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The catalytic domain of Penicillium crustosum endoglucanase EGL1 has cellulose-binding capacity and cellulolytic activity

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成果类型:
期刊论文
作者:
Xiong, Wei;Yang, Jiang-Ke*;Chen, Fang-yuan;Han, Zheng-gang
通讯作者:
Yang, Jiang-Ke
作者机构:
[Han, Zheng-gang; Chen, Fang-yuan; Yang, Jiang-Ke; Xiong, Wei] Wuhan Polytech Univ, Coll Biol & Pharmaceut Engn, Wuhan 430023, Peoples R China.
通讯机构:
[Yang, Jiang-Ke] W
Wuhan Polytech Univ, Coll Biol & Pharmaceut Engn, Wuhan 430023, Peoples R China.
语种:
英文
关键词:
Catalytic domain;Cellulase binding assay;Endoglucanase;Glycine scanning mutagenesis;Hydrophobic core
期刊:
Enzyme and Microbial Technology
ISSN:
0141-0229
年:
2017
卷:
97
页码:
71-81
机构署名:
本校为第一且通讯机构
院系归属:
生命科学与技术学院
摘要:
The cellulase-mediated degradation of cellulosic materials, which is initiated by endoglucanases by the random cleavage of the glycosidic bonds between glucose units to break long cellulose molecules into shorter ones, represents a major carbon flow in the global carbon cycle. The structure of a typical endoglucanase contains a classical (α/β)8 barrel fold catalytic domain, a linker region and a cellulose-binding domain. In this study, we found that both the full-length enzyme and the catalytic domain of endoglucanase EGL1 cloned from Penicillium crustosum strain 601 have CMCase and...

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