Purification and some properties of ε-poly-L-lysine-degrading enzyme from Kitasatospora sp CCTCC M205012

被引：4

作者：

Feng, Xiaohai ^{[1
]}

Xu, Hong ^{[1
]}

Xu, Xiaoying ^{[2
]}

Yao, Jun ^{[1
]}

Yao, Zhong ^{[1
]}

机构：

[1] Nanjing Univ Technol, Coll Life Sci & Pharm, State Key Lab Mat Oriented Chem Engn, Nanjing 210009, Peoples R China

[2] Jiangsu Prov Supervising & Testing Res Inst Prod, Nanjing 210009, Peoples R China

来源：

PROCESS BIOCHEMISTRY | 2008年 / 43卷 / 06期

基金：

中国国家自然科学基金; 国家高技术研究发展计划(863计划);

关键词：

epsilon-poly-L-lysine-degrading enzyme; Kitasatospora sp CCTCC m205012; purification; anion-exchange chromatography; properties; degradation;

D O I：

10.1016/j.procbio.2008.02.009

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

An epsilon-poly-L-lysine-degrading enzyme (PLD) from Kitasatospora sp. CCTCC M205012 has been purified to homogeneity by three steps of anion-exchange chromatography including DEAE-Sepharose, Source 15Q and Mono Q, with a 500-fold increase in specific activity and 40.9% yield. The PLD has a molecular mass of approximately 87.0 kDa and consists of two identical subunits with a molecular mass of 43.6 kDa. Electrophoretic shows that the PLD isoelectric point was about 7.2. The optimum temperature and pH for the PLD was 30 degrees C and 7.0, respectively. The PLD was deactivated by EDTA, which was indicated that the enzyme was a metallo enzyme. The activity of PLD was stimulated by Co2+ and inhibited by Ca2+ remarkably. The apparent K-m with L-lysyl-p-nitroanilide as substrate was 0.216 mM and the V-max was 0.112 mmol/min mg. The PLD was an exo-type enzyme and monomers of L-lysine were detected during the enzymatic degradation of epsilon-PL. (C) 2008 Published by Elsevier Ltd.

引用

页码：667 / 672

页数：6

共 19 条

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