Purification and characterization of an ε-poly-L-lysine-degrading enzyme from the ε-poly-L-lysine-tolerant Chryseobacterium sp OJ7

被引：19

作者：

Kito, M

Takimoto, R

Onji, Y

Yoshida, T

Nagasawa, T ^{[1
]}

机构：

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

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

来源：

JOURNAL OF BIOSCIENCE AND BIOENGINEERING | 2003年 / 96卷 / 01期

关键词：

epsilon-poly-L-lysine; endopeptidase; purification; Chryseobacterium sp OJ7; epsilon-poly-L-lysine-tolerant bacterium;

D O I：

10.1016/S1389-1723(03)90105-8

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 epsilon-poly-L-lysine-degrading enzyme of the epsilon-poly-L-lysine-tolerant Chryseobacterium sp. OJ7 was purified and characterized. The bacterium excreted the enzyme into the culture filtrate. The purified enzyme has a molecular mass of approximately 38.4 kDa and consists of two identical subunits with a molecular mass of 19.5 kDa. The enzyme catalyzed the endo-type degradation of epsilon-poly-L-lysine. A correlation between the epsilon-poly-L-lysine tolerance of the bacterium and the high epsilon-poly-L-lysine-degrading activity was suggested.

引用

页码：92 / 94

页数：3

共 10 条

[1]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[2] Purification and characterization of an ε-poly-L-lysine-degrading enzyme from an ε-poly-L-lysine-producing strain of Streptomyces albulus [J].