Enhanced Thermostability of an l -Rhamnose Isomerase for d -Allose Synthesis by Computation-Based Rational Redesign of Flexible Regions
文献类型： 外文期刊
作者： Wei, Meijing 1 ; Gao, Xin 1 ; Zhang, Wei 1 ; Li, Chao 1 ; Lu, Fuping 1 ; Guan, Lijun 2 ; Liu, Weidong 3 ; Wang, Jianwen 4 ; Wang, Fenghua 1 ; Qin, Hui-Min 1 ;
作者机构： 1.Tianjin Univ Sci & Technol, Tianjin Key Lab Ind Microbiol, Key Lab Ind Fermentat Microbiol, Minist Educ,Natl Engn Lab Ind Enzymes,Coll Biotech, Tianjin 300457, Peoples R China
2.Heilongjiang Acad Agr Sci, Inst Food Proc, Harbin 150086, Peoples R China
3.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Ind Enzymes Natl Engn Lab, Tianjin 300308, Peoples R China
4.Univ Tokyo, Grad Sch Agr & Life Sci, Tokyo 1138657, Japan
关键词：
期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：6.1； 五年影响因子：6.3 ）
ISSN： 0021-8561
年卷期： 2023 年 71 卷 42 期
页码：
收录情况： SCI
摘要： d-Allose is a low-calorie rare sugar with great application potential in the food and pharmaceutical industries. The production of d-allose has been accomplished using l-rhamnose isomerase (L-RI), but concomitantly increasing the enzyme's stability and activity remains challenging. Here, we rationally engineered an L-RI from Clostridium stercorarium to enhance its stability by comprehensive computation-aided redesign of its flexible regions, which were successively identified using molecular dynamics simulations. The resulting combinatorial mutant M2-4 exhibited a 5.7-fold increased half-life at 75 C-degrees while also exhibiting improved catalytic efficiency. Especially, by combining structure modeling and multiple sequence alignment, we identified an alpha 0 region that was universal in the L-RI family and likely acted as a "helix-breaker". Truncating this region is crucial for improving the thermostability of related enzymes. Our work provides a significantly stable biocatalyst with potential for the industrial production of d-allose.
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