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Beta-lactoglobulin (BLG) is the main whey protein and it is frequently used  additive in wide range of food products due to its excellent  techno-functional properties, high nutritional value and low cost. It is also  considered as acid-resistant drug carrier for delivery of pharmaceutical and  nutraceutical agents. However, BLG is the main allergen of milk. A variety of  methods have been explored for modification of BLG in attempt 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 way of  alteration of protein structural and functional properties, they are  associated with safety concern. 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 with desirable properties. The objective of  this review is to overview chemical, physical and enzymatic processing  techniques utilized to modify BLG and their effects on structure and  functional properties of BLG. [Projekat Ministarstva nauke Republike Srbije,  br. 172024 and FP7 RegPot project FCUB ERA GA No. 256716

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