PURIFICATION OF X-PROLYL DIPEPTIDYL AMINOPEPTIDASE FROM LACTOBACILLUS-CASEI SUBSPECIES

被引：15

作者：

ELABBOUDI, M

ELSODA, M

PANDIAN, S

SIMARD, RE

OLSON, NF

机构：

[1] UNIV LAVAL,FAC SCI AGR & ALIMENTAT,CTR RECH STELA,QUEBEC CITY G1K 7P4,QUEBEC,CANADA

[2] UNIV ALEXANDRIA,FAC AGR,ALEXANDRIA,EGYPT

[3] UNIV WISCONSIN,CTR DAIRY RES,MADISON,WI 53706

来源：

INTERNATIONAL JOURNAL OF FOOD MICROBIOLOGY | 1992年 / 15卷 / 1-2期

基金：

加拿大自然科学与工程研究理事会;

关键词：

X-PROLYL DIPEPTIDYL AMINOPEPTIDASE; LACTOBACILLUS-CASEI; PURIFICATION;

D O I：

10.1016/0168-1605(92)90138-S

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Prolyl dipeptidylaminopeptidases from two subspecies of Lactobacillus casei were purified and biochemically characterized. L. casei ssp. casei UL21 (a debittering strain) and L. casei ssp. rhamnosus UL26 (a non-debittering strain) were the source bacteria for this study. Purification of the enzymes from both the sources was effected by a gel filtration step through Sephacryl S-300 followed by ion-exchange chromatography through DEAE Sephacel. This rendered an electrophoretically homogeneous enzyme preparation. The purified enzymes from both the sources showed similar temperature optimum (45-degrees-C) and pH optimum (7.0). Their activity profiles on various substrates and the nature of inhibition by different inhibitors were also found to be similar, indicating that this enzyme is perhaps not significantly involved in the debittering process during the maturation of cheese.

引用

页码：87 / 98

页数：12

共 19 条

[1] X-PROLYL-DIPEPTIDYL AMINOPEPTIDASE OF LACTOBACILLUS-DELBRUECKII SUBSP BULGARICUS - CHARACTERIZATION OF THE ENZYME AND ISOLATION OF DEFICIENT MUTANTS [J].