Modeling of The β-D-Glucose Destruction Kinetics by Using Glucose Oxidase Enzyme Aggregates

Aim: 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 b-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 MichaelisMenten model was higher than the Michaelis-Menten model.

[1]  M. Izquierdo,et al.  Toxicity and delivery methods for the linamarase/linamarin/glucose oxidase system, when used against human glioma tumors implanted in the brain of nude rats. , 2011, Cancer letters.

[2]  Hüseyin Ayhan,et al.  Cross- Linked Glucose Oxidase Aggregates: Synthesis and Characterization Çapraz Bağli Glukoz Oksidaz Agregatlari: Sentez ve Karakterizasyonu , 2011 .

[3]  M. Izquierdo,et al.  Preclinical studies using the linamarase/linamarin/glucose oxidase gene therapy system against human glioma tumors in nude mice and rats. , 2011, Journal of clinical oncology : official journal of the American Society of Clinical Oncology.

[4]  Qinglin Sheng,et al.  In situ synthesis of thulium(III) hexacyanoferrate(II) nanoparticles and its application for glucose detection. , 2011, Analytica chimica acta.

[5]  Y. Chai,et al.  Fabrication of a novel glucose biosensor based on Pt nanoparticles-decorated iron oxide-multiwall carbon nanotubes magnetic composite , 2010 .

[6]  Fei Liao,et al.  The comparison of the estimation of enzyme kinetic parameters by fitting reaction curve to the integrated Michaelis-Menten rate equations of different predictor variables. , 2005, Journal of biochemical and biophysical methods.

[7]  Liang-Yin Chu,et al.  Preparation of glucose-sensitive microcapsules with a porous membrane and functional gates. , 2004, Colloids and surfaces. B, Biointerfaces.

[8]  Liang Ding,et al.  Development of an amperometric biosensor based on glucose oxidase immobilized through silica sol–gel film onto Prussian Blue modified electrode , 2004 .

[9]  C. Collins,et al.  Properties of horseradish peroxidase immobilised onto polyaniline , 2004 .

[10]  K. Fernandes,et al.  Covalent immobilisation of horseradish peroxidase onto poly(ethylene terephthalate)–poly(aniline) composite , 2004 .

[11]  Kao-cong Tian,et al.  Kinetic substrate quantification by fitting the enzyme reaction curve to the integrated Michaelis–Menten equation , 2003, Analytical and bioanalytical chemistry.

[12]  F. Liao,et al.  Assay of serum arylesterase activity by fitting to the reaction curve with an integrated rate equation. , 2001, Clinica chimica acta; international journal of clinical chemistry.

[13]  M. Auer,et al.  Enzyme inhibition assays using fluorescence correlation spectroscopy: a new algorithm for the derivation of kcat/KM and Ki values at substrate concentrations much lower than the Michaelis constant. , 2000, Biochemistry.

[14]  K. Kahn,et al.  Kinetic mechanism and cofactor content of soybean root nodule urate oxidase. , 1997, Biochemistry.

[15]  H. Pardue,et al.  Kinetic method having a linear range for substrate concentrations that exceed Michaelis-Menten constants. , 1982, Clinical chemistry.

[16]  Liu Jia-chu Measurement of mouse liver glutathione S-transferase activity by the integrated method , 2003 .

[17]  S. Aguas,et al.  Effect of a toothpaste containing amyloglucosidase and glucose oxidase on recurrent aphthous ulcers. , 1993, Acta odontologica latinoamericana : AOL.

[18]  David F. Ollis,et al.  Biochemical Engineering Fundamentals , 1976 .