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

Shangyong Li; Linna Wang; Samil Jung; Beom Suk Lee; Ningning He; Myeong-Sok Lee

doi:10.3389/fmicb.2020.00316

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

Front Microbiol. 2020 Mar 10:11:316. doi: 10.3389/fmicb.2020.00316. eCollection 2020.

Authors

Shangyong Li^{1

2}, Linna Wang³, Samil Jung², Beom Suk Lee², Ningning He¹, Myeong-Sok Lee²

Affiliations

¹ School of Basic Medicine, Qingdao University, Qingdao, China.
² Molecular Cancer Biology Laboratory, Cellular Heterogeneity Research Center, Department of Biosystem, Sookmyung Women's University, Seoul, South Korea.
³ Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao, China.

Abstract

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 Arg²³¹ 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.

Keywords: Laminaria japonica; Vibrio sp. SY01; alginate monomers; oligoalginate lyase; substrate specificity.