Lactoglobulin
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β-Lactoglobulin (BLG) 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. Its structure, properties and biological role have been reviewed many times. BLG is considered to be a milk allergen.


Function

The major protein in whey is β-lactoglobulin, followed by
α-lactalbumin Lactalbumin, alpha-, also known as LALBA, is a protein that in humans is encoded by the ''LALBA'' gene. Overview α-Lactalbumin is a protein that regulates the production of lactose in the milk of almost all mammalian species. In primates, al ...
(β-lactoglobulin ≈⁠ ⁠65%, α-lactalbumin ≈⁠⁠ ⁠25%, serum albumin ≈⁠⁠ ⁠8%, other ≈⁠ ⁠2%). β-lactoglobulin is a lipocalin protein, and can bind many hydrophobic molecules, suggesting a role in their transport. β-lactoglobulin has also been shown to be able to bind iron via siderophores and thus might have a role in combating pathogens. Upon ingestion BLG is able to shuttle complexed iron into human immune cells, thereby providing micronutrition to these cells and participating in immune tolerance. A homologue of β-lactoglobulin is lacking in human breast milk.


Structure

Several variants have been identified, the main ones in the cow being labelled A and B. Because of its abundance and ease of purification, it has been subjected to a wide range of biophysical studies. Its structure has been determined several times by X-ray crystallography and NMR.; β-lactoglobulin is of direct interest to the
food industry The food industry is a complex, global network of diverse businesses that supplies most of the food consumed by the world's population. The food industry today has become highly diversified, with manufacturing ranging from small, traditiona ...
since its properties can variously be advantageous or disadvantageous in
dairy A dairy is a business enterprise established for the harvesting or processing (or both) of animal milk – mostly from cows or buffaloes, but also from goats, sheep, horses, or camels – for human consumption. A dairy is typically located on ...
products and processing. Bovine β-lactoglobulin is a relatively small protein of 162 residues, with an 18.4 kDa. In
physiological condition Physiological condition or, more often "physiological conditions" is a term used in biology, biochemistry, and medicine. It refers to conditions of the external or internal milieu that may occur in nature for that organism or cell system, in contr ...
s it is predominantly dimeric, but dissociates to a monomer below about pH 3, preserving its
native state In biochemistry, the native state of a protein or nucleic acid is its properly folded and/or assembled form, which is operative and functional. The native state of a biomolecule may possess all four levels of biomolecular structure, with the s ...
as determined by using NMR. Conversely, β-lactoglobulin also occurs in tetrameric, octameric and other multimeric aggregation forms under a variety of natural conditions. β-Lactoglobulin solutions form
gel A gel is a semi-solid that can have properties ranging from soft and weak to hard and tough. Gels are defined as a substantially dilute cross-linked system, which exhibits no flow when in the steady-state, although the liquid phase may still di ...
s in various conditions, when the native structure is sufficiently destabilised to allow aggregation. Under prolonged heating at low pH and low
ionic strength The ionic strength of a solution is a measure of the concentration of ions in that solution. Ionic compounds, when dissolved in water, dissociate into ions. The total electrolyte concentration in solution will affect important properties such as ...
, a transparent `fine-stranded' gel is formed, in which the protein molecules assemble into long stiff fibres. β-Lactoglobulin is the main component of milk skin, coagulating and denaturing when the milk boils. Once denatured, the β-Lactoglobulin forms a thin gelatinous film on the surface of the milk. Folding intermediates for this protein can be studied using light spectroscopy and denaturant. Such experiments show an unusual but important intermediate composed purely of alpha helices, despite the fact that the native structure is beta sheet. Evolution has probably selected for the helical intermediate to avoid aggregation during the folding process.


Clinical significance

As milk is a known allergen,listed in Annex IIIa of Directive 2000/13/EC manufacturers in European Union need to prove the presence or absence of β-lactoglobulin to ensure their labelling satisfies the requirements of the
EC Directive A directive is a legal act of the European Union that requires member states to achieve a particular result without dictating the means of achieving that result. Directives first have to be enacted into national law by member states before the ...
. Food testing laboratories can use
enzyme linked immunosorbent assay The enzyme-linked immunosorbent assay (ELISA) (, ) is a commonly used analytical biochemistry assay, first described by Eva Engvall and Peter Perlmann in 1971. The assay uses a solid-phase type of enzyme immunoassay (EIA) to detect the presence ...
methods to identify and quantify β-lactoglobulin in food products. Though β-lactoglobulin is considered a major allergen, the protective impact of the consumption of raw milk has been shown to dependent on the protein-content of the whey fraction and thus of β-lactoglobulin. This great contrast, on the one hand an allergen and on the other protective, has now been linked with its ability to carry micronutrient. When β-lactoglobulin carried micronutrient it acted tolerogenic and protected against allergy development. However, when the loading was missing, it turned into an allergen. Laboratory polymerization of β-lactoglobulin by microbial transglutaminase reduces its allergenicity in children and adults with an IgE-mediated cow’s milk allergy.


Cows breeding

In 2018 it was announced that a genetically modified cows were grown. The cows had its β-Lactoglobulin producing genes removed by a zygote-mediated deletion process.


See also

*
Caseine Casein ( , from Latin ''caseus'' "cheese") is a family of related phosphoproteins ( αS1, aS2, β, κ) that are commonly found in mammalian milk, comprising about 80% of the proteins in cow's milk and between 20% and 60% of the proteins in human ...


References

{{Authority control Lipocalins Mammalian proteins Milk