ENZYMATIC DEGRADATION OF FUCOIDAN BY FUCOIDANASE FROM THE HEPATOPANCREAS OF PATINOPECTEN-YESSOENSIS

A fucoidanase from the hepatopancreas of Patinopecten yessoensis was purified by ammonium sulfate precipitation, anion exchange chromatography, isoelectric focusing, and gel chromatography. The purified enzyme gave a single band on polyacrylamide gel electrophoresis. The fucoidanase was pratically free from alpha-L-fucosidase and arylsulfatase activities. The molecular weight of the enzyme was estimated to be 85,000 by gel filtration on TSKgel G3000SW and 84,000 by SDS (sodium dodecyl sulfate) polyacrylamide gel electrophoresis. The enzyme hydrolyzed fucoidan to produce sulfated oligosaccharides as the reaction products.