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 in conducting polymer matrices
Download
index.pdf
Date
1997-09-01
Author
Selampinar, F
Akbulut, Ural
Ozden, MY
Toppare, Levent Kamil
Metadata
Show full item record
This work is licensed under a
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License
.
Item Usage Stats
218
views
0
downloads
Cite This
This paper reports a novel approach in the electrode immobilization of an enzyme, invertase, by electrochemical polymerization of pyrrole in the presence of enzyme. The polypyrrole/invertase and polyamide/polypyrrole/invertase electrodes were constructed by the entrapment of enzyme in conducting matrices during electrochemical polymerization of pyrrole. This study involves the preparation and characterization of polypyrrole/invertase and polyamide/polypyrrole/invertase electrodes under conditions compatible with the enzyme. It demonstrates the effects of pH and temperature on the properties of enzyme electrode. Enzyme leakage tests were carried out during reuse number studies. The preparation of enzyme electrodes was done in two different electrolyte/solvent systems. The enzyme serves as a sucrose electrode and retains its activity for several months. (C) 1997 Elsevier Science Limited. All rights reserved.
Subject Keywords
Immobilization
,
Conducting polymer matrices
,
Invertase
,
Polymerization
URI
https://hdl.handle.net/11511/34520
Journal
BIOMATERIALS
DOI
https://doi.org/10.1016/s0142-9612(97)00056-2
Collections
Department of Chemistry, Article
Suggestions
OpenMETU
Core
Immobilization of yeast cells in several conducting polymer matrices
Balci, Z; Akbulut, Ural; Toppare, Levent Kamil; Alkan, S; Bakir, U; Yagci, Y (2002-01-01)
Immobilization of yeast cells (Saccharomyces cerevisiae) in different polymer matrices was performed by constant potential electrolysis. These matrices were polypyrrole (PPy); poly(methyl methacrylate)/polypyrrole (,PMMA/PPy) and thiophene-capped poly(methyl methacrylate)/ polypyrrole (TPMMA/PPy). The characterization of PMMA/PPy copolymer was achieved by Fourier-transform Infrared Spectroscopy (FT-IR), Differential Scanning Calorimetry (DSC) and Scanning Electron Microscopy (SEM). The invertase activity of...
Immobilization of glucose isomerase in surface-modified alginate gel beads
TÜMTÜRK, HAYRETTİN; DEMİREL, Gökhan; ALTINOK, HAYDAR; AKSOY, SERPİL; Hasırcı, Nesrin (2008-04-01)
In this study, glucose isomerase enzyme was entrapped into modified and nonmodified calcium alginate gel beads. Various characteristics of free and immobilized enzymes such as the optimum pH, temperature and dependence of activity on storage and operational stability were evaluated. The optimum pH and temperature of free and immobilized glucose isomerase were found to be the same values as 7.5 and 60C, respectively. For free and immobilized enzymes, kinetic parameters were calculated as 1.79 x 10(-2) and 8....
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, polyphenol oxidase and glucose oxidase n conducting copolymers of thiophene-capped polytetrahydrofuran and pyrrole
Böyükbayram, Ayşe Elif; Toppare, Levent Kamil; Department of Chemistry (2005)
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 ...
Electrochemical polymerization of 1-(4-nitrophenyl)-2,5-di(2-thienyl)-1 H-pyrrole as a novel immobilization platform for microbial sensing
Tuncagil, Sevinc; ODACI DEMİRKOL, DİLEK; Varis, Serhat; TİMUR, SUNA; Toppare, Levent Kamil (2009-09-01)
Two types of bacterial biosensor were constructed by immobilization of Gluconobacter oxydans and Pseudomonas fluorescens cells on graphite electrodes modified with the conducting polymer; poly(1-(4-nitrophenyl)-2,5-di(2-thienyl)-1 H-pyrrole) [SNS(NO2)]. The measurement was based on the respiratory activity of cells estimated by the oxygen consumption at -0.7 V due to the metabolic activity in the presence of substrate. As well as analytical characterization, the linear detection ranges, effects of electropo...
Citation Formats
IEEE
ACM
APA
CHICAGO
MLA
BibTeX
F. Selampinar, U. Akbulut, M. Ozden, and L. K. Toppare, “Immobilization of invertase in conducting polymer matrices,”
BIOMATERIALS
, pp. 1163–1168, 1997, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/34520.