The liquid remains of milk after the milk is rained and curdled is termed as whey. It is a product that is similar to cheese and casein and is used for a vast number of commercial purposes. Whey protein is made up of a number of mixtures of milk and casein. In milk of cow, there is 80% casein protein and 20% whey protein and similarly, in human milk, there is a mixture of 30% casein protein and 70% whey protein. Whey proteinconsists of several different proteins, such as Alpha-lactalbumin, beta lactoglobulin, serum albumin, and immunoglobulins. Lactalbuminis also known as whey protein.
Function of beta-lactoglobulin
The main objective of beta-lactoglobulin powder is to improve the immune system of infants.It is the second most important protein that is found in milk. The function of beta-lactoglobulin is different from that of Alpha-lactalbumin. Beta-lactoglobulin, despite its most prominent compositions from the distribution of globular proteins, beta-lactoglobulin can bind a number of hydrophobic molecules. The function of beta-lactoglobulin is similar to that of lipocalin i.e. it has the ability to transport hydrophobic molecules that are small in size. Beta-lactoglobulin is beneficial in many of the biological processes like improving the immune system, transport of pheromone, retinoid-binding,and interactions of Cancer cells.
Features of beta-lactoglobulin as a whey protein
Beta lactoglobulin is a globular protein of the lipocalin family. The cavity formed in the protein can be the binding site for a range of low molecular weight compounds, including fatty acids and retinal. A significant feature of beta-lactoglobulin is thesulfur chemistry of this protein.
It is the major whey protein of bovine milk and is a natural molecular Nanocarrier for hydrophobic molecules, retinoic acid, cholesterol, vitamin D, various Aroma compounds and fatty acids, for example, bind with its hydrophobic calyx. This provides a means of enhancing the stability of beta-lactoglobulin during food manufacturing processes and offer greater control over its ability to deliver specific bioactivities in food.
System- the changes observed on the beta-lactoglobulin irradiated in solution, related to secondary and mainly to tertiary structure, explain, at least partially, the protein aggregation. The major bands remained intact as the sub-unit molecular weight of a native beta-lactoglobulin. An increase in protein concentration of beta-lactoglobulin revealed that the gel permission chromatogram profile was similar to that of the control, which was not irradiated.
It is generally thought that disulfide cross-linking is the main basis of gel formation, an investigation where disulfide formation was prevented gel fracture proteins were greatly altered. When gels are formed in the presence of disulfide, there were minor effects on the properties of the gel.
A significant feature of beta-lactoglobulin is the sulfur chemistry of this protein. The reasons for the apparent discrepancy between these sets of results are unclear. However, there are few major important differences between α-lactalbumin and Alpha-lactalbumin.