Computer-Aided Rational Design Strategy to Improve the Thermal Stability of Alginate Lyase AlyMc
文献类型： 外文期刊
作者： Cui, Yongyan 1 ; Yang, Min 2 ; Liu, Nan 2 ; Wang, Shanshan 2 ; Sun, Yong 2 ; Sun, Guohui 2 ; Mou, Haijin 3 ; Zhou, Deqing 2 ;
作者机构： 1.Ocean Univ Shanghai, Coll Food Sci, Shanghai 201306, Peoples R China
2.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Qingdao 266071, Shandong, Peoples R China
3.Ocean Univ China, Coll Food Sci & Engn, Qingdao 266003, Shandong, Peoples R China
关键词： alginate lyase; alginate oligosaccharides; rational design; thermal stability; moleculardynamicssimulation
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： 2024 年 72 卷 6 期
页码：
收录情况： SCI
摘要： Alginate lyase degrades alginate by the beta-elimination mechanism to produce unsaturated alginate oligosaccharides (UAOS), which have better bioactivities than saturated AOS. Enhancing the thermal stability of alginate lyases is crucial for their industrial applications. In this study, a feasible and efficient rational design strategy was proposed by combining the computer-aided Delta Delta G value calculation with the B-factor analysis. Two thermal stability-enhanced mutants, Q246V and K249V, were obtained by site-directed mutagenesis. Particularly, the t(1/2, 50 degrees C) for mutants Q246V and K249V was increased from 2.36 to 3.85 and 3.65 h, respectively. Remarkably, the specific activities of Q246V and K249V were enhanced to 2.41- and 2.96-fold that of alginate lyase AlyMc, respectively. Structural analysis and molecular dynamics simulations suggested that mutations enhanced the hydrogen bond networks and the overall rigidity of the molecular structure. Notably, mutant Q246V exhibited excellent thermal stability among the PL-7 alginate lyase family, especially considering the heightened enzymatic activity. Moreover, the rational design strategy used in this study can effectively improve the thermal stability of enzymes and has important significance in advancing applications of alginate lyase.
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