PURIFICATION AND CHARACTERIZATION OF A NEW TRIPEPTIDASE FROM LACTOBACILLUS-DELBRUECKII SSP BULGARICUS B14

被引：13

作者：

BOCKELMANN, W

BEUCK, HP

LICK, S

HELLER, K

机构：

[1] Federal Dairy Research Center, Institute of Microbiology, 24103 Kiel

来源：

INTERNATIONAL DAIRY JOURNAL | 1995年 / 5卷 / 05期

关键词：

D O I：

10.1016/0958-6946(95)00029-3

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

A new tripeptidase was purified from Lactobacillus delbrueckii ssp. bulgaricus B14. Ammonium sulphate precipitation, anion exchange chromatography, hydrophobic interaction chromatography and HPLC-gel filtration were used for purification. SDS-PAGE skewed a single band at 29 kDa. On gel filtration, an apparent molecular weight of about 85 kDa was observed, indicating that the enzyme probably consists of three subunits. It is a metal-dependent enzyme with a temperature optimum of 40 degrees C and a pH optimum of pH 6.0. Of all substrates tested, only tripeptides were cleaved, the K-m-value for the cleavage of Leu-Leu-Leu being 0.83 mM. Proline- containing tripeptides, however, were not cleaved. Until now, there has been no report on the purification of a similar enzyme in other lactic acid bacteria.

引用

页码：493 / 502

页数：10

共 18 条

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