| 초록 |
Alginate lyase can catalyze beta-elimination of the glycosidic bond in alginate, thus degrade alginate to unsaturated uronate. A novel oligoalginate lyase exhibiting an alginate-degradation activity through the formation of oligomers was functionally analyzed by site-directed mutagenesis. Homology modelling-inspired mutants were generated and characterized on the basis of the analysis of endolytic and exolytic lyase activity. The recombinant oligoalginate lyase was used as the biocatalyst for the conversion of alginate to its monosaccharide, unsaturated uronic aicd. Combination use of complementary alginate lyases could enhance the conversion efficiency. Acknowledgement: This work was supported by Ministry of Oceans and Fisheries, Republic of Korea. |
