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 degrees 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 activat ion time on molecular characteristics of whey protein hydrolysates pro duced by 30S and the commercial pancreatic preparation Corolase PP wer e compared. Amino acid analysis and gel permeation chromatography were used to characterize lactalbumin hydrolysates produced. Physicochemic al characteristics of whey protein hydrolysates could be altered by ma nipulation of zymogen activation conditions in pancreatic proteinase p reparations to be used during subsequent protein hydrolysis.