Yeast alcohol dehydrogenase immobilized on sepharose derivatives by non-specific adsorption followed by cross-linkage with glutaraldehyde

Abstract

1. 1. Yeast alcohol dehydrogenase was adsorbed on acetyl and phenylglycyl derivatives of agarose. Glutaraldehyde cross-linkage was required to eliminate enzyme desorption which occurred in the presence of NAD +. 2. 2. The immobilized enzyme was less stable than the soluble enzyme at 20°C. 3. 3. Albumin co-immobilized with the enzyme increased its stability above that of soluble enzyme.