Show/Hide Menu
Hide/Show Apps
Logout
Türkçe
Türkçe
Search
Search
Login
Login
OpenMETU
OpenMETU
About
About
Open Science Policy
Open Science Policy
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 bacteriorhodopsin on synthetic membrane
Download
Vedat Sediroğlu.pdf
Date
1992
Author
Sediroğlu, Vedat
Metadata
Show full item record
Item Usage Stats
48
views
0
downloads
Cite This
URI
https://hdl.handle.net/11511/9691
Collections
Graduate School of Natural and Applied Sciences, Thesis
Suggestions
OpenMETU
Core
IMMOBILIZATION OF NADH-CYTOCHROME B5 REDUCTASE INTO GELATIN BY CROSS-LINKING
Yıldırım, Onur; Akbulut, Ural (1994-01-01)
In this work NADH-cytochrome b5 reductase enzyme (EC 1.6.2.2) obtained from rabbit liver microsomes was immobilized into gelatin by crosslinking. Chromium (III) acetate and chromium (III) sulfate were used as crosslinkers. To find the most suitable immobilization parameters; effect of crosslinker, enzyme and gelatin concentrations on immobilized enzyme activity were investigated. Unbounded enzyme was determined by washing experiments.
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 in conducting copolymers of 3-methylthienyl methacrylate
Çırpan, Ali; Toppare, Levent Kamil; Yagci, Y. (Elsevier BV, 2003-4)
Immobilization of invertase in conducting copolymer matrices of 3-methylthienyl methacrylate with pyrrole and thiophene was achieved by constant potential electrolysis using sodium dodecyl sulfate (SDS) as the supporting electrolyte. Polythiophene (PTh) was also used in entrapment process for comparison. Kinetic parameters, Michaelis-Menten constant, Km, and the maximum reaction rate, Vmax, were investigated. Operational stability and temperature optimization of the enzyme electrodes were also examined.
Immobilization of glucose oxidase in poly(2-hydroxyethyl methacrylate) membranes
Arica, Y.; Hasirci, V.N.; Arica, Yakup (Elsevier BV, 1987-11)
Glucose oxidase (GOD) was immobilized in a poly(2-hydroxyethyl methacrylate) (HEMA) membrane through matrix entrapment in order to investigate the effect of various parameters (e.g. concentration of ingredients, temperature, repeated interaction with glucose and shelf storage) on the activity of the enzyme. Permeability of the membrane to a model permeant was tested and SEMs were obtained. It was observed that upon immobilization the affinity of GOD towards glucose was substantially decreased, and increasin...
Immobilization of glucose oxidase enzyme in conducting graft copolymers of pyrrole
Tirkeş, Seha; Toppare, Levent; Department of Chemistry (2001)
Citation Formats
IEEE
ACM
APA
CHICAGO
MLA
BibTeX
V. Sediroğlu, “Immobilization of bacteriorhodopsin on synthetic membrane,” Middle East Technical University, 1992.