A bifunctional endolytic alginate lyase with two different lyase catalytic domains from Vibrio sp. H204

文献类型： 外文期刊

第一作者： Peng, Chune

作者： Peng, Chune;Xu, Wei;Wang, Xinkun;Dong, Xiaodan;Peng, Lizeng;Wang, Qingbin;Li, Fuchuan;Wang, Qingbin;Zheng, Qianqian;Liang, Xiaohui

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关键词： alginate lyase; bifunctional; catalytic domain; oligosaccharides; marine bacterium

期刊名称：FRONTIERS IN MICROBIOLOGY （ 影响因子：4.5； 五年影响因子：5.2 ）

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年卷期： 2024 年 15 卷

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收录情况： SCI

摘要： Alginate lyases can fully degrade alginate into various size-defined unsaturated oligosaccharide products by beta-elimination. Here, we identified the bifunctional endolytic alginate lyase Aly35 from the marine bacterium Vibrio sp. Strain H204. The enzyme Aly35 is classified into the polysaccharide lyase 7 superfamily and contains two alginate lyase catalytic domains. The relationship and function of the two lyase domains are not well known. Thus, the full-length recombinant enzyme and its truncated proteins Aly35-CD1 (catalytic domain 1), Aly35-CD2 (catalytic domain 2 domain) were constructed. The three enzymes showed similar biochemical characteristics and exhibited temperature and pH stability. Further research showed that Aly35 and Aly35-CD2 can efficiently degrade alginate, polymannuronate (PM) and polyguluronate (PG) into a series of unsaturated oligosaccharides, while Aly35-CD1 exhibits greater PM-degrading activity than that of Aly35-CD2 but can not degraded PG efficiently. The results suggest that the domain (Trp295-His582) is critical for PG-degrading activity, the domain has (Leu53-Lys286) higher PM-degrading activity, both catalytic domains together confer increased alginate (including M-blocks and G blocks)-degrading activity. The enzyme Aly35 and its truncations Aly35-CD1 and Aly35-CD2 will be useful tools for structural analyses and for preparing bioactive oligosaccharides, especially Aly35-CD1 can be used to prepare G unit-rich oligosaccharides from alginate.

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