Catalytic conditions offucoidanase from vasticardium flavum

Abstract

Fucoidanases are widely distributed in both marine microorganisms and marine invertebrates, however the data on the properties of this enzyme are scarce. In the present study, we isolated the fucoidanase from gastrointcstinal tracts ofthe marine shell Vasticardium flavum and determined its enzymatic properties. The fucoidanase cleaved 1→3-α-L-fucan link of fucoidan extracted from sea cucumbers Stichopus variegatus, Holothuria spinifera, did not cleave fucoidans from F. evanescens and F. vesiculosus including rotational α-1→4 and α-1→3 glycoside chains. This enzyme did neither catalyzethe hydrolysis of fucoidans from U.pinnatifida, S. mcclurei, which belongs to the galactofucan group. The fucoidanase showed the best activity at pH 3-4 and 24 hours of incubation. The enzyme activity was enhanced by Ca²⁺, Ba²⁺, CO2- and Mg²ˉ cations, but it was inhibited by the Cu²⁺, Sn²⁺, Fe₂- and Al₃- cations. After incubation at 650C for 5 min, the enzyme activity was completely disappeared.