Zymogen Activation in Pancreatic Endoproteolytic Preparations and Influence on Some Whey Protein Hydrolysate Characteristics

MARGARET M. MULLALLY, DANIEL M. O'CALLAGHAN, RICHARD J. FITZGERALD, W. J. DONNELLY, JOHN P. DALTON

Research output: Contribution to journalArticlepeer-review

Abstract

A proteolytic preparation from porcine pancreas was isolated. Trypsin, chymotrypsin and elastase were characterized and their time‐dependent stability at 37°C was studied. The supematant 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.

Original languageEnglish
Pages (from-to)227-233
Number of pages7
JournalJournal of Food Science
Volume60
Issue number2
DOIs
Publication statusPublished - Mar 1995

Keywords

  • endoprotease
  • hydrolysates
  • whey protein
  • zymogen activation

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