Proteolytic and Peptidolytic Activities in Commercial Pancreatic Protease Preparations and Their Relationship to 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

Endoproteinase and exopeptidase activities in the commercially available pancreatic protease preparations Corolase PP, PTN 3.0S, pancreatin, PEM 2500S, PEM 2700S, and PEM 800S were quantified using synthetic peptide substrates. These preparations were generally found to be low in aminopeptidase and dipeptidase activity. Trypsin and chymotrypsin, albeit in different ratios, were present in all pancreatic preparations. Elastase was present only in Corolase PP and pancreatin. The ability of these protease preparations to hydrolyze the insoluble heat denaturted whey protein, lactalbumin, was compared and contrasted with that of crystalline trypsin, chymotrypsin, and elastase in addition to a commercial exopeptidase preparation, Debitrase DBP.20. When the source, number, or ratio of endoprotease activity changes, there are distinctive differences in products produced with respect to percentage degrees of hydrolysis, gel permeation profile, solubility, and free amino acids present in the hydrolysate.

Original languageEnglish
Pages (from-to)2973-2981
Number of pages9
JournalJournal of Agricultural and Food Chemistry
Volume42
Issue number12
DOIs
Publication statusPublished - 1 Dec 1994
Externally publishedYes

Keywords

  • enzymatic hydrolysis
  • Pancreatic proteases
  • proteolytic activity
  • whey protein

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