The Ideal Form of Protein
by Luke R. Bucci, PhD, CCN C(ASCP) CNS.
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It has been said that during the last decade science has revealed more sports
nutrition breakthroughs than in the previous 100 years. For athletes in the
know, this is their secret weapon, the place where brains and brawn come
together to go beyond genetic potential. This article will focus on the state of
the art for protein, the most revered macronutrient for athletic recovery and
growth.
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What Forms of Protein Intake are Available?
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Today, we have four ways to get protein or amino acids into the bloodstream.
Lets review the list before we go on.
Whole Food Proteins: The oldest method for getting your daily dose of protein
comes from Mother Nature. The protein sources in this group are supplied from
intact or whole foods such as meat, fish, poultry, dairy products or vegetables.
Not so long ago this was the only way to get protein into our diets until the
advent of protein supplements, which are now readily available.
Protein Supplements: These supplements contain purified forms of native proteins
such as Whey, Egg or Soy, with the degree of purification being quite different
from product to product. The varying degrees of purification go from protein
concentrates (lower grade) to isolates, which are much higher in quality. In any
case most protein supplements are usually low in fat and add only moderate
amounts of carbohydrate, a welcome feature for athletes who want to stay lean.
Free Form Amino Acids: Due to their unique properties, the use of pharmaceutical
grade (pure and sterile) free form amino acids to support muscle repair and
growth would work best by being injected into the bloodstream. Feeding people
this way is called parenteral feeding, or total parenteral nutrition (TPN). TPN
was a great medical advance because it feeds people who otherwise could not eat.
Most of the scientific research done on free amino acids has revealed that they
work best taken on an empty stomach. When free amino acids are taken without
interference from other proteins they can be utilized to elicit specific
responses.
Protein Hydrolysates: Protein can be hydrolyzed (broken into smaller pieces) by
enzymes, producing small chains of amino acids called peptides. This process
mimics our own digestive actions thus making it an ideal way to process protein.
Keep in mind that protein quality must always be considered, regardless of which
form is ingested. Also, one can mix all of the forms together in unlimited ways.
Table One gives some pros and cons for each form of getting amino acids into the
bloodstream.
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Step One: How is Protein Absorbed, Really?
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Scientists and doctors realized in the late 60s and early 70s that protein is
not completely broken down to single (free) amino acids inside the small
intestine (gut), and then the single amino acids absorbed by the gut and simply
transferred to the bloodstream. Rather, proteins are chopped into small pieces
in the stomach and gut by acid and enzymes. When the pieces get between four and
six amino acids long (small Oligopeptides), enzymes on the surface of gut cells
quickly chop them up into even smaller peptides (either two or three amino acids
long) and single amino acids. These little pieces (one, two or three amino acids
long) are taken inside gut cells. Anything larger simply does not get into gut
cells in significant amounts. The pieces that are two amino acids long (dipeptides)
and three amino acids long (tripeptides) are then chopped into single amino
acids inside the gut cells by hordes of enzymes. Chopping di- and tripeptides
into single amino acids is practically instantaneous after being taken up into
gut cells. The single amino acids are then rapidly dumped into the bloodstream.
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The Magic of Small Peptides
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Why would our gut want to absorb di- and tripeptides instead of single amino
acids? The answer is easy - economy of effort. To absorb anything from inside
the intestine to the inside of gut cells, membranes must be crossed. This means
receptors must be used to take in substances into gut cells. Gut cells are
loaded with receptors that grab nutrients very selectively. No receptor, no
absorption. Gut cells have receptors for single amino acids, but they have even
more receptors for dipeptides and tripeptides.
Receptors are like subway turnstiles - only one molecule at a time can pass
through. Because di-and tripeptides are small enough to pass through receptors
as fast as single amino acids, our bodies have figured out that by absorbing a
tripeptide, it can get three amino acids for the cost of one. It is then very
easy to have lots of peptidase enzymes inside the gut cells that rapidly chop
the tripeptide into single amino acids, which are pushed out of intestinal cells
into the bloodstream as single amino acids. Cells throughout the body
(especially muscle cells) can then pick and choose what single amino acids they
want.
This means that instead of having a bunch of single amino acids queuing up to go
through a limited number of intestinal turnstiles, di- and tripeptides push
through two or three people at a time. The net result is 2-3 times more people
(amino acids) on the subway (bloodstream) in the same time period as if people
went through the turnstiles one at a time. Efficiency is the key.
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Evidence For Taster Absorption of Amino Acids
From Peptides - Peptides Versus Intact Proteins
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Is there any evidence that hydrolysates (peptides) are better than food proteins
or intact proteins for getting amino acids into the bloodstream? Yes, so much so
that it is now considered dogma. Hospitals routinely use hydrolysate products
from pharmaceutical companies as the primary amino acid source for feeding
patients in hospitals. A large and consistent body of literature has shown that
at higher levels of total amino acid intake (obviously bodybuilders are at the
high end) hydrolysates are absorbed faster than either intact proteins or free
form amino acids. Usually hydrolysates get into the bloodstream about twice as
fast as intact proteins or free form amino acid mixtures in normal humans. This
coincides perfectly with the subway turnstile analogy.
Let's skip the animal and hospitalized human studies, and look at research that
more closely applies to bodybuilders. Ten years ago, Grimble and coworkers from
the Department of Gastroenterology and nutrition in Central Middlesex Hospital
in London, United Kingdom, looked at absorption of amino acids from intact egg
protein and different degrees of hydrolysis in 12 normal humans. Best uptake
came from the hydrolysates richest in di-and tripeptides. These results clearly
show that a small peptide hydrolysate is preferred to a partial hydrolysate or
intact protein for getting amino acids into the bloodstream faster in humans.
A recent study by Collin-Vidal from the Human Nutrition Laboratory of the
University of Clermont at Auvergne in France fed 12 normal volunteers either
carbohydrates / lipids alone or with whole casein or casein peptides
continuously by a nasogastric tube. Leucine metabolism was measured as a marker
of protein metabolism by a leucine tracer. Similar to bodybuilders, these
subjects were in positive leucine balance and were already eating a high intake
of leucine. Subjects showed higher leucine levels in the bloodstream, more
protein synthesis and more leucine oxidation with the hydrolysate, indicating
more leucine got into muscles and other tissues. Since the subjects were not
exercising, extra leucine was broken down (oxidized for energy) instead of being
used to build muscle. The moral of the story is that if these subjects were
exercising, then more of the leucine would have been targeted to building muscle
and not broken down. The net result is that more leucine got to tissues
(including muscles) with the hydrolysate.
An overwhelming amount of literature has reported the superiority of
hydrolysates over equivalent compositions of free form amino acids for getting
amino acids into the bloodstream faster. As an example, a report by Silk from
Middlesex Hospital in London using normal humans will be examined. First,
absorption of amino acids was greater from hydrolysates of casein or lactalbumin
(whey) than from equivalent free form amino acid mixtures. In fact 11 out of 16
amino acids measured where absorbed significantly better, including leucine,
valine and glutamine. In fact, glutamine absorption was doubled by hydrolysates.
Also of importance is the quantitative or total amount of amino acids getting
into the bloodstream. figure 2 shows how a fish protein hydrolysate got more
amino acids into the bloodstream faster than an equivalent free form amino acid
mixture again, the importance of this fact will be seen later in this article.
Another important point is that hydrolysates can get more amino acids into the
bloodstream faster into normal, healthy volunteers than an equivalent free form
amino acid mixture when intakes are high. what does this mean in real life?
According to a study by Hegarty from st. bartholomew's hospital in london,
england, whey protein hydrolysate (lactalbumin) and an identical composition of
free form amino acids were equivalent in uptake until 12 grams of total amino
acids were given. Over 12 grams of intake, uptake of every amino acid from the
hydrolysate was equal to or superior to the free form amino acid mixture. again,
a doubling of glutamine uptake was found. this is very important for
bodybuilders, because 12 grams is a measly amount of amino acids compared to
typical intakes of 50 grams of amino acids per meal. Thus, at high intakes of
protein, hydrolysates get absorbed better than intact proteins or free form
amino acid mixtures.
It is easy to relate these results to real life. Free form amino acid receptors
on gut cells can keep up with peptide receptors until a certain level of total
amino acids are reached (about 12 grams per feeding), then the subway turnstile
effect comes into play for hydrolysates, showing their superiority for amino
acid absorption at real-life levels of supplementation.
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Why is Faster Amino Acid Absorption Better tor Bodybuilders?
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Why all the fuss about getting more amino acids into the bloodstream faster? The
answer is simple - more amino acids in the bloodstream (especially with insulin)
means more amino acids in muscle means more muscle protein synthesis means more
growth/recovery/repair.
We already know that protein needs of weightlifters are double those of other
athletes and sedentary people. We also know that after lifting weights, amino
acid transport, protein synthesis and protein breakdown (catabolism) are all
increased in muscles. We also know that amino acids, not carbohydrates, fat or
insulin, are responsible for increased anabolism (more protein synthesis and
less protein breakdown) in humans after eating. In other words, muscles are
hungry for amino acids, which they can only get from the bloodstream, right
after a workout (within 30 minutes).This happens to be the window where
hydrolysates are superior to proteins or free form amino acid mixtures.
Before we get too focused on protein, keep in mind that right after a weight
training workout, a combination of protein and carbohydrate outperformed both
protein alone and carbohydrate alone for increasing insulin and growth hormone
levels. Thus, even an ideal hydrolysate would have better effects when consumed
with simple carbohydrates since carbohydrates are absorbed by different
receptors on gut cells, there is little or no competition with amino acids and
peptides for absorption.
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Why Rapid Glutamine Uptake by Hydroysates is so Important?
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Muscle cell content of glutamine is now thought to be the major influence on
muscle protein synthesis. In other words, more muscle glutamine, more muscle
protein synthesis, more muscle. research clearly shows that glutamine levels in
the bloodstream are dramatically raised by feeding small peptide hydrolysates
compared to amino acid mixtures and intact proteins. Supplying glutamine may
indirectly prevent the immune system, gut and brain (other major users of
glutamine) from signaling muscles to break down protein to feed them. Net result
is more glutamine for muscles.
Fortunately, a glutamine peptide has been developed commercially that is 30%
glutamine in the form of small peptides, which we now know are better absorbed
than an equal amount of free glutamine. Derived from wheat gluten, glutamine
peptide is hydrolyzed suffidently to virtually remove any possible antigenicity,
a typical advantage of hydrolysates over intact proteins. thus, getting
glutamine to muscles has never been easier.
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What an Ideal protein (amino acid) Supplement should look like?
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Why not cut to the chase and sell a mixture of 20% free form amino acids, 80 %
di- and tripeptides, just like our gut absorbs? This type of hydrolysate is
recently available in commercial amounts, and is being used in medical
situations, mostly via nasogastric tube feedings. wouldn't this be an ideal
supplement? No, for several real-life reasons. one is cost. a serving (25 grams
of amino acids) would have a raw material cost (before packaging, shipping and
profit) of $3-5. Second, it would taste really terrible, a fact which is no
probjem if you have a nasogastric tube, but a big, real-life problem if you have
to eat the stuff every day. Flavoring is essential for compliance. Third, you
actually want some carbohydrate, as discussed earlier (this also helps the
taste). Fourth, small peptides (up to six amino acids long) are just are
effective as di- and tripeptides because of gut cell membrane (brush border)
oligopeptidases. Fifth, intact proteins help flavot stability and mixability
(when instantized or agglomerated), and still have potent anabolic effects on
protein synthesis.
A product profile of an ideal source of amino acids for feeding muscles after
workouts should look like this:
Over 50% of total amino acids from small peptides (hydrolysates)
Rich-quality protein and hydrolysate sources (whey, casein, egg, soy all
qualify)
glutamine rich (preferably from glutamine peptide)
Some high glycemic carbohydrate (maltodextrin, glucose)
Creatine and other single amino acids are optional
Good ispersability with a spoon or shaking for easy mixing and portability
Low viscosity and good flavoring for long-term use and compliance
Advantages of such a product are more than supplying the most important amino
acids most efficiently to hungry muscles. hidden advantages include being able
to ingest the supplement immediately after a grueling workout without getting
bloated, and not suppressing appetite so you can eat a full meal sooner after
ingesting the ideal protein supplement.
There is no question that protein (amino acids) is the single most important
nutrient for muscular hypertrophy it is clear that efficient delivery of amino
acids to muscles as soon as possible after workouts improves the anabolic
hormonal milieu, muscle protein synthesis, and reduces muscle catabolism. all
these effects are part of the normal response to resistance training.
In the quest for the ultimate protein, consumers have been bombarded with
choices, hype and hearsay. why not give the body what it has already told us it
needs, as verified by scientific studies in normal humans and weightlifters?
This means a supplement rich in small peptides (over 50%) from high-quality
protein sources, with emphasis on glutamine peptides, combined with some
carbohydrate and made practical by easy mixability and good flavor. such a
product now exists,