الفهرس 
Purification and characterization of alginate lyase extracted from marine bacteria
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Abstract
Alginate lyase-producing bacteria were isolated from brown algae collected from the Red Sea, Egypt. The isolated strains were subjected to molecular characterization and phylogenetic analysis. The alginate lyase gene from Cobetia litoralis P65a was cloned and over-expressed in Escherichia coli as a soluble and functional protein. The recombinant enzyme (Alg-P65a) was purified to homogeneity by Ni-NTA affinity chromatography yielding a single distinct band with an apparent molecular mass of 36 kDa on SDS-PAGE.The optimum temperature and pH values for Alg-P65a were 45 {u00B0}C and 8, respectively. Alg-P65a has an ability to hydrolyze sodium alginate, polymannuronic acid (polyM), and poly-guluronic acid (polyG) indicating that it is a bifunctional alginate lyase. The purified enzyme exhibited antibiofilm activity against Pseudomonas aeruginosa, in vitro. Furthermore, alginate-hydrolysates produced by Alg-P65a showed promising antioxidant properties.These results suggest the great potential of alginate lyase from C. litoralis P65a to be employed in biotechnological fields