Journal
CURRENT RESEARCH IN FOOD SCIENCE
Volume 6, Issue -, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.crfs.2022.100414
Keywords
Alginate lyase; Alkaline resistant; Oligosaccharides; Molecular docking
Categories
Funding
- Chongqing Science and Technology Bureau [cstc2020jcyj-msxmX0463]
- Guangxi Key Laboratory of Agricultural Resources Chemistry and Biotechnology Open Fund [2021KF04]
- Fundamental Research Funds for the Central Universities, Southwest University [SWU019034]
- Chongqing Key Laboratory of Speciality Food Co-Built by Sichuan and Chongqing, Postgraduate mentor team-building program of Southwest University [XYDS201905]
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This study successfully cloned and expressed the PL6 alginate lyase gene alyrm1 from Rubrivirga marina. The recombinant AlyRm1 showed good activity and stability at 30 degrees C and pH 10.0, and it could preferentially degrade into AOSs with DP 2-5 and monosaccharides, suggesting its potential applications.
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 degrees 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.
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