Characterization of degradation patterns and enzymatic properties of a novel alkali-resistant alginate lyase AlyRm1 from Rubrivirga marina

Yuting Zheng; Yujie Wang; Meiling Dan; Yanping Li; Guohua Zhao; Damao Wang

doi:10.1016/j.crfs.2022.100414

Characterization of degradation patterns and enzymatic properties of a novel alkali-resistant alginate lyase AlyRm1 from Rubrivirga marina

Curr Res Food Sci. 2022 Dec 10:6:100414. doi: 10.1016/j.crfs.2022.100414. eCollection 2023.

Authors

Yuting Zheng¹, Yujie Wang², Meiling Dan¹, Yanping Li¹, Guohua Zhao¹, Damao Wang^{1

3}

Affiliations

¹ College of Food Science, Southwest University, Chongqing, 400715, China.
² Department of Chemistry, College of Resource and Environment, Baoshan University, Baoshan, 678000, PR China.
³ Guangxi Key Lab of Agricultural Resources Chemistry and Biotechnology, College of Chemistry and Food Science, Yulin Normal University, Yulin, Guangxi, 537000, PR China.

Abstract

Alginate lyase is essential for the production of alginate oligosaccharides (AOSs), which exhibit diverse bioactivities and have numerous applications in the food and pharmaceutical industries. The creation of recombinant alginate lyase by genetic engineering lays a crucial foundation for the commercialization of alginate lyase. This study cloned and expressed the polysaccharide lyase family 6 (PL6) alginate lyase gene alyrm1 from Rubrivirga marina.The optimum temperature and pH for recombinant AlyRm1 are 30 °C and 10.0, respectively. AlyRm1 shows good alkaline stability, for it remained over 80% of the enzyme activity after being incubated at pH 10.0 for 24 h AlyRm1 preferentially degrades PolyM into AOSs with degrees of polymerization (DP) 2-5 and monosaccharides as an endolytic bifunctional lyase. In addition, the analysis of degradation products toward oligosaccharides revealed that the minimal substrate of AlyRm1 is trisaccharide and clarified the degradation patterns.

Keywords: Alginate lyase; Alkaline resistant; Molecular docking; Oligosaccharides.