IMMOBILIZATION OF GLUCOSE-OXIDASE - A COMPARISON OF ENTRAPMENT AND COVALENT BONDING

Date

1993-01-01

Author

ARICA, MY
Hasırcı, Vasıf Nejat

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Glucose oxidase was immobilized onto poly(2-hydroxyethyl methacrylate) (pHEMA) membranes by two methods: by covalent bonding through epichlorohydrin and by entrapment between pHEMA membranes. The highest immobilization efficiency was found to be 17.4% and 93.7% for the covalent bonding and entrapment, respectively. The K(m) values were 5.9 mmol dm-3, 8.8 mmol dm-3 and 12.4 mmol dm-3 for free, bound and entrapped enzyme, respectively. The V(max) values were 0.071 mmol dm-3 min-1, 0.067 mmol dm-3 min-1 and 0.056 mmol dm-3 min-1 for free, bound and entrapped enzyme. When the medium was saturated with oxygen, K(m) was not significantly altered but V(max) was. The optimum pH values for the free, covalently-bound and entrapped enzyme were determined to be 5, 6, and 7, respectively. The optimum temperature was 30-degrees-C for free or covalently-bound enzyme but 35-degrees-C for entrapped enzyme. The deactivation constant for bound enzyme was determined as 1.7 x 10(-4) min-1 and 6.9 x 10(-4) min-1 for the entrapped enzyme.

Subject Keywords

Glucose Oxidase, Entrapment, Covalent Bonding, Phema

URI

https://hdl.handle.net/11511/32078

Journal

JOURNAL OF CHEMICAL TECHNOLOGY AND BIOTECHNOLOGY

DOI

https://doi.org/10.1002/jctb.280580313

Collections

Graduate School of Natural and Applied Sciences, Article

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BIOREACTOR APPLICATIONS OF GLUCOSE-OXIDASE COVALENTLY BONDED ON PHEMA MEMBRANES ARICA, MY; Hasırcı, Vasıf Nejat (1993-09-01) Glucose oxidase was immobilized onto poly(2-hydroxyethyl methacrylate) membranes by covalent bonding through epichlorohydrin. The highest immobilization efficiency was found to be 17.4%. The K(m) values were 5.9 and 8.8 mm for free and bound enzymes, respectively, and the V(max) values were 0.071 and 0.067 mm/min for free and bound enzymes. When the medium was saturated with oxygen K(m) was not altered significantly but V(max) was. The optimum pHs for the free and bound enzyme were determined to be 5 and 6,...
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. ...
Immobilization of glucose oxidase in conducting graft copolymers and determination of glucose amount in orange juices with enzyme electrodes Yildiz, HB; Kiralp, S; Toppare, Levent Kamil; Yagci, Y (Elsevier BV, 2005-12-15) Glucose oxidase was immobilized in conducting copolymers of three different types of poly(methyl methacrylate-co-thienyl methacrylate). Immobilization of enzyme was carried out by the entrapment in conducting polymers during electrochemical polymerization of pyrrole on the copolymer electrodes. Maximum reaction rate, Michaelis-Menten constants, temperature, pH and operational stabilities were determined for immobilized enzyme. The amount of glucose in orange juices of Turkey was investigated by using enzyme...
Comparison of beta-galactosidase immobilization by entrapment in and adsorption on poly(2-hydroxyethylmethacrylate) membranes Baran, T; Arica, MY; Denizli, A; Hasırcı, Vasıf Nejat (1997-12-01) beta-Galactosidase was immobilized in/on poly(2-hydroxyethyl methacrylate) (pHEMA) membranes by two different methods: adsorption on Cibacron F3GA derivatized pHEMA membranes (pHEMA-CB), and entrapment in the bulk of the pHEMA membranes. The maximum beta-galactosidase adsorption on pHEMA-CB membranes was obtained as 95.6 mu g cm(-2) in 2.0 mg cm(-3) enzyme solution. The adsorption phenomena appeared to follow a typical Langmuir isotherm. In the entrapment, an increase in beta-galactosidase loading resulted ...
Immobilization of invertase and glucose oxidase in poly 2-methylbutyl-2-(3-thienyl) acetate/polypyrrole matrices Isik, S; Alkan, S; Toppare, Levent Kamil; Cianga, I; Yagci, Y (Elsevier BV, 2003-12-01) Immobilization of invertase and glucose oxidase in conducting polypyrrole and copolymers of poly 2-methylbutyl-2-(3-thienyl) acetate with pyrrole were achieved via electrochemical method. Sodium dodecyl sulphate was found to be the most suitable supporting electrolyte. Maximum reaction rate, Michaelis-Menten constant and optimum temperatures were determined for native and immobilized enzymes. Storage and operational stabilities of enzyme electrodes were also investigated.

Citation Formats

M. ARICA and V. N. Hasırcı, “IMMOBILIZATION OF GLUCOSE-OXIDASE - A COMPARISON OF ENTRAPMENT AND COVALENT BONDING,” JOURNAL OF CHEMICAL TECHNOLOGY AND BIOTECHNOLOGY, pp. 287–292, 1993, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/32078.