| Abstract: | The glucose oxidase and catalase activities immobilized to the gamma-aminopropyltriethoxysilane derivative of nickel-impregnated silica alumina was controlled by several factors. The most important of these was enzyme concentration. In constructing the dual immobilized enzyme catalyst, competition between the two enzymes for available binding sites was observed. The order of addition of the various reactants during immobilization was also important. Higher glucose oxidase activities were immobilized when glutaraldehyde was added concurrently with enzyme, while maximal coupling of catalase occurred if glutaraldehyde was first added to react with the amino derivative of the silica alumina support, excess reagent washed away, and then the catalase added. Bovine serum albumin, which aids in the crosslinking of glucose oxidase, hindered the coupling of the enzyme to the support particles. |
