BIOREACTOR APPLICATIONS OF GLUCOSE-OXIDASE COVALENTLY BONDED ON PHEMA MEMBRANES

Date

1993-09-01

Author

ARICA, MY
Hasırcı, Vasıf Nejat

Metadata

Show full item record

This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Item Usage Stats

137
views

0
downloads

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, respectively, and the optimum temperature was 30-degrees-C for both forms. The inactivation constant for the bound enzyme was found to be 1.7 x 10(-4) min-1.

Subject Keywords

Immobilization, Epichlorohydrin, Phema, Glucose oxidase

URI

https://hdl.handle.net/11511/32338

Journal

BIOMATERIALS

DOI

https://doi.org/10.1016/0142-9612(93)90001-i

Collections

Graduate School of Natural and Applied Sciences, Article

Suggestions

OpenMETU
Core

IMMOBILIZATION OF GLUCOSE-OXIDASE - A COMPARISON OF ENTRAPMENT AND COVALENT BONDING ARICA, MY; Hasırcı, Vasıf Nejat (1993-01-01) 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....
GLUCOSE-OXIDASE SANDWICHED BETWEEN PHEMA LAYERS - A CONTINUOUS-FLOW REACTOR APPLICATION ARICA, MY; Hasırcı, Vasıf Nejat (1993-09-01) Glucose oxidase was entrapped between poly(2-hydroxyethyl methacrylate) membranes and conditions were optimized for high enzyme activity and high levels of entrapment. Highest entrapment was with a 78 mum thick coat. A continuous flow membrane reactor was designed and used. The reaction was first order with respect to glucose and to oxygen. V(max) values for the native and immobilized enzymes were 0.182 and 0.133 mm/min. The K(m)'s for native and immobilized enzymes were 6.2 and 16.9 mm, respectively. At hi...
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. ...
Bioactive Surface Design Based on Functional Composite Electrospun Nanofibers for Biomolecule Immobilization and Biosensor Applications Uzun, Sema Demirci; Kayaci, Fatma; UYAR, Tamer; TİMUR, SUNA; Toppare, Levent Kamil (2014-04-09) The combination of nanomaterials and conducting polymers attracted remarkable attention for development of new immobilization matrices for enzymes. Hereby, an efficient surface design was investigated by modifying the graphite rod electrode surfaces with one-step electrospun nylon 6,6 nanofibers or 4% (w/w) multiwalled carbon nanotubes (MWCNTs) incorporating nylon 6,6 nanofibers (nylon 6,6/4MWCNT). High-resolution transmission electron microscopy study confirmed the successful incorporation of the MWCNTs in...
Asymmetric aldol addition of alpha-azido ketones to ethyl pyruvate mediated by a cinchona-based bifunctional urea catalyst Okumus, Seda; Tanyeli, Cihangir; Demir, Ayhan Sıtkı (Elsevier BV, 2014-07-30) The first asymmetric synthesis of ethyl 4-aryl-3-azido-2-hydroxy-2-methyl-4-oxobutanoates via a cinchona organocatalyst induced aldol addition of alpha-azido ketones to ethyl pyruvate has been developed. The coupling reaction under optimized conditions was carried out to furnish tetrafunctionalized synthons with enantioselectivities of up to 91:9 and enriched diastereoselectivities of up to 95:5 (syn:anti).

Citation Formats

M. ARICA and V. N. Hasırcı, “BIOREACTOR APPLICATIONS OF GLUCOSE-OXIDASE COVALENTLY BONDED ON PHEMA MEMBRANES,” BIOMATERIALS, pp. 803–808, 1993, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/32338.