Immobilization of tyrosinase in polysiloxane/polypyrrole copolymer matrices

Date

2005-04-01

Author

Arslan, A
Kiralp, S
Toppare, Levent Kamil
Yagci, Y

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Immobilization of tyrosinase in conducting copolymer matrices of pyrrole functionalized polydimethylsiloxane/polypyrrole (PDMS/PPy) was achieved by electrochemical polymerization. The polysiloxane/polypyrrole/tyrosinase electrode was constructed by the entrapment of enzyme in conducting matrices during electrochemical copolymerization. Maximum reaction rate (V-max) and Michaelis-Menten constant were investigated for immobilized enzyme. Enzyme electrodes were prepared in two different electrolyte/sol vent systems. The effect of supporting electrolytes, p-toluene sulfonic acid and sodium dodecyl sulfate on the enzyme activity and film morphology were determined. Temperature and pH optimization, operational stability and shelf-life of enzyme electrodes were also examined. Phenolic contents of green and black tea were determined by using enzyme electrodes.

Subject Keywords

Biochemistry, Molecular Biology, Structural Biology, General Medicine

URI

https://hdl.handle.net/11511/42683

Journal

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES

DOI

https://doi.org/10.1016/j.ijbiomac.2005.01.006

Collections

Department of Chemistry, Article

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Immobilization of tyrosinase in polysiloxane/polypyrrole copolymer matrices Arslan, Ahu; Toppare, Levent Kamil; Department of Chemistry (2006) Immobilization of tyrosinase in conducting copolymer matrices of pyrrole functionalized polydimethylsiloxane/polypyrrole (PDMS/PPy) were achieved by electrochemical polymerization. The polysiloxane/polypyrrole/tyrosinase electrode was constructed by the entrapment of enzyme in conducting matrices during electrochemical copolymerization. Maximum reaction rate (Vmax) and Michaelis-Menten constant (Km) were investigated for immobilized enzyme. Enzyme electrodes were prepared in two different electrolyte/solven...
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...
Various applications of immobilized glucose oxidase and polyphenol oxidase in a conducting polymer matrix Cil, M.; Boyukbayram, A. E.; Kiralp, S.; Toppare, Levent Kamil; Yagci, Y. (Elsevier BV, 2007-06-01) In this study, glucose oxidase and polyphenol oxidase were immobilized in conducting polymer matrices; polypyrrole and poly(N-(4-(3-thienyl methylene)-oxycarbonyl phenyl) maleimide-co-pyrrole) via electrochemical method. Fourier transform infrared and scanning electron microscope were employed to characterize the copolymer of (N-(4-(3-thienyl methylene)-oxycarbonyl phenyl) maleimide) with pyrrole. Kinetic parameters, maximum reaction rate and Michealis-Menten constant, were determined. Effects of temperatur...
Structural properties of an engineered outer membrane protein G mutant, OmpG-16SL, investigated with infrared spectroscopy Yilmaz, Irem; Yildiz, Ozkan; KORKMAZ ÖZKAN, FİLİZ (Informa UK Limited, 2019-05-31) The structural and functional differences between wild type (WT) outer membrane protein G and its two mutants are investigated with Fourier transform infrared spectroscopy. Both mutants have a long extension to the primary sequence to increase the number of beta-strands from 14 (wild type) to 16 in an attempt to enlarge the pore diameter. The comparison among proteins is made in terms of pH-dependent conformational changes and thermal stability. Results show that all proteins respond to pH change but at dif...
Immobilization of tyrosinase and alcohol oxidase in conducting copolymers of thiophene functionalized poly(vinyl alcohol) with pyrrole Yildiz, Huseyin Bekir; Sahmetlioglu, Ertugrul; Boyukbayram, Ayse Elif; Toppare, Levent Kamil; Yagci, Yusuf (Elsevier BV, 2007-08-01) Immobilization of tyrosinase and alcohol oxidase is achieved in the copolymer of pyrrole with vinyl alcohol with thiophene side groups (PVATh-co-PPy) which is a newly synthesized conducting polymer. PVATh-co-PPy/alcohol oxidase and PVATh-co-PPy/tyrosinase electrodes are constructed by the entrapment of enzyme in conducting copolymer matrix during electrochemical copolymerization. For tyrosinase and alcohol oxidase enzymes, catechol and ethanol are used as the substrates, respectively. Kinetic parameters: ma...

Citation Formats

A. Arslan, S. Kiralp, L. K. Toppare, and Y. Yagci, “Immobilization of tyrosinase in polysiloxane/polypyrrole copolymer matrices,” INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, pp. 163–167, 2005, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/42683.