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dc.contributor.authorAkpolat, Oguz
dc.contributor.authorAyhan, Fatma
dc.contributor.authorAyhan, Hakan
dc.date.accessioned2020-11-20T16:20:25Z
dc.date.available2020-11-20T16:20:25Z
dc.date.issued2013
dc.identifier.issn0250-4685
dc.identifier.issn1303-829X
dc.identifier.urihttps://doi.org/10.5505/tjb.2013.85866
dc.identifier.urihttps://hdl.handle.net/20.500.12809/3900
dc.descriptionWOS: 000329577500017en_US
dc.description.abstractAim: The object of the study is calculation of the kinetic constants for the reduction reaction of glucose by glucose oxidase (GOD) aggregate systems by the mathematical model simulated the concentrations of the reactants or products and comparision of the calculated kinetic values with the experimental data. Methods: In the first part of the study, aggregate formation was made by the treatment with a bi-functional cross-linker in the presence of an appropriate precipitator and the activity of GOD enzyme aggregates was estimated by enzyme amount which oxidase beta-D-glucose to gluconic acid and H2O2. The mathematical model suggested for simulation depends on the rapid equilibrium approach of the kinetic model proposed by Michaelis and Menten for single substrate-enzyme catalyzed reactions and the substrate concentration is an initial value problem defined in terms of the reaction rate. Results: The convergence of calculated results from simulated curves to experimentally measured values based on the optimization of kinetic constants present in the mathematical model and Euler numerical method was applied in the solution of the problem. More effective results with higher correlations were obtained for the optimizations achieved by the Substrate affective Michaelis and Menten model when the simulation curves drawn for the selected kinetic parameter values. It was determined that high glucose concentrations are out of the optimum kinetic parameters range. Conclusions: In the calculation of kinetic constants of GOD aggregates, the consistency of the values obtained from the analysis of initial substrate concentration effective Michaelis-Menten model was higher than the Michaelis-Menten model.en_US
dc.item-language.isoturen_US
dc.publisherTurkish Biochem Socen_US
dc.item-rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectGlucose Oxidaseen_US
dc.subjectEnzyme Aggregatesen_US
dc.subjectEnzyme Kineticsen_US
dc.subjectMathematical Modelen_US
dc.subjectSimulationen_US
dc.titleModelling of the beta-D-glucose destruction kinetics by using glucose oxidase enzyme aggregatesen_US
dc.item-typearticleen_US
dc.contributor.departmenten_US
dc.contributor.departmentTemp[Akpolat, Oguz; Ayhan, Fatma; Ayhan, Hakan] Mugla Sitki Kocman Univ, Kimya Bolumu, Biyokimya & Biyomalzemeler Arastirma Lab, Mugla, Turkeyen_US
dc.identifier.doi10.5505/tjb.2013.85866
dc.identifier.volume38en_US
dc.identifier.issue4en_US
dc.identifier.startpage483en_US
dc.identifier.endpage493en_US
dc.relation.journalTurkish Journal of Biochemistry-Turk Biyokimya Dergisien_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US


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