Enzymatic Oxidation and Separation of Various Saccharides with Immobilized Glucose Oxidase.

Mislovičová, Danica; Pätoprstý, Vladimír; Vikartovská, Alica

Glucose oxidase from Aspergillus niger, the specific enzyme for β- d-glucose oxidation, can also oxidize other related saccharides at very slow or negligible rates. The present study aimed to compare the kinetics of d-glucose oxidation using immobilized glucose oxidase on bead cellulose for the oxidation of related saccharides using the same biocatalyst. The significant differences were observed between the reaction rates for d-glucose and other saccharides examined. As a result, k/ K ratio for d-glucose was determined to be 42 times higher than d-mannose, 61.6 times higher than d-galactose, 279 times higher than d-xylose, and 254 times higher than for d-fructose and d-cellobiose. On the basis of these differences, the ability of immobilized glucose oxidase to remove d-glucose from d-cellobiose, d-glucose from d-xylose, and d-xylose from d-lyxose was examined. Immobilized catalase on Eupergit and mixed with immobilized glucose oxidase on bead cellulose or co-immobilized with glucose oxidase on bead cellulose was used for elimination of hydrogen peroxide from the reaction mixture. The accelerated elimination of d-glucose and d-xylose in the presence of co-immobilized catalase was observed. The co-immobilized glucose oxidase and catalase were able to decrease d-glucose or d-xylose content to 0–0.005% of their initial concentrations, while a minimum decrease of low oxidized saccharides d-xylose, d-cellobiose, and d-lyxose, respectively, was observed.

ASPERGILLUS niger; SACCHARIDES; GLUCOSE; ENZYMES; OXIDATION; BIOENGINEERING

Applied Biochemistry & Biotechnology, 2010, Vol 162, Issue 6, p1669

0273-2289

Academic Journal

10.1007/s12010-010-8948-6