Screening, purification and characterization of a novel cold-active and organic solvent-tolerant lipase from Stenotrophomonas maltophilia CGMCC 4254

被引：58

作者：

Li, Mu ^{[1
]}

Yang, Li-Rong ^{[1
]}

Xu, Gang ^{[1
]}

Wu, Jian-Ping ^{[1
]}

机构：

[1] Zhejiang Univ, Dept Chem & Biol Engn, Inst Bioengn, Hangzhou 310027, Zhejiang, Peoples R China

来源：

BIORESOURCE TECHNOLOGY | 2013年 / 148卷

基金：

中国国家自然科学基金;

关键词：

Lipase; Solvent tolerant; Cold-active; Stenotrophomonas maltophilia; Non-aqueous; ALKALINE LIPASE; ENZYMES; OIL; STABILITY; IMPROVEMENT; ADAPTATION; EMULSIONS; BACTERIA; STRAIN; ESTER;

D O I：

10.1016/j.biortech.2013.08.101

中图分类号：

S2 [农业工程];

学科分类号：

0828 ;

摘要：

An extracellular organic solvent-tolerant and cold-active lipase producing bacterium was isolated from oil-contaminated soil samples, and identified taxonomically as Stenotrophomonas maltophilia. The lipase from S. maltophilia CGMCC 4254 (SML) was purified 60.5-fold to homogeneity with 38.9 U/mg specific activity. Partially purified SML displayed remarkable stability in 50% and 100% (v/v) hydrophobic organic solvents after incubation for 7 days. The enzyme also retained more than 50% of its residual activity in several pure hydrophilic organic solvents after incubation for 7 days. SML showed 57% maximum activity at 5 degrees C, and had optimal activity at 35 degrees C. These unique properties of SML make it promising as a biocatalyst for industrial processes. (C) 2013 Elsevier Ltd. All rights reserved.

引用

页码：114 / 120

页数：7

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