β-Lactoglobulin is the major whey protein of cow and sheep’s milk (~3 g/l), and is also present in many other mammalian species; a notable exception being humans.
Unlike the other main whey protein, α-lactalbumin, no clear function has been identified for β-lactoglobulin. ß-lactoglobulin is a lipocalin protein, and can bind many hydrophobic molecules, suggesting a role in their transport. ß-lactoglobulin has also been shown to be able to bind iron via siderophores and thus might have a role in combating pathogens. A homologues of ß-lactoglobulin is lacking in human breast milk.
As milk is a known allergen (as listed in Annex IIIa of Directive 2000/13/EC), manufacturers need to prove the presence or absence of β-lactoglobulin to ensure their labelling satisfies the requirements of the aforementioned directive. Food testing laboratories can use ELISA (enzyme linked immunosorbent assay) methods to identify and quantify β-lactoglobulin in food products.
Laboratory polymerization of β-lactoglobulin by microbial transglutaminase reduces its allergenicity in children and adults with an IgE-mediated cow’s milk allergy.
- None are recorded.
Source: Wikipedia, https://en.wikipedia.org/wiki/Beta-lactoglobulin