Rational Design of Alginate Lyase AlgL3199 for Thermal Stability and Specific Activity Enhancement
文献类型： 外文期刊
作者： Chen, Zhifang 1 ; Hao, Jianhua 1 ; Guo, Yingying 1 ; Zhu, Tiantian 1 ; Sun, Jingjing 1 ; Wang, Wei 1 ; Jiang, Chengcheng 1 ; Wang, Haiying 1 ;
作者机构： 1.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Qingdao Marine Sci & Technol Ctr, Lab Marine Drugs & Byproducts, Qingdao 266071, Peoples R China
2.Dalian Ocean Univ, Coll Fisheries & Life Sci, Dalian 116000, Peoples R China
3.Jiangsu Collaborat Innovat Ctr Exploitat & Utiliza, Lianyungang 222005, Peoples R China
关键词： alginate lyase; thermal stability; site-directedmutagenesis; molecular docking
期刊名称：JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY （ 影响因子：6.2； 五年影响因子：6.4 ）
ISSN： 0021-8561
年卷期： 2025 年 73 卷 24 期
页码：
收录情况： SCI
摘要： Alginate lyase is a critical enzyme that catalyzes alginate degradation; however, its low thermal stability limits its industrial application. This study proposes a feasible and efficient rational design strategy based on computer-aided structure analysis and energy calculation for generating thermally stable alginate lyases. Through site-directed mutagenesis, we obtained four thermal stability-enhanced mutants, namely K81A, D148P, K81A/D148P, and K81A/D148P/V163T, which exhibited 5.18-, 4.66-, 3.22-, and 3.53-fold longer half-lives, respectively, than AlgL3199 at 60 degrees C. Additionally, K81A, D148P, K81A/D148P, and K81A/D148P/V163T showed 28.59%, 42.56%, 34.71%, and 12.15% increased specific activities, respectively, compared to AlgL3199. Structural and hydrophobicity analyses revealed that the obtained mutants showed enhanced hydrogen-bond networks, structural rigidity, and hydrophobic interactions. Among the four mutants, K81A exhibited the most pronounced structural modification. The findings of this study indicate that the proposed rational design strategy provides a valuable method for improving both thermal stability and specific activity of alginate lyases.
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