PARTIAL CHARACTERIZATION OF A WHEY PROTEIN CONCENTRATE AND ITS ENZYME HYDROLYSATES

A whey protein concentrate (WPC) was produced from fresh whey by ultrafiltration (MW cut off 10 kDa) and lyophilization. Enzymatic hydrolysis was performed with three enzyme systems: pancreatin (PA), protamex (PR) or alcalase 0.6L (AL) to produce hydrolysates with 20% degree of hydrolysis (DH). The peptide profiles of the hydroly sates were determined by high performance capillary electrophoresis (HPCE). The relationship between enzyme system and preferential protein substrate could be established. The alcalase hydrolysate (ALH) differed from the other two hydrolysates, and the enzyme showed the lowest specificity for β‐lactaglobulin. Considering the protein content from WPC the pancreatin hydrolytic system was the most efficient leaving only 4.69% unhydrolyzed protein in the final hydrolysate (PAH). For 20% degree of hydrolysis alcalase left 7.98% unhydrolyzed protein, while protamex left 9.81% unhydrolyzed protein in the final hydrolysate.