期刊
FRONTIERS IN MICROBIOLOGY
卷 11, 期 -, 页码 -出版社
FRONTIERS MEDIA SA
DOI: 10.3389/fmicb.2020.00316
关键词
oligoalginate lyase; substrate specificity; alginate monomers; Laminaria japonica; Vibrio sp; SY01
类别
资金
- National Natural Science Foundation of China (NSFC) [31900031]
- National Research Foundation of Korea (NRF) [NRF-2016R1A5A1011974, NRF-2017R1D1A103033528, NRF2019R1I1A1A01052833]
- Korea Research Fellowship Program [2019H1D3A1A01102881]
- Shandong Provincial Natural Science Foundation [ZR2019BD027]
- Open Research Fund Program of Shandong Provincial Key Laboratory of Glycoscience and Glycotechnology (Ocean University of China) [KLGGOUC201703]
- Key Lab of Marine Bioactive Substance and Modern Analytical Technique (SOA) [MBSMAT-2019-02]
Oligoalginate lyases catalyze the degradation of alginate polymers and oligomers into monomers, a prerequisite for biotechnological utilizing alginate. In this study, we report the cloning, expression and biochemical characterization of a new polysaccharide lyase (PL) family 17 oligoalginate lyase, OalV17, from the marine bacterium Vibrio sp. SY01. The recombinant OalV17 showed metal ion independent and detergent resistant properties. Furthermore, OalV17 is an exo-type enzyme that yields alginate monomers as the main product and recognizes alginate disaccharides as the minimal substrate. Site-directed mutagenesis followed by kinetic analysis indicates that the residue Arg(231) plays a key role in substrate specificity. Furthermore, a rapid and efficient alginate monomer-producing method was developed directly from Laminaria japonica. These results suggest that OalV17 is a potential candidate for saccharification of alginate.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据