Show/Hide Menu
Hide/Show Apps
Logout
Türkçe
Türkçe
Search
Search
Login
Login
OpenMETU
OpenMETU
About
About
Open Science Policy
Open Science Policy
Open Access Guideline
Open Access Guideline
Postgraduate Thesis Guideline
Postgraduate Thesis Guideline
Communities & Collections
Communities & Collections
Help
Help
Frequently Asked Questions
Frequently Asked Questions
Guides
Guides
Thesis submission
Thesis submission
MS without thesis term project submission
MS without thesis term project submission
Publication submission with DOI
Publication submission with DOI
Publication submission
Publication submission
Supporting Information
Supporting Information
General Information
General Information
Copyright, Embargo and License
Copyright, Embargo and License
Contact us
Contact us
Immobilization of invertase and glucose oxidase in conducting copolymers of thiophene functionalized poly(vinyl alcohol) with pyrrole
Date
2006-03-01
Author
Sahmetlioglu, E
Yuruk, H
Toppare, Levent Kamil
Cianga, I
Yagci, Y
Metadata
Show full item record
This work is licensed under a
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License
.
Item Usage Stats
205
views
0
downloads
Cite This
In this study, immobilizations of invertase and glucose oxidase were achieved in conducting thiophene functionalized copolymers of vinyl alcohol with thiophene side groups and pyrrole (PVATh/PPy) 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 the enzyme activity and film morphologies was examined. The optimum temperature, operational and storage stabilities of immobilized enzymes were determined. PVATh/PPy copolymer was found to exhibit significantly enhanced properties compared to pristine polypyrrole.
Subject Keywords
Materials Chemistry
,
Biochemistry
,
General Chemistry
,
General Chemical Engineering
,
Polymers and Plastics
,
Environmental Chemistry
URI
https://hdl.handle.net/11511/48665
Journal
REACTIVE & FUNCTIONAL POLYMERS
DOI
https://doi.org/10.1016/j.reactfunctpolym.2005.08.009
Collections
Department of Chemistry, Article
Suggestions
OpenMETU
Core
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 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.
Immobilization of invertase on a conducting polymer of 1-(4-nitrophenyl)-2,5-di(2-thienyl)-1H-pyrrole
Tuncagil, Sevinc; Kiralp, Senem; Varls, Serhat; Toppare, Levent Kamil (Elsevier BV, 2008-03-01)
In this study, immobilization of invertase was achieved on a conducting polymer of 1-(4-nitrophenyl)-2,5-di(2-thienyl)-1H-pyrrole) (SNS (NO2)) via electrochemical polymerization. Kinetic parameters, maximum reaction rate (V-max) and substrate affinity (K-m), optimum temperature and pH, operational and storage stabilities of immobilized enzyme were determined.
Immobilization of cholesterol oxidase in a conducting copolymer of thiophene-3-yl acetic acid cholesteryl ester with pyrrole
Çırpan, Ali; Toppare, Levent Kamil; YAGCI, Y (Informa UK Limited, 2003-01-01)
Cholesterol oxidase has been immobilized in conducting copolymers of thiophene-3-yl acetic acid cholesteryl ester with pyrrole (CM/PPy) and polypyrrole (PPy) via electropolymerization. p-Toluene sulphonic acid was used as the supporting electrolyte. Kinetic parameters (V-max and K-m) and operational stability of enzyme electrodes were investigated. Surface morphology of the films was examined by scanning electron microscope.
Immobilization of Tyrosinase in Poly(2-thiophen-3-yl-alkyl ester) Derivatives
ÇAMURLU, PINAR; Kayahan, Senem; Toppare, Levent Kamil (Informa UK Limited, 2008-01-01)
In this study, construction of novel biosensors for the determination of phenolic compound was performed via immobilization of tyrosinase during the electrochemical synthesis of conducting block copolymers of 2-thiophen-3-yl-alkyl ester derivatives with 3,4-ethylenedioxythiophene and synthesis of poly(3,4-ethylenedioxythiophene) (PEDOT). The resultant biosensors were characterized in terms of their maximum reaction rates, Michaelis-Menten constants (Km), temperature and pH stabilities. All the copolymer mat...
Citation Formats
IEEE
ACM
APA
CHICAGO
MLA
BibTeX
E. Sahmetlioglu, H. Yuruk, L. K. Toppare, I. Cianga, and Y. Yagci, “Immobilization of invertase and glucose oxidase in conducting copolymers of thiophene functionalized poly(vinyl alcohol) with pyrrole,”
REACTIVE & FUNCTIONAL POLYMERS
, pp. 365–371, 2006, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/48665.