β-lactoglobulin
β-lactoglobulin
is the major protein present in whey protein. It is about 50% of the whey
protein. It has a numerous binding sites, which binds minerals, fat soluble
vitamins and lipids, and act as a transport protein for desirable lipophilic compounds
(tocopherol and vitamin A).
Modifications
are made in the β-lactoglobulin and made many products which have the strong
antiviral activity against HIV strains 1 and 2.
ɑ-Lactalbumin
Also
it is major protein in milk which constitute about 20-25% of the total whey
protein in milk. This protein comprises of an excellent amino acid profile,
which is rich in lysine, leucine, threonine, tryptophan and cystine.
The
main known biological function of ɑ-lactalbunim is to modulate the synthesis of
lactose in the mammary gland, also protein is strongly advocated in the
formulation of “humanized” infant formulas and to create other products for
people with limited or restricted protein intakes.
Work
on ɑ-lactalbumin shows that it may be effective as an anti-cancer agent in
several different types of cancer.
Immunoglobulins
These
are the complex group of proteins that make a significant contribution to the protein
content and also take part in exerting an important immunological function.
They are well known to provide disease
protection to newborns through passive immunity and there is well-known
evidence the immunoglobulins taking high contribution in the disease control in
adults. It is known that whey protein concentrates from mixed milk supplies
generally contain sufficient antibody to E. coli K-99 to meet the requirements
of the USDA to serve as a colostrum supplement.
Bovine serum albumin
The
amino acid profile of bovine serum is very good and it is a good source of
essential amino acid.
BSA
has the capability to bind the free fatty acids, other lipids and flavor
compounds. BSA's primary function has been associated with its lipid binding
properties. It may play a role in mediating lipid oxidation. Denatured BSA
might reduce the probability of a person acquiring certain diseases, such as
insulin dependent diabetes or auto-immune disease.
Lactoferrin
It
is an iron binding protein. It has a potential and has a good capability of
acting as an antimicrobial agent related to its iron chelating ability, it
deprive the microorganism of from iron. Most recently, it has been shown to
have a number of other physiological and biological functions. The biological
activities of lactoferrin include iron transport, antimicrobial activity,
antifungal activity, antiviral activity, anticancer activity, toxin binding
properties, immunomodulating effects, wound and wound healing, and
anti-inflammatory activity.
Lactoperoxidase
Lactoperoxidase
system is a good antimicrobial agent and has been identified in milk, saliva
and tears. This system also have been proven to be both bacterial
and bacteriostatic to a wide variety of microorganisms, while having no
effect on the proteins and enzymes of the organisms producing it. Clinical
studies have supported the possibility that plaque accumulation, gingivitis and
early onset carries may be reduced by appropriate lactoperoxidase preparations.
Glycomacropeptide
Glycomacropeptide
is the part of the whey when we precipitate the casein by the action of enzyme
rennin, it is about 20% contributes in this whey. Usually GMP, the glycosylated
portion of caseinomacropeptide (CMP), is present in sweet whey formed following
the K-casein cleavage and casein precipitation by rennin; it is absent from
acid whey.
The
biological and physiological properties that have been attributed to GMP or
peptides derived from it include: reduction in gastric secretion, dental plaque
and dental caries inhibition, growth promoting activity for Bifidobacteria,
product for control of phenylketunoria, inhibition of platelet aggregation and
others. GMP cans suppress appetite via stimulation of the pancreatic hormone
cholecystokinin (CCK) release. It alters pigment production in melanocytes,
acts as prebiotic and has immunomodulatory actions. Physiologic activity of GMP
depends on its glycosylation.
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