Bayramoglu, GAkgol, SBulut, ADenizli, AArica, MY2020-06-252020-06-252003closedAccess1369-703Xhttps://doi.org/10.1016/S1369-703X(02)00170-5https://hdl.handle.net/20.500.12587/3134Akgol, Sinan/0000-0002-8528-1854; AKGOL, Sinan/0000-0003-2836-7181Invertase was covalently immobilised on the poly(hydroxyethyl methacrylate-co-glycidyl methacrylate) (poly(HEMA-GMA)) film. The invertase immobilisation capacity of the films was increased as the GMA ratio increased in the film structure. The immobilised invertase on the poly(HEMA-GMA-3) composition exhibited an activity of 32.7 U cm(-2) film. The optimum temperature of the immobilised invertase increased by 5 degreesC, and the optimal pH values for the free and the immobilised enzymes were determined as 5.0. The retained activity of the immobilised invertase was between 53 and 85%. Kinetic parameters were determined for immobilised invertase as well as for the free enzyme. The values of the Michael's constant K-m of invertase were significantly larger, ca. 2.7 times upon immobilisation, indicating decreased affinity by the enzyme for its substrate, whereas V-max was smaller for immobilised invertase. Activity of the immobilised invertase was quite stable with respect to free counterpart. After 168 h reaction, only 8% of immobilised invertase activity was lost. The operational inactivation rate constant (k(opi)) of the immobilised invertase at 35 degreesC with 200 mM sucrose was 8.23 x 10(-6) min(-1). (C) 2002 Elsevier Science B.V. All rights reserved.eninfo:eu-repo/semantics/closedAccessimmobilisationimmobilised enzymesinvertasesucrose hydrolysiskinetic parametersenzyme bioreactorsfilmArticle14211712610.1016/S1369-703X(02)00170-52-s2.0-0345352783Q2WOS:000182361900006Q1