CATALYTIC CONDITIONS OF FUCOIDAN DEGRADING ENZYMES FROM VASTICARDIUM FLAVUM

Abstract

The fucoidanase from the digestive glands of the marine shell Vasticardium flavum was studied. The fucoidanase catalysed the hydrolysis of 1→3-L-fucan from sea cucumbers Stichopus variegatus , Holothuria spinifera , did not catalyze the hydrolysis of fucoidan from F. evanescens and F. vesiculosus containing alternating α-1→4 and α-1→3 glycoside bonds. This enzyme also did not catalyze the hydrolysis of fucoidan from U . p innatifida , S . m cclurei , which belong to the galactofucan group. Optima of pH and time incubation were at 3-4 and 24 hours, respectively. The enzyme activity was significantly increased in the presence of the Ca 2+ , Ba 2+ , Co 2+ and Mg 2+ cations, but the Cu 2+ , Sn 2+ , Fe 2+ and Al 3+ cations partially inactivated the enzyme. The enzyme was completely inactivated after 5 min of incubation at 65° C.