Immobilization of invertase, polyphenol oxidase and glucose oxidase n conducting copolymers of thiophene-capped polytetrahydrofuran and pyrrole

Download

index.pdf

Date

2005

Author

Böyükbayram, Ayşe Elif

Metadata

Show full item record

Item Usage Stats

213
views

102
downloads

Immobilization of invertase, polyphenol oxidase (PPO) and glucose oxidase (GOD) enzymes were performed in electrochemically synthesized two types of conducting copolymers. One end and two end thiophene-capped polytetrahydrofuran (TPTHF-1 and TPTHF-2) were copolymerized with pyrrole under conditions of constant potential electrolysis. The copolymers were characterized by thermal, spectroscopic and scanning electron microscopy analyses. Immobilization was carried out via entrapment of enzymes in two types of matrices during the copolymerization of pyrrole with the insulating polymers in the presence of sodium dodecyl sulphate (SDS). Kinetic parameters: Maximum reaction rate (Vmax) and Michaelis-Menten constant (Km) were determined for the enzyme electrodes. Temperature optimization, pH optimization, operational stability and shelf-life of the enzyme electrodes were investigated. Enzyme electrodes of polyphenol oxidase and glucose oxidase were used to determine the amount of their substrates in samples. Polyphenol oxidase converts mono and diphenols to quinone. Amount of phenolic compounds in two kinds of wines were determined by analyzing the quinone amount. Glucose oxidase converts ?-D-glucose to D-glucono-1,5-lactone. Glucose amount was determined in two kind of factory-produced orange juices by analyzing D-glucono-1,5-lactone.

Subject Keywords

Polymers., Macromolecules.

URI

http://etd.lib.metu.edu.tr/upload/12605935/index.pdf
https://hdl.handle.net/11511/14720

Collections

Graduate School of Natural and Applied Sciences, Thesis

Suggestions

OpenMETU
Core

Immobilization of glucose oxidase and polyphenol oxidase in poly(N-(4-(3-thienyl methylene)-oxycarbonylphenyl) maleimide)-co-pyrrole) matrice Çil, Mahmut; Toppare, Levent Kamil; Department of Chemistry (2006) In this study, glucose oxidase and polyphenol oxidase were immobilized in conducting copolymer poly(N-(4-(3-thienyl methylene)-oxycarbonylphenyl)maleimide)-co-pyrrole(P(MBThi-co-Py)). A copolymer was electrochemically synthesized by using sodium dodecyl sulfate (SDS) as supporting electrolyte and characterized by FTIR, scanning electron microscopy (SEM) and conductivity measurements. Immobilization of glucose oxidase (GOD) and polyphenol oxidase (PPO) enzymes were performed in conducting PPy and P(MBThi-co-...
Modified acrylic hydrogels as controlled release systems Pınardağ, Fatma Esra; Hasırcı, Nesrin; Department of Chemistry (2006) In this study, pH-sensitive poly(acrylamide-co-acrylic acid) hydrogels were synthesized as controlled release systems in the presence of N,N-methylene bisacrylamide as crosslinker and ammonium persulfate as initiator. A set of hydrogels were used in the form they were prepared. One set of hydrogels were prepared as porous networks by incorporating sodium chloride into the reaction medium and then leaching of it after the completion of polymerization reaction. Two sets of hydrogels were modified by argon-pla...
Covalent immobilization of glucose isomerase on poly(2-hydoxyethyl methacrylate) particles Yıldız, Ümit Hakan; Hasırcı, Nesrin; Department of Chemistry (2004) In this study, poly (2-hydroxyethyl methacrylate), P(HEMA), particles were prepared by suspension polymerization of the monomer 2-hydroxyethyl methacrylate with addition of ethylene glycol dimethyacrylate, EGDMA, as cross linker. Glucose isomerase, GI, enzyme was covalently immobilized on the prepared P(HEMA) particles after activation of the particles with cyanuric chloride. The activities of the free and immobilized enzymes were measured with Ethanol-Carbazole method. The immobilization of GI on P(HEMA) p...
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. ...
Immobiliation of glucose oxidase and polyphenol oxidase in conducting copolymer of pyrrole functionalized polystyrene with pyrrole Ekinci, Olçun; Toppare, Levent Kamil; Department of Chemistry (2006) Electrochemical polymerization of pyrrole functionalized polystyrene (PStPy) with pyrrole was carried out in water-sodium dodecyl sulfate solvent-electrolyte couple. Characterization of the resulting copolymer was performed via Fourier transform infrared spectroscopy (FTIR), scanning electron microscopy (SEM) and four probe conductivity measurements. Glucose oxidase and polyphenol oxidase enzymes were immobilized in polypyrrole (PPy) and conducting copolymer of pyrrole functionalized polystyrene with pyrrol...

Citation Formats

A. E. Böyükbayram, “Immobilization of invertase, polyphenol oxidase and glucose oxidase n conducting copolymers of thiophene-capped polytetrahydrofuran and pyrrole,” Ph.D. - Doctoral Program, Middle East Technical University, 2005.