Alkali Protease and Alcohol Dehydrogenase Immobilized to Weakly Basic Anion Exchange Resins Using 2-Carboxymethylamino-4, 6-dichloro-s-triazine

Abstract

Alkali protease partially purified from a strain of Bacillus subtilis and yeast alcohol dehydrogenase were immobilized to weakly basic anion exchange resins using a bifunctional reagent, 2-carboxymethylamino-4, 6-dichloro-s-triazine.
Properties of these immobilized enzymes were studied both in batchwise operation and in packed bed reactor systems.