Immobilization of extracellular glucose oxidase from Penicillium funiculosum 46.1 on gels of aluminum or zinc hydroxides

Abstract

Different methods of immobilization of extracellular glucose oxidase (GO) from Penicillium funiculosum 46.1 on gels of aluminum or zinc hydroxides have been compared. GO from the culture liquid filtrate (CLF) associated with Zn(OH)2 but not Al(OH)3 gels. Preparation of samples of immobilized GO does not require isolation of the enzyme (CLF may be used). GO immobilized on Zn(OH)2 gels from CLF was 1.6 times more efficient in catalyzing D-glucose oxidation than the enzyme contained in the original culture liquid. Crosslinking of gel-adsorbed CLF proteins affected the properties of GO adversely and to a considerable extent. Various means of polymerization and immobilization of GO isolated from CLF have been studied. Optimum results were obtained when GO polymeric products were pre-synthesized in solution, followed by adsorption to Al(OH)3 but not Zn(OH)2 gels. The catalytic efficiency of GO immobilized on a Zn(OH)2 gel was significantly lower than that of the enzyme associated with Al(OH)3.