Glucose oxidase immobilization on a novel cellulose acetate–polymethylmethacrylate membrane

• Published in: Journal of biotechnology Vol. 121; no. 3; pp. 351 - 360
• Main Authors: Rauf, S., Ihsan, A., Akhtar, K., Ghauri, M.A., Rahman, M., Anwar, M.A., Khalid, A.M.
• Format: Journal Article
• Language: English
• Published: Lausanne Elsevier B.V 10.02.2006; Amsterdam Elsevier; New York, NY
• Subjects: Biological and medical sciences; Biosensing Techniques; Biosensor; Biotechnology; Cellulose - analogs & derivatives; Cellulose - chemistry; Cellulose - ultrastructure; Cellulose acetate–polymethylmethacrylate (CA–PMMA); Enzyme Stability; Enzymes, Immobilized - metabolism; Enzymes, Immobilized - ultrastructure; FT-IR; Fundamental and applied biological sciences. Psychology; Glucose oxidase (GOD); Glucose Oxidase - analysis; Glucose Oxidase - metabolism; Glucose Oxidase - ultrastructure; Hot Temperature; Hydrogen-Ion Concentration; Immobilization; Kinetics; Membrane; Membranes, Artificial; Microscopy, Electron, Scanning; Polymethyl Methacrylate - chemistry; SEM; Spectroscopy, Fourier Transform Infrared; Urea - pharmacology; Glucose oxidase (GOD); Biosensor; Immobilization; Membrane; FT-IR; SEM; Cellulose acetate–polymethylmethacrylate (CA–PMMA); Glucose oxidase; Scanning electron microscopy; Fourier transformation; Enzyme; Infrared spectrometry; Oxidoreductases; Cellulose acetate; Cellulose acetate-polymethylmethacrylate (CA-PMMA)
• ISSN: 0168-1656; 1873-4863
• DOI: 10.1016/j.jbiotec.2005.08.019

Glucose oxidase (GOD) was immobilized on cellulose acetate–polymethylmethacrylate (CA–PMMA) membrane. The immobilized GOD showed better performance as compared to the free enzyme in terms of thermal stability retaining 46% of the original activity at 70 °C where the original activity corresponded to that obtained at 20 °C. FT-IR and SEM were employed to study the membrane morphology and structure after treatment at 70 °C. The pH profile of the immobilized and the free enzyme was found to be similar. A 2.4-fold increase in K m value was observed after immobilization whereas V max value was lower for the immobilized GOD. Immobilized glucose oxidase showed improved operational stability by maintaining 33% of the initial activity after 35 cycles of repeated use and was found to retain 94% of activity after 1 month storage period. Improved resistance against urea denaturation was achieved and the immobilized glucose oxidase retained 50% of the activity without urea in the presence of 5 M urea whereas free enzyme retained only 8% activity.