ENHANCED HYDROLYSIS OF SOLUBLE CELLULOSIC SUBSTRATES BY A METALLOCELLULASE WITH VERATRYL ALCOHOL-OXIDASE ACTIVITY

A cellulase enzyme fraction was separated from Trichoderma reesei Pulp zyme HA(TM), and its characteristics suggested that it was mainly comp osed of cellobiohydrolase II (CBH II). The covalent attachment of pent aammineruthenium(III) to this enzyme resulted in threefold and fourfol d enhancements of its hydrolytic activity on carboxymethyl cellulose ( CMC) and barley beta-glucan, respectively, as well as endowing it with veratryl alcohol-oxidase activity. Enhancement of hydrolysis was not affected by addition of tartrate or hydrogen peroxide to the reaction mixture. Both native and pentaammineruthenium-modified enzymes had neg ligible activity on cellobiose and p-nitrophenyl beta-cellobioside (PN PC).