The modifications of bovine β-lactoglobulin -effects on its structural and functional properties

Abstract

Due to its excellent techno-functional properties, high nutritional value and low cost, β-lactoglobulin (BLG), the main protein in whey, is a frequently used additive in wide range of food products. It is also considered as an acid-resistant drug carrier for the delivery of pharmaceutical and nutraceutical agents. However, BLG is the main allergen of milk. A variety of methods has been explored for the modification of BLG in attempts to improve its functional properties and to decrease its allergenicity. Due to its compact globular structure, BLG is relatively resistant to modifications, especially under mild conditions. BLG can be modified by physical, chemical and enzymatic treatments. Although chemical modifications offer efficient routes to the alteration of the structural and functional properties of proteins, they are associated with safety concerns. In the last decade, there is a tendency for application of novel non-thermal physical processing methods, as well as enzymes in order to obtain BLG derivatives with desirable properties. The objective of this review is to overview the chemical, physical and enzymatic processing techniques utilized to modify BLG and their effects on the structural and functional properties of BLG.