Abstract
Commercially available glucose-oxidase preparations contain also maltase and isomaltase activity. Attempts to separate glucose oxidase from these contaminating glycosidase activities were unsuccessful. The presence of 0.5M-tris buffer, pH 7.0, selectively inhibits these glycosidase activities, without interfering with the production of colour with free glucose by a glucose-oxidase reagent containing o-dianisidine as a chromogen. A method for the determination of intestinal maltase and isomaltase activities based upon a tris[long dash] glucose-oxidase reagent is described. The tris[long dash]glucose-oxidase reagent may be used as a general reagent for the determination of glucose liberated by glycosidases from di- and oligo-saccharides. It is not suitable for the assay of the hydrolysis of phenylglucosides.