Journals / Türk Biyokimya Dergisi / 2013 / Cilt: 38 - Sayı: 4

Modelling of the β-D-glucose destruction kinetics by using glucose oxidase enzyme aggregates

Glukoz oksidaz enzim agregatları kullanılarak β-Dglukozun parçalanma kinetiğinin modellenmesi

Pages
483–493
Publication Date
2022-11-05
DOI
—
🏛️Bibliographic metadata and full text access for this article are provided via DergiPark.
DergiPark Record ↗
✨

AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

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

📌 3 Key Takeaways

🎯
Objective & Hypothesis: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.
📊
Key Findings & 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.
💡
Conclusion & Impact: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
🔬Design:Modeling & Simulation
📍Scope:Comprehensive Sample
⚙️Variables:Domain Parameters

Abstract

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

Özet

Amaç: Bu araştırmanın amacı glukoz oksidaz (GOD) enzimi ile hazırlanan agregat sistemlerinin glukozu indirgemesi sırasında oluşan tepkimenin kinetik değişmezlerinin zamana bağlı olarak ölçünen derişim değerlerini benzeştiren matematiksel model ile hesaplanması ve saptanan kinetik değerler ile deneysel verilerin karşılaştırılmasıdır. Gereçler ve Yöntemler: Araştırmanın ilk kısmında enzim uygun bir çöktürücü varlığında bifonksiyonel bir çapraz bağlayıcı ile muamele edilerek agregat oluşumu sağlanmış ve GOD agregatlarının aktiviteleri ?-D-glukozu glukonik asit'e ve H2O2'ye oksitleyen enzim miktarı olarak belirlenmiştir. Benzeşim için önerilen matematik model tek substrat-enzim katalizli tepkimeler için Michaelis ve Menten tarafından geliştirilmiş olan kinetik model çerçevesinde hızlı denge yaklaşımı varsayımını esas alır ve substrat derişimi, tepkime hızına bağlı olarak ifade edilen bir başlangıç değer problemidir. Bulgular: Benzeştirme eğrilerinden hesaplanan sonuçların deneysel ölçüm değerlerine yaklaştırılması ise matematiksel modelin içerdiği kinetik sabitlerin optimizasyonuna dayanmakta olup, çözümleme için Euler sayısal yöntemi uygulanmıştır ve optimizasyon için seçilen kinetik parametre değerleri ile çizilen simulasyon eğrilerinde substrat etkili Michaelis-Menten kinetik reaksiyon modeli ile yapılan optimizasyonlarda daha yüksek uyumluluk gösteren çok daha etkin sonuçlar alınmıştır. Yüksek glukoz derişimlerinin optimum değerleri veren kinetik parametre bölgesinin dışında kaldığı belirlenmiştir.Sonuçlar: GOD agregatlarının kinetik sabitlerinin hesaplamasında başlangıç substrat derişimi etkili Michaelis-Menten modelinin çözümlenmesi ile elde edilen değerlerin uyumunun Michaelis-Menten modeline göre daha yüksek olduğu belirlenmiştir

🔖

Cite This Article

AKPOLAT, O., AYHAN, H., AYHAN, F. (2022). Modelling of the β-D-glucose destruction kinetics by using glucose oxidase enzyme aggregates. Türk Biyokimya Dergisi, Cilt: 38 - Sayı: 4, 483–493. https://ajindex.com/articles/621288

📄 Full Text PDF Viewer

📄

PDF görüntüleyici hazırlanıyor...

References (12)

  1. Willie G, Alejandro C, Marta I, Toxicity and delivery methods for the linamarase/linamarin/glucose oxidase system, when used against human glioma tumors implanted in the brain of nude rats. Cancer Letters 2011; 313; 99–107
  2. Izquierdo M, Girald W, Gil J, Gargini R, Preclinical studies using the linamarase/linamarin/glucose oxidase gene therapy system against human glioma tumors in nude mice and rats. Universidad Autonoma de Madrid. 2011; Centro de Biologia Molecular Severo Ochoa, ASCO Annual Meeting
  3. Adler I, Bazerque PM, Crivelli MR, Aguas S, Quarracino C, Effect of a toothpaste containing amyloglucosidase and glucose oxidase on recurrent aphthous ulcers. Acta Odontol Latinoam 1993; 7; 33-38
  4. Li T, Yao Z, Ding L, Development of an amperometric biosensors based on glucose oxidase immobilized through silica SolGel film onto Prussian Blue Modified Electrode, Sens Act B Chem 2004; 101; 155-162
  5. Chu L Y, Liang Y J, Chen WM, Ju X J, Wang, HD, Preparation of glucose-sensitive microcapsules with a porous membrane and functional gates. Colloid Surf B 2004; 37: 9-15
  6. Jingjing L, Ruo Y, Yaqin C, Xin C, Fabrication of a novel glucose biosensor based on Pt nanoparticles-decorated iron oxidemultiwall carbon nanotubes magnetic composite. Journal of Molecular Catalysis B: Enzymatic 2010; 66; 8-14
  7. Zuchao M, Jianbin Z, Qinglin S, Xiaohui Z, In situ synthesis of thulium (III) hexacyanoferrate (II) nanoparticles and its application for glucose detection. Analytica Chimica Acta 2011; 689; 47-51
  8. Caramori SS, Fernandes KF, Covalent immobilization of horse radish peroxide onto poly (ethylene terephthalate)-poly (aniline) composite, Process Biochem 2004; 39; 883-888 [9] Fernandes KF, Lima CS, Lapes M, Collins CH, Properties of horse radish peroxide immobilised onto polyaniline, Process Biochem 2004; 39; 957-962
  9. Tyagi R, Batra R, Gupta N, Amorphus enzyme aggregate: Sta- bility toward heat and aqeous-organic cosolvent mixtures. Enzyme and Microbial Tech 1999; 24; 348-354
  10. İspirli Y, Ayhan H, Taşıyıcısız immobilizasyon yöntemiyle glukoz oksidaz (GOD) enzim agregatlarının ve kristallerinin sentezi ve karakterizasyonu, Muğla Üniversitesi Fen Bilimleri Enstitüsü, Yüksek Lisans Tezi, 2008
  11. Ayhan, F, İspirli Doğaç Y, Ayhan H, Cross-linked glucose oxidase aggregates: Synthesis and characterization, Hacettepe J. Biol Chem 2011; 39; 241-251
  12. Bailey JE, Ollis DF, Biochemical Engineering Fundamentals 1986; McGraw-Hill Int. Edition