Characterisation of a cell-envelope proteinase from Lactobacillus helveticus

被引：22

作者：

Hébert, EM

Raya, RR

de Giori, GS

机构：

[1] CONICET, Ctr Referencia Lactobacilos, RA-4000 San Miguel De Tucuman, Tucuman, Argentina

[2] Univ Nacl Tucuman, Fac Bioquim Quim & Farm, Catedra Microbiol Super, RA-4000 San Miguel De Tucuman, Tucuman, Argentina

来源：

BIOTECHNOLOGY LETTERS | 1999年 / 21卷 / 09期

关键词：

Lactobacillus; proteinase;

D O I：

10.1023/A:1005590731382

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

The cell-envelope proteinase from Lactobacillus helveticus CRL 1062 was detected in the cell membrane fraction. The enzyme remained associated with the cells even after treatment with lysozyme and was not released from washed cells in absence of calcium. The proteinase was maximally active at pH 6.5-7.0 and 42 degrees C and hydrolysed alpha- and beta-caseins at different rates. Activity was inhibited (98%) by 1 mM PMSF, suggesting it was a serine-type protease.

引用

页码：831 / 834

页数：4

共 8 条

[1] STABILITY AND SPECIFICITY OF THE CELL WALL-ASSOCIATED PROTEINASE FROM LACTOCOCCUS-LACTIS SUBSP CREMORIS H2 RELEASED BY TREATMENT WITH LYSOZYME IN THE PRESENCE OF CALCIUM-IONS [J].