Whey
protein, often
referred to as lactalbumin, is currently the supplemental protein
source of choice for many bodybuilders and strength athletes. Whey
proteins represent the major proteins in human breast milk, as
opposed to bovine milk which is comprised primarily of casein with
lesser amounts of whey. Whey is comprised of alpha-lactoglobulin,
beta-lactoglobulin, bovine serum albumin (BSA), and immunoglobulins
(IgG1, IgG2, Secretory IgA, and IgM). Other components of the
lactalbumin fraction include: enzymes, iron binding proteins, calcium,
potassium, sodium, phosphorous, and vitamins A, C, B1, B2, B3, B5, B12,
folic acid, and biotin.
Whey is a balanced source of essential amino
acids and peptides with a high protein efficiency ratio. It is
considered to be an excellent source of sulfur amino acids (methionine
and cysteine), as well as the branched chain amino acids (leucine,
isoleucine and valine), and glutamine. (See sections on branched chain
amino acids and glutamine for information on their potential benefits).
Whey
transits the stomach quickly and is rapidly absorbed from the human
intestine. The beta-lactoglobulin component remains soluble in the
stomach and empties rapidly as an intact protein needing further
hydrolysis by pancreatic enzymes. Casein, on the other hand, transits
the stomach slowly.
Skeletal
muscle is the largest repository of metabolically active protein and a
major contributor to total body nitrogen balance. Supplying energy
alone (i.e., carbohydrate and lipids) cannot prevent negative nitrogen
balance (net protein catabolism) in animals or humans; only provision
of protein or amino acids allows the attainment of nitrogen balance.
While
no studies exist comparing the impact on nitrogen balance, body
composition, or performance of different protein sources in trained
athletes, whey has been shown to promote growth and enhance nitrogen
balance in experimental animals, low birth-weight infants, and burn
victims.
Whey
protein
is rich in substrates for glutathione synthesis, containing
substantially more cysteine, which is considered to be a rate-limiting
step in glutathione synthesis, than does casein. Whey also contains
high amounts of glutamine and glycine.
Glutathione
is a powerful antioxidant and is involved in metabolic detoxification
pathways. The role free radicals play in the development of
exercise-induced tissue damage, or the protective role antioxidants
might play, remains to be completely elucidated.
Research has indicated
free radical production and subsequent lipid peroxidation are normal
sequelae to the rise in oxygen consumption with exercise.However,
physical training has been shown to result in an augmented antioxidant
system and a reduction in lipid peroxidation. Supplementation with
antioxidants appears to further reduce lipid peroxidation but has not
been shown to enhance
exercise
performance.
Glutathione
levels have been shown to decrease with exercise. Additionally,
running a marathon causes a large increase in the tissue content of
oxidized glutathione (189%) at the expense of reduced glutathione
(-18%).While no information is available on the effects of
resistance exercise and glutathione levels, it is hypothesized an
increased intake of antioxidants might protect the active person
against minor muscle injuries.
Whey
protein is more efficient at inducing supernormal glutathione levels
than a cysteine-enriched casein diet. A whey-rich diet has been shown
to increase heart and liver tissue glutathione content in rats. The whey protein diet
appeared to also increase longevity when fed at the onset of
senescence.Whey-based formula enhances cysteine retention and
results in greater taurine excretion, thought to be a reflection of
greater taurine stores.Whey protein fed to three HIV-sero-positive
individuals over a period of three months, at doses increasing
progressively from 8.4 to 39.2 g per day, resulted in progressive
weight gain and increased glutathione levels in all three cases.
Experimental
studies suggest the whey protein component of milk might exert an
inhibitory effect on the development of several types of tumors. It is
thought the rich supply of substrates for glutathione synthesis
contributes to this inhibitory effect.In experimental animals, a
diet consisting of 20 g of whey/100 g diet has been shown to be more
protective than similar diets utilizing casein, soybean, or red meat
against dimethylhydrazine-induced intestinal cancers.Peptides from
whey protein have also been shown to have antithrombotic and
immunoenhancing activities.
The
primary concerns about supplementing whey protein are the possibility
of food allergies, its lactose content, and proposed links to
insulin-dependent diabetes mellitus (IDDM). While the possibility of
food allergies from whey has to be considered, it is probable it is no
more and possibly less antigenic than soy, casein, or egg-based protein
supplements.
A significant concern might be the method of processing of
the whey protein, since high temperatures during heating or drying can
generate browning reaction products by covalent interaction of proteins
and lactose. Browned proteins have lowered digestibility and are
thought to result in more uptake of intact protein through intestinal
mucosa. All whey protein available contains some degree of lactose,
although many have very low amounts.
The
BSA component of whey has been implicated as a possible trigger for
IDDM in children. A similarity exists between the amino acid sequence
of the beta cell protein, found on the insulin-secreting beta cells of
the pancreas, and BSA. Because elevated levels of anti-BSA antibodies
have been found in sera from children developing IDDM, it has been
proposed that absorption of BSA, or partially digested fragments of
BSA, stimulate the immune system which then incorrectly destroys beta
cells.Pardini found the prevalence of anti-BSA antibodies was
52% in children with less than one year of IDDM, 47% in children with
greater than one year of IDDM, and 28% in the control group.
They concluded the prevalence of anti-BSA antibodies is higher in IDDM
subjects than in controled subjects; however, because of the large
overlap of antibody titers observed in patients and controled subjects,
anti-BSA antibodies were not sensitive nor specific markers of IDDM.
Ivarsson et al found IgG antibodies to BSA were not significantly
increased at onset of IDDM. Currently, the exact nature of the
relationship between BSA and IDDM remains unclear.
The
routine use of a post-workout shake might be the
most important nutritional supplementation habit for
enhancing body composition. It is probably in this manner whey can be
best utilized by athletes concerned
with maximizing lean body mass and strength
Amino
acid availability following a workout regulates protein synthesis and
degradation. Because of the anabolic effects of insulin on protein
synthesis and protein degradation, a rapid synergistic response occurs
when both amino acids and insulin increase after a protein-containing
meal.It is thought the body is highly insulin sensitive after
exercise and preferentially shuttles carbohydrates and protein into
muscle cells rather than fat cells. Experts think this sensitivity
gradually declines post-workout for about two hours until it again
reaches normal sensitivity.
A
carbohydrate-whey protein supplement has been shown to be more
effective in generating a plasma insulin response than either a
carbohydrate or a protein supplement alone during recovery from
prolonged exhaustive exercise. The rate of muscle glycogen storage was
also significantly faster during the carbohydrate-protein treatment.
The participants in this study ingested 112.0 g carbohydrate and 40.7 g
protein immediately after each exercise bout.
Whey
is an excellent choice as a protein source
for the post-workout
shake because of its rapid transit into the small intestine and because
of its high levels of branched chain amino acids and glutamine.
Glucose-polymers or maltodextrins are considered to be the best form of
carbohydrates to use because of their ability to stimulate an insulin
response. Fat should not
be added because it might slow transit and decrease the
insulin response.