Alginate is a polysaccharide found within brown seaweeds and has been targeted as a carbon source for biofuel production. Alginate consists of α-L-guluronate (G) and β-D-mannuronate (M) linked in various patterns, which results in either a homo- or heteropolymeric structure. Alginate lyases are enzymes that degrade the linkage between G and M blocks and can have specificity to either polyG, polyM, or polyMG block degradation. The marine bacterium Vibrio splendidus 12B01 contains four putative alginate lyases which were investigated in this study. We identified, purified, and characterized the four PL7 alginates lyases. We found that these lyases have optimal activity between pH 7.5-8.5 and 20-25°C, consistent with use in a marine environment. Additionally, Ca2+ is necessary for optimal enzyme activity. The binding constant (Km) of the lyases toward alginate was found to be between 22 and 123 mM alginate and the maximum reaction rate (Vmax) was found to be between 0.13 and 0.83 µM s-1. The turnover numbers for the lyases was found to be between 0.60 and 7.1 s-1.

Over-expression and characterization of four alginate lyases from Vibrio splendidus 12B01

249th National Meeting (2015)

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