Enzymic degradation of fucoidan by enzymes from the hepatopancreas of abalone, Haliotus species

Abstract

An α- l-fucosidase was partially purified from the hepatopancreas of abalone ( Haliotus sp.). This enzyme hydrolyzed the algal polymer fucoidan (α-1,2-fucoside 4-sulfate) but was incapable of degrading α- p-nitrophenyl- l-fucoside or blood group substance. The preparation was low in sulfatase activity toward fucoidan or fucose sulfate oligosaccharides, but did contain an active sulfatase for hydrolysis of p-nitrophenyl-sulfate. Our data indicate that this fucoidanase hydrolyzed fucoidan without desulfation to form oligosaccharides ranging from 10 to 2 fucose units plus the monosaccharide, fucose. Fucose could not be detected until late in the hydrolysis period, and sulfate release was not detectable during the first 4 hours of fucoidanase action. Properties of abalone fucoidanase such as pH, heat stability, pH profile, and enzyme and substrate concentration are reported.