Arica, MYBaran, TDenizli, A2020-06-252020-06-251999closedAccess0021-89951097-4628https://doi.org/10.1002/(SICI)1097-4628(19990606)72:10<1367https://hdl.handle.net/20.500.12587/2822Baran, Erkan/0000-0002-0563-6943; Baran, Erkan/0000-0002-0563-6943;The activity of beta-galactosidase immobilized into a poly(2-hydroxyethyl methacrylate) (pHEMA) membrane increased from 1.5 to 10.8 U/g pHEMA upon increase in enzyme loading. The K-m values for the free and the entrapped enzyme were found to be 0.26 and 0.81 mM, respectively. The optimum reaction temperatures for the free and the entrapped beta-galactosidase were both found to be 50 degrees C. Similarly, the optimum reaction pH was 7.5 for both the free and the entrapped enzyme. The immobilized beta-galactosidase was characterized in a continuous system during lactose hydrolysis and the operational inactivation rate constant (k(iop)) of the entrapped enzyme was found to be 3.1 x 10(-5) min(-1). (C) 1999 John Wiley & Sons, Inc.eninfo:eu-repo/semantics/closedAccessbeta-galactosidaseenzyme immobilizationpHEMAlactose hydrolysisenzyme-membrane reactorArticle72101367137310.1002/(SICI)1097-4628(19990606)72:10<13672-s2.0-0032687636Q2WOS:000079480800017Q2