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ORIGINAL RESEARCH article

Front. Microbiol.
Sec. Microbiotechnology
Volume 15 - 2024 | doi: 10.3389/fmicb.2024.1509599

A Bifunctional Endolytic Alginate Lyase with Two Different Lyase Catalytic Domains From Vibrio sp. H204

Provisionally accepted
Chune Peng Chune Peng 1Wang Qingbin Wang Qingbin 2Wei Xu Wei Xu 1*Xinkun Wang Xinkun Wang 1Qianqian Zheng Qianqian Zheng 3*Xiaohui Liang Xiaohui Liang 4*Xiaodan Dong Xiaodan Dong 1*Fuchuan Li Fuchuan Li 2*Lizeng Peng Lizeng Peng 1*
  • 1 Shandong Academy of Agricultural Sciences, Jinan, China
  • 2 Shandong University, Jinan, Shandong Province, China
  • 3 Xinxiang Medical University, Xinxiang, Henan Province, China
  • 4 Qilu Normal University, Jinan, Shandong, China

The final, formatted version of the article will be published soon.

    Alginate lyases can fully degrade alginate into various size-defined unsaturated oligosaccharide products by β-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 (Trp 295 -His 582 ) is critical for PG-degrading activity, the domain has (Leu 53 -Lys 286 ) 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.

    Keywords: alginate lyase, Bifunctional, Catalytic Domain, Oligosaccharides, marine bacterium

    Received: 11 Oct 2024; Accepted: 04 Dec 2024.

    Copyright: © 2024 Peng, Qingbin, Xu, Wang, Zheng, Liang, Dong, Li and Peng. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

    * Correspondence:
    Wei Xu, Shandong Academy of Agricultural Sciences, Jinan, China
    Qianqian Zheng, Xinxiang Medical University, Xinxiang, 453003, Henan Province, China
    Xiaohui Liang, Qilu Normal University, Jinan, 250013, Shandong, China
    Xiaodan Dong, Shandong Academy of Agricultural Sciences, Jinan, China
    Fuchuan Li, Shandong University, Jinan, 250100, Shandong Province, China
    Lizeng Peng, Shandong Academy of Agricultural Sciences, Jinan, China

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