Enzymatic hydrolysis of beta-lactoglobulin

Selective depiction of beta-lactoglobulin in whey protein products has been identified as a potential approach to the preparation of whey protein prod ucts with modified responses to heat treatment. The rationale for this appr oach is based on the principle that through a reduction in the content of b eta-lactoglobulin, the effects of any heat-mediated aggregates involving be ta-lactoglobulin (e.g. membrane fouling deposits, increased viscosity) shou ld be substantially reduced. In addition, any anti-nutritional and/or aller gic properties of the beta-lactoglobulin molecule may be modulated through a reduction in the content of this protein via conversion into smaller pept ide species. The approach reported here has been to deplete beta-lactoglobu lin in commercial whey protein concentrate (WPC) through selective enzymati c hydrolysis, Using this approach, beta-lactoglobulin has been depleted whi le the remaining whey proteins have been left largely intact. The heat stab ility and gelation properties of two prototype hydrolysates have been chara cterised, and results are presented here.