Department of Chemical and Petrochemical Engineering,Sharif University of Technology
Abstract
In this paper, immobilization of penicillin G acylase onto non-porous ultrafine silica particles has been studied. The amount of penicillin G acylase immobilized was increased by increasing the free enzyme concentration and, at 0.45 mg/ml concentration of the free enzyme, 80% of the enzyme was immobilized. The optimum pH for immobilization was found to be 7.0, close to the pI of the enzyme. Although immobilization of the enzyme on ultrafine silica particles with and without glutaraldehyde showed almost the same activities, the enzyme immobilized with glutaraldehyde retained its initial activity much longer during 40 cycle-repeated batches with a half life of 163.2 h.
