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Zymogen activation in pancreatic endoproteolytic preparations and influence on some whey protein hydrolysate characteristics

A proteolytic preparation from porcine pancreas was isolated. Trypsin, chymotrypsin and elastase were characterized and their time-dependent stability at 37 o C was studied. The supernatant of a 30% (w/v) saturated ammonium sulfate precipitation of a pancreatic extract (30S) was developed to pilot-scale level. The influence of zymogen activation time on molecular characteristics of whey protein hydrolysates produced by 30S and the commercial pancreatic preparation Corolase PP were compared. Amino acid analysis and gel permeation chromatography were used to characterize lactalbumin hydrolysates produced. Physicochemical characteristics of whey protein hydrolysates could be altered by manipulation of zymogen activation conditions in pancreatic proteinase preparations to be used during subsequent protein hydrolysis