A Novel pH-Stable, Bifunctional Xylanase Isolated from a Deep-Sea Microorganism, Demequina sp JK4

被引：22

作者：

Meng Xin ^{[1
]}

Shao, Zongze ^{[3
]}

Hong, Yuzhi ^{[2
]}

Lin, Ling ^{[1
]}

Li, Chanjuan ^{[1
]}

Liu, Ziduo ^{[1
]}

机构：

[1] Huazhong Agr Univ, Coll Life Sci & Technol, State Key Lab Agr Microbiol, Wuhan 430070, Peoples R China

[2] Huazhong Agr Univ, Coll Plant Sci & Technol, Wuhan 430070, Peoples R China

[3] State Ocean Adm, Inst Oceanog 3, Key Lab Marine Biogenet Resources, Xiamen 361005, Peoples R China

来源：

JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY | 2009年 / 19卷 / 10期

关键词：

Demequina sp JK4; xylanase; pH-stable; bifunctional; carbohydrate-binding module; CRYSTAL-STRUCTURE; EXPRESSION; PURIFICATION; SPECIFICITY; SEQUENCE; CLONING; FAMILY; GENES;

D O I：

10.4014/jmb.0901.017

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：

A genomic library was constructed to clone a xylanase gene (Mxyn10) from Demequina sp. JK4 isolated from a deep sea. Mxyn10 encoded a 471 residue protein with a calculated molecular mass of 49 kDa. This protein showed the highest sequence identify (70%) with the xylanase from Streptomyces lividans. Mxyn10 contains a catalytic domain that belongs to the glycoside hydrolase family 10 (GH10) and a carbohydrate-binding module (CBM) belonging to family 2. The optimum pH and temperature for enzymatic activity were pH 5.5 and 55 degrees C, respectively. Mxyn10 exhibited good pH stability, remaining stable after treatment with buffers ranging from pH 3.5 to 10.0. The protein was not significantly affected by a variety of chemical reagents, including some compounds that usually inhibit the activity of other related enzymes. In addition, Mxyn10 showed activity on cellulose. These properties mark Mxyn10 as a potential enzyme for industrial application and saccharification processes essential for bioethanol production.

引用

页码：1077 / 1084

页数：8

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