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Enzymes were immobilized on a magnetic support by a cocross-linking method with an inactive protein. Active porous particles obtained were used in a fluidized bed reactor. Outlet product concentration was measured as a function of a flow rate and inlet substrate concentration. No enzyme leakage was observed and a circular magnet surrounding the column was shown to be an efficient device for the retention of fine particles.

Summary Continuous hydrolysis of sucrose solutions by yeast invertase has been studied in a continuous stirred tank reactor (C.S.T.R.) limited by an ultrafiltration membrane capable of selectively retaining the enzyme. o 1. Initially, studies were made of the kinetics of batch sucrose hydrolysis and of invertase stability, under conditions applicable to a continuous process, in particular at high sucrose concentrations. 2. Ultrafiltration studies showed that various membranes retain invertase selectively and remain permeable to solutions of hydrolysed sucrose. The flux of the products of hydrolysis was found to be maximum when the concentration of the solution was close to 50 p. cent. 3. Studies of continuous hydrolysis without enzyme retention showed that the steady state ratio of sucrose hydrolysis may be predicted from the kinetics of the batch enzymatic reaction and from the substrate material balance in a C.S.T.R. 4. Studies of continuous hydrolysis with enzyme retention through ultrafiltration showed that invertase reutilisation for 5 days, at 50°C, does not lead to any detectable loss of enzyme activity. Under the conditions adopted, the ratio of sucrose hydrolysis remained constant, and close to 90 p. cent.