Separation and Characterization of a Glycogenolytic Enzyme from a Glucose Oxidase Preparation Obtained from Aspergillus Niger

A glycogen cleaving factor was separated from commercial glucose oxidase by gel filtration on a combined column of Sephadex G 150 + G 25, and proved to be an enzyme. The enzyme was studied with purified glycogen and maltose as substrates and has been classified as an amyloglucosidase. Primary product of the reaction was found to consist exclusively of β-glucose. pH optimum was 4.6, the temperature optimum 50°. Several amines such as Tris, cetylpyridinium, and protamine inhibited the reaction at pH 7.0. Above separation procedure may be used for achievement of specificity for glucose determination by glucose oxidase method.