TY - JOUR
T1 - Proteolytic and Peptidolytic Activities in Commercial Pancreatic Protease Preparations and Their Relationship to Some Whey Protein Hydrolysate Characteristics
AU - Mullally, Margaret M.
AU - O'Callaghan, Daniel M.
AU - FitzGerald, Richard J.
AU - Donnelly, W. J.
AU - Dalton, John P.
PY - 1994/12/1
Y1 - 1994/12/1
N2 - 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.
AB - 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.
KW - enzymatic hydrolysis
KW - Pancreatic proteases
KW - proteolytic activity
KW - whey protein
UR - http://www.scopus.com/inward/record.url?scp=0000081341&partnerID=8YFLogxK
U2 - 10.1021/jf00048a062
DO - 10.1021/jf00048a062
M3 - Article
AN - SCOPUS:0000081341
SN - 0021-8561
VL - 42
SP - 2973
EP - 2981
JO - Journal of Agricultural and Food Chemistry
JF - Journal of Agricultural and Food Chemistry
IS - 12
ER -