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Direct Influence of the Conserved Motif in PL7 Family Alginate Lyases on Enzyme Cold Adaptability

文献类型： 外文期刊

作者： He, Zhixiao 1 ; Meng, Shanshan 1 ; Xu, Yan 3 ; Zhong, Mingqi 1 ; Han, Xuefeng 1 ; Xie, Qingyi 5 ; Ding, Mo 1 ; Li, Jin 2 ; Hu, Zhong 1 ;

作者机构： 1.Shantou Univ, Coll Sci, Dept Biol, Shantou 515063, Peoples R China

2.Shantou Univ, Guangdong Prov Key Lab Marine Disaster Predict & P, Shantou 515063, Peoples R China

3.Heyuan Polytech, Dept Biol, Heyuan 517000, Peoples R China

4.Guangdong Prov Key Lab Marine Biol, Shantou 515063, Peoples R China

5.CATAS, Inst Trop Biosci & Biotechnol, Haikou Key Lab Res & Utilizat Trop Nat Prod, Haikou 571101, Peoples R China

6.China West Normal Univ, Coll Life Sci, Nanchong 637002, Peoples R China

关键词： alginate lyase; cold-adaptation; conservedmotif; mutation

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 7 期

页码：

收录情况： SCI

摘要： Alginate lyase, a vital component of polysaccharide lyases, is instrumental in the efficient degradation of alginate and the production of single oligosaccharides. Although numerous alginate lyases have been characterized, only a few display extreme cold adaptability in the range of 0-20 degrees C. In this study, we identified a novel cold-adapted alginate lyase, Aly423, from Tamlana laminarinivorans PT2-4 isolated from Sargassum. Phylogenetic classification, enzyme structure, and catalytic property analyses confirmed that Aly423 could be classified as a member of subfamily 5 of the PL7 family and exhibited significant cold adaptability at low temperatures. Further analysis of the secondary structure and homology modeling of several cold-adapted enzymes revealed two variable amino acid sites in the conserved amino acid motif (YFK*G*Y) of Aly423, which may affect the cold adaptation mechanism. Point mutation experiments demonstrated that mutant A304T significantly altered the temperature adaptation of Aly423, highlighting the critical role of this amino acid site in the cold-adaptation mechanism of the enzyme. In summary, we effectively enhanced the enzymatic activity of the PL7 alginate cold-adapted enzyme through a rational design using computational methods. This advancement is of significant importance for the efficient utilization of sodium alginate in the food, agricultural, and pharmaceutical industries under low-temperature conditions.

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