are considered to be “essential” in the first place. Of these nine EAAs, only three are classified as branched-chain amino acids (BCAAs), which are denoted in parentheses above.
How Much Of Each Do I Need?
You don’t need to eat foods with amino acids at every mea and you certainly don’t need to be guzzling down BCAA supplements all day long like the bodybuilders you see at the gym.
What’s important is to get a balance of amino acids throughout your day by consuming a high protein meal or drinking a protein shake. The recommended daily allowance for every 2.2 pounds of body weight for each of the essential amino acids are:
Now that we know which amino acids you need in your diet, let’s look at what your body does to protein and how that affects when you eat your protein.
Protein Turnover & The Leucine Threshold
This refers to the continual renewal or replacement of protein in the body. It is defined by the balance between protein synthesis and protein degradation. When an organism or a cell (for example muscle cells) is growing, the rate of protein synthesis exceeds that of protein degradation (anabolism), while the opposite is true during periods of catabolism. As mentioned above, there is a constant flux between the two. There is never a standstill.
What does that mean for us? In times where protein availability in the body is low and protein breakdown is high (let’s say you had a hard training session) there is no or little muscle protein synthesis build up. This is because the available amino acid pool is low so your organs like the liver and heart get preferential pull off of the available amino acids. Why? Because they are obviously more essential for your survival, which is always your body’s number one task.
But, protein synthesis is never simply on or off. During times where there is not much food in the system, the rates of protein turnover in various tissues changes.
Does this mean performing your workouts fasted, using longer periods of intermittent fasting or only eating one high protein meal per day has a detrimental impact on your performance or for hypertrophy? No, there is a good amount of research that shows total protein over the course of the day is most important.
BUT, could your workouts, muscle growth and performance be optimized if you went into them with more amino acids in your blood? Likely. It’s logical to consider that organs get priority during fasting and the muscles (which account for 50% of protein needs in the body) will pull a lot more from that amino acid pool after being fed.
Eating a meal causes an uptick in protein synthesis and down regulation in protein breakdown. Fasting between meals and at night causes an uptick in protein breakdown and decrease in protein synthesis. But once again, the TOTAL protein eaten every day is what determines if you push the entire system in muscle gain or muscle loss territory. So far so good, you likely already knew this, but I wanted to lay the groundwork.
But let us make our point more specifically…
Why Protein Is Important In Every Meal
While much of your body tissue (so weight loss or gain) is highly sensitive to total calories in terms of repair, muscle tissue is impacted on a greater scale by total protein.
This is controlled in large part by the enzyme called mTor. Mammalian target of rapamycin (mTOR) is an evolutionarily conserved serine/threonine kinase, and is known to play vital roles in protein synthesis. Here is a quick breakdown of what it does: mTor is essentially the master switch of protein synthesis at the initiation phase. Think of turning the key in your car to start the engine. You can have a full tank of gas, fresh oil, great tires and a big engine but none of that will run unless you have something to turn it all on. That is how you can think of mTor: the “on” switch for muscle building.
mTor is sensitive to a few other things:
- Strength training and exercise
- Total Calories
It should come as no surprise that you won’t build much muscle if you don’t exercise, eat very little total food and eat very little protein. Most people can wrap their heads around that. But, what is it specifically about leucine that is so important for building muscle?
The Leucine Threshold
Leucine is one of the nine essential amino acids (the compounds protein is broken down to).
When you eat protein that contains leucine, leucine enters the bloodstream and goes straight to the muscle; this is how your muscles sense the ingestion of a meal and whether or not they can begin protein synthesis to create more tissue (build muscle).
The hypothesis is that to maximize this response about 2.5g of leucine is required, otherwise known as the LEUCINE THRESHOLD.
In more detail, a meal containing 0.04 g of leucine per kilogram of bodyweight (g/kg BW) or about 0.18 g per pound, from a high-quality protein source will allow you to hit the leucine threshold. For most people this is somewhere between 2–4g leucine per meal.
How to determine your leucine threshold requirement
Let’s take an average cut of beef, which has a bit over 8% leucine of total protein. So in a 5oz steak with 40g protein, the leucine content for that meal is about 3.2g. It meets the leucine threshold but not to the whopping extent most people would assume.
This also sheds some light on why eating enough protein in a meal is important. For example, if you cut that portion down to 3 oz, you would only be getting about 1.92g leucine which does not quite meet the threshold for protein synthesis.
How Much Protein Should I Eat Per Meal?
Without getting into too many details about the quality of protein and amount of protein absorbed (more on that later) it's important to set a general target for protein consumption to ensure that the leucine threshold is met so the body stays in an anabolic state via muscle protein synthesis as often as possible, especially if your goal is to build and maintain lean muscle.
Research conducted by Brad Schoenfeld and Alan Aragon in 2018, published in the Journal of the International Society of Sports Nutrition, discovered that the maximum amount of protein that most individuals can absorb per meal is around 0.55 g/kg, equating to 35-45 grams for the average person.
Protein scientist Don Layman also provides further insight on this topic on Peter Attia, M.D.'s podcast. He uses 30 grams of protein as the baseline for how much protein you should try to get per meal. Fast forward to the 1:20:02 to get his research-based insights about protein timing, pre-workout vs. post-workout meals, optimal time between feeding windows for recovery and more.
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Protein Quality, Digestion, and Absorption
Digestion of food begins in the mouth and continues until all nutrients have been absorbed in the intestines. Several digestive enzymes are involved in the digestion process which break down – or hydrolyze – protein into short-chain oligopeptides or amino acids. The simplest units of proteins are amino acids of which there are 20-odd different types. Two amino acids linked together are called dipeptides, a few amino acids in a peptide chain are called oligopeptides and long chains of them are called polypeptides.
Amino acids are absorbed in their basic form by an active transport process, where they are pumped across the cell membranes and then into the blood. However, there is a second process which happens simultaneously to the active transport mechanism where oligopeptides can be taken up in their current form and when inside the cells of the intestine, are then further broken down to free amino acids. The process of this is a cell enzyme-related system that relies on a chemical ion gradient.
As there are two independent protein absorption systems in operation, this allows for more protein absorption at times when it’s required as the second system only comes into play when there are oligopeptides present. In a high-protein meal with more than one protein source (i.e. the majority of meals), both systems come into play at similar rates.
Protein Digestibility-Corrected Amino Acid Score (PDCAAS)
PDCAAS takes into account the profile of individual amino acids (IAA) of the protein in question, as well as its digestibility in humans; it is the amino acid score with an added digestibility component. Scores are from 0.1 to 1.0, with 1.0 being a high-quality protein. PDCAAS is the current accepted measure of protein quality, and is the method adopted by the World Health Organization / Food and Agriculture Organization (WHO/FAO) and the US Food and Drug Administration (FDA), because it’s both simple to test and has a direct relationship to human protein requirements.
Although more up to date and accurate, PDCAAS isn’t without its shortcomings. All proteins of a score greater than 1.0 are rounded down to 1.0 as scores above are considered to indicate that the protein contains IAAs in excess of human requirements. This obviously limits the validity of comparisons between proteins.
Another flaw of PDCAAS is that the scores are based on that of a 2 to 5-year-old child (considered to be nutritionally the most demanding group). Adults have a proportionally larger maintenance : growth ratio and this is not considered when using PDCAAS. As PDCAAS doesn’t account for certain factors influencing the digestion of the protein, the PDCAAS of a single protein source is of limited use for application to human protein requirements. This is because what is measured is the maximal potential of quality and therefore it’s not a true estimate of the quality at requirement level.
PDCAAS is also limited by the fact that it doesn’t account for conditionally essential amino acids, and these contribute to the nutritional value of a protein. For example, a good intake of non-essential cysteine – a sulfur-containing amino acid – reduces the requirement for the essential sulfur-containing methionine, and tyrosine reduces the need for the EAA phenylalanine. Arginine is also considered conditionally essential as in certain population sub-groups and at times of high demand, an insufficient amount may be synthesized within the body.
Another crucial limitation of PDCAAS is the fact that human diets generally consist of varied protein sources, even in a single meal. This means the total amino acid profile of a meal is improved and there are other food constituents that may affect protein hydrolysis, digestion, and absorption. In order to assess the true PDCAAS of a meal, all individual amino acids need to be taken into account. Fortunately, PDCAAS can be adapted to account for this in order to evaluate the protein quality of a meal more reliably.
The protein from rice has a PDCAAS of 0.4-0.5, limited only by the fact that it’s significantly low in the EAA lysine. However, it’s abundant in methionine and cysteine; the high content of these two key amino acids is a point that PDCAAS doesn’t account for when looking at a single food. The PDCAAS of pulses ranges from 0.4-0.8, depending on the pulse, and pulse proteins are low in methionine and cysteine but abundant in lysine. So, when beans and rice are consumed together in a meal, their combined constituent PDCAAS is 1.0: an ideal protein source.
This gives a whole new meaning to the saying “They go together like beans & rice.”
Despite its limitations, PDCAAS is currently the most widely adopted protein scoring system as it provides a valid method of assessing protein quality as long as the cumulative score of the different protein sources in a meal is accounted for. Indeed, in US labeling regulations, the protein quality of a food using PDCAAS needs to be considered when labeling the total protein content of a food.
Digestible Indispensable Amino Acid Score (DIAAS)
DIAAS is much like PDCAAS in that it determines the digestibility of the amino acids as well as the protein’s contribution to human amino acid and nitrogen requirements. However, DIASS is shown as a percentage and doesn’t limit to scoring the protein to a maximum value; instead, proteins can have a higher score. It has been suggested that DIAAS should be the adopted scoring method for the US FAO, but as yet hasn’t been adopted as the preferred protein scoring method.
An advantage of DIASS over PDCAAS is that proteins with greater amounts of IAAs have a higher score that may be more reflective of the amino acid profile with relevance for those with higher protein requirements. However, while this may have relevance to single foods, the combination of protein sources in a meal still needs to be considered.
So why do PDCAAS and DIAAS matter to us?
Someone who is trying to optimize and maximize their protein consumption need to look at the amount of protein they're eating (0.8-1.1 gram per pound of body weight), whether their getting all the 9 essential amino acids or not and have to look at the protein quality as well.
And this sounds like a lot work for someone who already has a lot on their plate: family, health, career.
Which is why we've taken all the legwork for you. We taken all of this into consideration when creating the Essentails Shake to make sure that you get just right protein quantity, quality, and all the essential amino acids.
Is Plant Based Protein Inferior To Animal Based Protein?
Let’s start our journey into plant based protein by looking at the typical amino acid composition of whey protein:
*Sulfur Amino Acids (SAA)
As you can see, whey protein is extremely high in Leucine – one of the most important essential amino acids. Leucine is also in fact one of the branch-chain amino acids (more on the difference between EAAs and BCAAs here).
Because whey, and most of the dairy proteins contain all 9 EAAs, they are used commonly by athletes to rebuild muscle, and by anyone looking to add quality protein in their diet.
Let’s look at a few amino profiles of the most common types of vegan proteins, and then we’ll go over the most popular vegan protein pairing strategies.
Looking at the table of amino acids in pea protein, a few key differences from the whey profile are immediately noticeable.
The most glaring difference between dairy and pea protein, from an amino acid standpoint, is in the SAA, or ‘sulfur amino acids’.
Whey contains almost 5x more cysteine, and 4x more methionine.
While methionine is both an SAA and an EAA, cysteine is not considered an EAA, because our body can make it on it’s own. However, both cysteine and methionine are considered critically important to our overall health, as they play important roles in our immune, cardiovascular, and endocrine systems.
In addition to the SAA-content of pea protein being much lower than in whey protein, the BCAA content is also about 30% lower – making it a less attractive choice for athletes.Or is it?A study in 2015 conducted in Dijon, France (yes, like the mustard), actually found that a certain brand of pea protein that was ‘particularly high in branch chain amino acids’ increased the biceps size of participants as much as whey protein.
So, is pea protein as effective as whey protein at building muscle? More research is likely needed, as it is unclear whether the pea protein used in the study was specialized or represented a common pea protein you would find in the store.
While pea may still be behind whey when it comes to amino completeness, it is considered the best vegan protein source, and is the basis for almost all modern day complementation strategies.
But before we talk strategy, let’s look at a few other vegan protein sources, and their amino profiles.
Brown Rice Protein
Brown rice is one of the most common vegan proteins and it does contain more of the SAAs than pea protein, but it is still used less frequently than pea for three reasons:
First, it is incredibly low in the amino acid Lysine – with only 1/3 the amount found in pea, and 1/5 the amount found in whey. Lysine is an important precursor to carnitine, which helps us metabolize fat effectively. Lysine is therefore a critical nutrient to any weight loss program- making brown rice, on its own, a poor choice for those looking to slim down.
Second, brown rice has a slightly lower in BCAAs (branch-chain amino acids) than pea protein. With less leucine, isoleucine, and valine per gram than other popular vegan protein sources, brown rice falls short when it comes to helping build and maintain lean muscle.
Lastly, brown rice is not a gel-forming protein, and it has a distinct ‘chalky’ taste when drinking. While these reasons are less important than the two relating to its nutritional value, it is a big part of why brown rice is used less and less these days.
Quinoa is a well-known superfood, and is considered one of the best vegan protein sources.
Quinoa protein is high in branch chain aminos, and is the best source of naturally-occurring lysine of any plant-based protein source!
Along with magnesium, riboflavin, and other micronutrients, quinoa makes for an excellent addition to any vegan protein blend.
Here's how to combine them
The most popular way to combine vegan proteins is by blending pea protein with brown rice.
PROS: The brown rice has complementary SAAs that the pea is missing, while the pea has plenty of lysine to cover for the brown rice. Brown rice is also a highly cost-effective protein, which means most pea + rice mixes are relatively affordable.
CONS: Brown rice often yields a ‘chalky’ taste and texture, and you don’t get as broad a range of micronutrients. This challenge, however, can easily be overcome by first sprouting the grains to make them more bioavailable and cleaner tasting.
And this exactly what we've done in our Essentials Shake.
|Good for Gut Health
LyfeFuel uses a combination of yellow pea protein and sprouted brown rice protein to make a highly digestible complete protein. We source our Non-GMO pea and rice blend from Canada — which means it's traceable, sustainable, and tested for heavy metals.
Now you basically know everything there is to protein.
So here are some actionable for you:
1. Eat enough protein (0.8-1.1 gram per pound of body weight)
2. Eat more protein as you get older
3. You need to get all 9 essential amino acids from your diet
4. You should look at protein quality as well
5. If you're vegetarian or vegan, then you should combine complementary protein sources to get everything you need.
Fortunately, the plant-based supplements industry has come a long way so you easily get your protein intake on a plant based diet.
If you’re serious about a healthier and more sustainable future and interested in optimizing your protein intake, check out LyfeFuel’s line of great-tasting protein + superfood powders.
Ongoing education, challenging old beliefs, and continuing to ask questions about the food and products we consume helps us make more informed decisions.
Sometimes the smallest and simplest choices we make can have the greatest impact.
- Howatson G et al., “Exercise-induced muscle damage is reduced in exercise-trained males by branched-chain amino acids: a randomized, double-blind, placebo controlled study,” Journal of the Internal Society of Sports Nutrition, vol. 9, no. 1 (May 8, 2012): 20 [Epub ahead of print].
- Is dietary carbohydrate essential for human nutrition? The American Journal of Clinical Nutrition, Volume 75, Issue 5, May 2002, Pages 951–953, https://doi.org/10.1093/ajcn/75.5.951a
- Witard OC, Wardle SL, Macnaughton LS, Hodgson AB, Tipton KD. Protein Considerations for Optimising Skeletal Muscle Mass in Healthy Young and Older Adults. Nutrients. 2016;8(4):181. Published 2016 Mar 23. doi:10.3390/nu8040181
Disclaimer: The LYFE Fuel blog is for informational purposes only. The information does not serve as a replacement for professional medical advice or treatment. We kindly ask you not to ignore professional medical advice because of any information you’ve read on https://lyfefuel.com/. If you have any concerns about your health, please consult a physician or appropriate health care expert.