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Aromatic amino acids in the cellulose binding domain of Penicillium crustosum endoglucanase EGL1 differentially contribute to the cellulose affinity of the enzyme

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成果类型:
期刊论文
作者:
Yang, Jiang-Ke*;Xiong, Wei;Chen, Fang-Yuan;Xu, Li;Han, Zheng-Gang
通讯作者:
Yang, Jiang-Ke
作者机构:
[Xu, Li; Han, Zheng-Gang; Chen, Fang-Yuan; Yang, Jiang-Ke; Xiong, Wei] Wuhan Polytech Univ, Coll Biol & Pharmaceut Engn, Wuhan, Peoples R China.
通讯机构:
[Yang, Jiang-Ke] W
Wuhan Polytech Univ, Coll Biol & Pharmaceut Engn, Wuhan, Peoples R China.
语种:
英文
关键词:
Cellulose;Aromatic amino acids;Cell binding;Cell binding assay;Cellulases;Medical facies;Filter paper;Binding analysis
期刊:
PLOS ONE
ISSN:
1932-6203
年:
2017
卷:
12
期:
5
页码:
e0176444
基金类别:
Wuhan Science and Technology Project, China [2016020101010084]
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 cellulose binding domain (CBD) of cellulase binding to cellulosic materials is the initiation of a synergistic action on the enzymatic hydrolysis of the most abundant renewable biomass resources in nature. The binding of the CBD domain to cellulosic substrates generally relies on the interaction between the aromatic amino acids structurally located on the flat face of the CBD domain and the glucose rings of cellulose. In this study, we found the CBD domain of a newly cloned Penicillium crustosum endoglucanase EGL1, which was phylogenetically related to Aspergillus, Fusarium and Rhizopus, a...

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