Extra carbohydrate binding module contributes to the processivity and catalytic activity of a non-modular hydrolase family 5 endoglucanase from Fomitiporia mediterranea MF3/22
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- 作者：Ronghua Pan1 ; Yimei Hu1 ; Liangkun Long ; Jing Wang ; Shaojun Ding ; dshaojun@hotmail.com" class="auth_mail" title="E-mail the corresponding author
- 关键词：Family 5 glycoside hydrolase ; Endoglucanase ; Carbohydrate-binding modules ; Processivity ; Fomitiporia mediterranea
- 刊名：Enzyme and Microbial Technology
- 出版年：2016
- 出版时间：September 2016
- 年：2016
- 卷：91
- 期：Complete
- 页码：42-51
- 全文大小：1593 K
文摘
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Extra CBM1 significantly improved FmEG processivity and activity on insoluble celluloses.
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Extra CBM1 also caused an alteration of cleavage pattern on insoluble celluloses.
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Improvements in processivity and activity may arise from CBM1 binding affinity.
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Deleting N-terminal extension led to reduction in thermostability but not activity.
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N-terminal extension might play a function as flexible connector between two domains.