作者: MARGARET M. MULLALLY , DANIEL M. O'CALLAGHAN , RICHARD J. FITZGERALD , W.J. DONNELLY , JOHN P. DALTON
DOI: 10.1111/J.1365-2621.1995.TB05643.X
关键词:
摘要: A proteolytic preparation from porcine pancreas was isolated. Trypsin, chymotrypsin and elastase were characterized their time-dependent stability at 37 o C studied. The supernatant of a 30% (w/v) saturated ammonium sulfate precipitation pancreatic extract (30S) developed to pilot-scale level. influence zymogen activation time on molecular characteristics whey protein hydrolysates produced by 30S the commercial Corolase PP compared. Amino acid analysis gel permeation chromatography used characterize lactalbumin produced. Physicochemical could be altered manipulation conditions in proteinase preparations during subsequent hydrolysis