Immobilization of glucose oxidase in poly(2-hydroxyethyl methacrylate) membranes

1987-11
Arica, Y.
Hasirci, V.N.
Arica, Yakup
Glucose oxidase (GOD) was immobilized in a poly(2-hydroxyethyl methacrylate) (HEMA) membrane through matrix entrapment in order to investigate the effect of various parameters (e.g. concentration of ingredients, temperature, repeated interaction with glucose and shelf storage) on the activity of the enzyme. Permeability of the membrane to a model permeant was tested and SEMs were obtained. It was observed that upon immobilization the affinity of GOD towards glucose was substantially decreased, and increasing the GOD content of the membrane adversely affected the activity. Membranes with the highest enzyme activity were also found to be the most permeable. Changes were detected in the pH and temperature where GOD is most active. Membrane permeability was observed to increase when crosslinker, and/or HEMA concentrations were low. The same parameters were also found to alter the morphology of the membrane as observed under SEM.

Suggestions

Immobilization of glucose oxidase onto gelatin for biosensor construction
Emregul, E; Sungur, S; Akbulut, Ural (Informa UK Limited, 2005-01-01)
The properties of a glucose biosensor made by immobilization of glucose oxidase onto gelatin in a layer of electrochemically deposited polyaniline have been investigated. Glucose oxidase was immobilized within gelatin cross-links with chromium(III) acetate. The glucose oxidase biosensor was developed by forming a polyaniline-deposited electrode surface as support for the immobilized enzyme gel, in order to increase its durability. The polyaniline/gelatin/glucose oxidase biosensor has been characterized usin...
Immobilization of yeast cells in acrylamide gel matrix
Hasirci, V.N.; Alaeddinoglu, G.; Aykut, Gül (Elsevier BV, 1988-3)
Entrapment of yeast cells in a three-dimensional polymer matrix was achieved, and various properties of the polymer matrix as well as the invertase activity of the yeast cells were studied. When the matrix was highly cross-linked or synthesized from concentrated polymer solutions, its swelling ratio decreased. Invertase activity was found to increase with water content of the matrix. Cell content of the gel was found to affect adversely enzyme activity. The enzyme was found to retain its activity after seve...
Optimization studies on the features of an activated charcoal-supported urease system
Kibarer, GD; Akovali, G (Elsevier BV, 1996-08-01)
The adsorption of urease onto a well-defined solid support, petroleum-based activated charcoal, has been achieved to provide the enzymatic hydrolysis of urea. In order to produce a biocompatible surface, the enzyme support system has been coated with hexamethyldisiloxane through plasma polymerization. The quality of the resulting coat was tested by electronic spectroscopy for chemical analysis and scanning electron microscopy techniques. Studies on the adsorption of urease, and activity and stability of the...
POLYESTER FILM STRIPS COATED WITH PHOTOGRAPHIC GELATIN CONTAINING IMMOBILIZED GLUCOSE-OXIDASE HARDENED BY CHROMIUM(III) SULFATE
ELCIN, YM; Akbulut, Ural (Elsevier BV, 1992-01-01)
Glucose oxidase was immobilized into photographic gelatin hardened by chromium(III) sulphate. The enzyme-gelatin mixture was coated on polyester film strips which allowed easy and simple handling during assays. The effect of gelatin and cross-linker concentrations on water content and enzymatic activity was studied. The effect of pH during immobilization and that of incubation temperature on maximum activity were examined- Enzyme leakage tests were carried out during reuse number studies. Consecutive use of...
Immobilization of invertase and glucose oxidase in conducting H-type polysiloxane/polypyrrole block copolymers
Gursel, A; Alkan, S; Toppare, Levent Kamil; Yagci, Y (Elsevier BV, 2003-01-01)
In this study, immobilizations of enzymes, invertase and glucose oxidase, were achieved in conducting copolymers of N-pyrrolyl terminated polydimethylsiloxane/polypyrrole (PDMS/PPy) matrices via electrochemical polymerization. The kinetic parameters, v(max) (maximum reaction rate) and K-m (substrate affinity), of both free and immobilized enzymes were determined. The effect of supporting electrolytes, p-toluene sulfonic acid and sodium dodecyl sulfate, on enzyme activity and film morphologies was examined. ...
Citation Formats
Y. Arica, V. N. Hasirci, and Y. Arica, “Immobilization of glucose oxidase in poly(2-hydroxyethyl methacrylate) membranes,” Biomaterials, pp. 489–495, 1987, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/51904.