PROTEOLYTIC AND PEPTIDOLYTIC ACTIVITIES IN COMMERCIAL PANCREATIC PROTEASE PREPARATIONS AND THEIR RELATIONSHIP TO SOME WHEY-PROTEIN HYDROLYSATE CHARACTERISTICS

被引：55

作者：

MULLALLY, MM ^{[1
]}

OCALLAGHAN, DM ^{[1
]}

FITZGERALD, RJ ^{[1
]}

DONNELLY, WJ ^{[1
]}

DALTON, JP ^{[1
]}

机构：

[1] DUBLIN CITY UNIV, SCH BIOL SCI, DUBLIN 11, IRELAND

来源：

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY | 1994年 / 42卷 / 12期

关键词：

PANCREATIC PROTEASES; PROTEOLYTIC ACTIVITY; WHEY PROTEIN; ENZYMATIC HYDROLYSIS;

D O I：

10.1021/jf00048a062

中图分类号：

S [农业科学];

学科分类号：

09 ;

摘要：

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.

引用

页码：2973 / 2981

页数：9

共 57 条

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