Biochemical Characterization of a New Oligoalginate Lyase and Its Biotechnological Application in Laminaria japonica Degradation

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,...

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Bibliographic Details
Published in:Frontiers in microbiology 2020-03, Vol.11, p.316-316
Main Authors: Li, Shangyong, Wang, Linna, Jung, Samil, Lee, Beom Suk, He, Ningning, Lee, Myeong-Sok
Format: Article
Language:English
Subjects:
alginate monomers
Laminaria japonica
Microbiology
oligoalginate lyase
substrate specificity
Vibrio sp. SY01
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Summary: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 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 plays a key role in substrate specificity. Furthermore, a rapid and efficient alginate monomer-producing method was developed directly from . These results suggest that OalV17 is a potential candidate for saccharification of alginate.
ISSN:1664-302X
1664-302X
DOI:10.3389/fmicb.2020.00316