Pilot plant production of glucose with glucoamylase immobilized to porous silica

Abstract

Glucoamylase was immobilized to porous silica and its kinetics and stability were observed with acid- and α-amylase-hydrolyzed dextrin as feed. The enzyme was found to be extremely stable in both laboratory and pilot plant operations. When the feed had been previously only lightly hydrolyzed, pore diffusion limitation caused appreciable decreases in glucose production rate. The severity of starch hydrolysis to dextrin markedly affected ultimate glucose yields. The diffusional gradients present in the carrier pores caused the immobilized enzyme to yield lower glucose concentrations than the free enzyme at similar feed conditions.