Abstract
Enzymatic hydrolysis of lactose by β-galactosidase (Lactozym) has been studied in a jacketed stirred-tank reactor (JSTR) and in a recirculation hollow-fibre bioreactor (RHFB). The hollow-fibre module was manufactured with modified cellulose-acetate membrane (Cuprophan). The variables tested were: temperature (25–40°C), lactose concentration (0.0278– 0.208 M ) and enzyme concentration (0.100– 4.51 g l −1 ). Within the experimental range analysed, the conversions in the RHFB, were lower than in the JSTR. A kinetic model is proposed for enzymatic hydrolysis of lactose in the RHFB, which considers competitive inhibition by the product (galactose) and reversible adsorption of the enzyme–galactose complex on the hollow-fibre membrane. The adsorption enthalpy of the enzyme–galactose complex onto the membrane was determined as being 77 5 kJ mol −1 .
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