Show/Hide Menu
Hide/Show Apps
anonymousUser
Logout
Türkçe
Türkçe
Search
Search
Login
Login
OpenMETU
OpenMETU
About
About
Açık Bilim Politikası
Açık Bilim Politikası
Frequently Asked Questions
Frequently Asked Questions
Browse
Browse
By Issue Date
By Issue Date
Authors
Authors
Titles
Titles
Subjects
Subjects
Communities & Collections
Communities & Collections
Characterization of beta-galactosidase immobilized into poly(hydroxyethylmethacrylate) membranes
Date
1998-05-01
Author
Adalı, Orhan
Baran, T
Arica, MY
Metadata
Show full item record
This work is licensed under a
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License
.
Item Usage Stats
0
views
0
downloads
beta-galactosidase was immobilized into pHEMA membranes with the highest specific activity yield of 9.5%. The specific activity of the entrapped enzyme was found to be decreased as the enzyme loading increased in pHEMA membranes. The optimum pH and temperature for maximum activity of the immobilized beta-galactosidase was found to be at pH 7.5 and 50 degrees C, respectively, and were the same as native enzyme. K-m and V-max values for the free enzyme were found to be 0.256 mM and 26.6 mu mole/min/mg, respectively. K-m value of immobilized beta-galactosidase was found to be increased about 3 folds upon immobilization. Operational, thermal and storage stability of beta-galactosidase were found to increase with immobilization. Immobilized enzyme preparation was reused in 15 cycles without significant loss in activity.
Subject Keywords
Beta-galactosidase
,
Immobilization
URI
https://hdl.handle.net/11511/56039
Journal
BIOCHEMICAL ARCHIVES
Collections
Department of Biology, Article