Cloning, expression and characterization of an alkaline thermostable GH9 endoglucanase from Thermobifida halotolerans YIM 90462T

被引：30
|
作者：
Zhang, Feng [1 ,2 ]
Chen, Jiu-Jiu [1 ,2 ]
Ren, Wan-Zeng [1 ,2 ]
Nie, Guo-Xing [3 ]
Ming, Hong [4 ]
Tang, Shu-Kun [1 ,2 ]
Li, Wen-Jun [1 ,2 ]
机构：
[1] Yunnan Univ, Key Lab Microbial Divers SW China, Minist Educ, Kunming 650091, Peoples R China
[2] Yunnan Univ, Lab Conservat & Utilizat Bioresources, Yunnan Inst Microbiol, Kunming 650091, Peoples R China
[3] Henan Normal Univ, Coll Life Sci, Xinxiang 453007, Peoples R China
[4] Xinxiang Med Univ, Dept Life Sci & Technol, Xinxiang 453003, Peoples R China
来源：
BIORESOURCE TECHNOLOGY | 2011年 / 102卷 / 21期
关键词：
Thermobifida halotolerans YIM 90462(T); Endoglucanase; Thermostable; Alkali-tolerant; EMENDED DESCRIPTION; SP NOV; PURIFICATION;
D O I：
10.1016/j.biortech.2011.08.019
中图分类号：
S2 [农业工程];
学科分类号：
0828 ;
摘要：
The endoglucanase gene, thcel9A, from Thermobifida halotolerans YIM 90462(T) was cloned and expressed in Escherichia coli BL 21(DE). The 2895-bp full-length gene encodes a 964-residue polypeptide (Thcel9A) containing a catalytic domain belonging to glycosyl hydrolases (GH) family 9. Phylogenetic analysis indicated that Thcel9A is closely related to Cel9A of Thermobifida fusca YX. Thcel9A was purified from the culture supernatant by Ni2+-affinity chromatography and the purified enzyme exhibited optimal activity at 55 degrees C and pH 8.0. Substrate specificity assays showed that it not only had CMCase activity, but also hydrolase activity on microcrystalline cellulose and filter paper. These properties suggested that Thcel9A is a classical GH9 group A endoglucanase. (C) 2011 Elsevier Ltd. All rights reserved.
引用
收藏
页码：10143 / 10146
页数：4
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