Rational design for the stability improvement of Armillariella tabescens β-mannanase MAN47 based on N-glycosylation modification

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• 作者：Weixiong Hu^a ; ¹ ; Xiaoyun Liu^a ; ¹ ; Yufeng Li^a ; Daling Liu^a ; ^c ; Zhihe Kuang^b ; Chuiwen Qian^b ; Dongsheng Yao^a ; ^b ; ^{tdsyao@jnu.edu.cn}
• 关键词：N-glycosylation ; Posttranslational modification ; Homology modeling ; Enzyme stability ; Molecular dynamics simulations
• 刊名：Enzyme and Microbial Technology
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：97
• 期：Complete
• 页码：82-89
• 全文大小：1811 K
• 卷排序：97

文摘

We put forward a rational strategy to improve several characters of β-mannanase. N-glycosylation sites were selected in the loop area; carbohydrate chain was introduced without affecting the enzyme activity. Results showed that the thermal stability, pH stability, protease-resistance of the mutants with glycosylation were improved.