Molecular characterization of the thermostability and carbohydrate-binding module from a newly identified GH118 family agarase, AgaXa

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• 作者：Yi-Rui Wu¹ ; Zheng-Rong Zhou¹ ; Min Zhao ; Bokun Lin ; Mingqi Zhong ; Zhong Hu ; ^{hzh@stu.edu.cn}
• 关键词：WT ; wild-type ; CD ; circular dichroism ; PCR ; polymerase chain reaction ; GH ; glycoside hydrolase ; CBM ; carbohydrate-binding module ; CM ; catalytic module ; DNS ; 3 ; 5-dinitrosalicylic acid ; SDS-PAGE ; sodium dodecyl sulphate-polyacrylamide gel electrophoresis ; BSA ; bovine serum albumin
• 刊名：Process Biochemistry
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：52
• 期：Complete
• 页码：192-199
• 全文大小：1590 K
• 卷排序：52

文摘

AgaXa mutants were generated via the random and site-directed mutagenesis. The crucial amino acids related to thermostability and enzymatic activity were demonstrated. The location of carbohydrate-binding site was identified from the truncated mutants of AgaXa. Molecular mechanism of this new agarase member in GH118 family was firstly investigated.