Impact of enzymatic hydrolysis followed by transglutaminase-induced cross-linking on decreasing antigenicity and reserving partial interfacial properties of whey protein isolate.

Whey protein isolate (WPI) was hydrolyzed by alcalase and trypsin for three hydrolysis degrees (DHs), followed by transglutaminase (TGase) induced cross-linking. The prepared products were measured for surface hydrophobicity and emulsifying and foaming properties, as well as in vitro antigenicity for α-lactalbumin and β-lactoglobulin. The results indicated that enzymatic hydrolysis of WPI mostly resulted in WPI hydrolysates with significantly decreased antigenicity of α-lactalbumin and β-lactoglobulin, especially in the case of a higher DH value.