Occurrence of ε-polu-L-lysine-degrading enzyme in ε-poly-L-lysine-tolerant Sphingobacterium multivorum OJ10:: purification and characterization

被引：24

作者：

Kito, M

Onji, Y

Yoshida, T

Nagasawa, T ^{[1
]}

机构：

[1] Gifu Univ, Dept Biomol Sci, Fac Engn, Gifu 5011193, Japan

[2] Chisso Corp, Yokohama Res Ctr, Kanazawa Ku, Yokohama, Kanagawa 2368065, Japan

来源：

FEMS MICROBIOLOGY LETTERS | 2002年 / 207卷 / 02期

关键词：

epsilon-poly-L-lysine; aminopeptidase; Sphingobacterium multivorum;

D O I：

10.1111/j.1574-6968.2002.tb11043.x

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

epsilon-Poly-L-lysine (epsilon-PL)-degrading enzyme was found in the epsilon-PL-tolerant strain Sphingobacterium multivorum OJ10 and purified to homogeneity. The purified enzyme has a molecular mass of approximately 80 kDa. The enzyme catalyzed exo-type degradation of epsilon-PL and released L-lysine. The enzyme was a Co2- or Ca2+ ion-activated aminopeptidase. (C) 2002 Federation or European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：147 / 151

页数：5

共 10 条

[1] AMINOPEPTIDASE CO, A NEW YEAST PEPTIDASE [J].