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Characterization of β-galactosidase immobilized into poly(hydroxyethyl methacrylate) membranes
Date
1998-01-01
Author
Adalı, Orhan
Arica, M.y.
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β-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 βgalactosidase was found to be at pH 7.5 and 50°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 μmole/min/mg, respectively. K(m) value of immobilized βgalactosidase was found to be increased about 3 folds upon immobilization. Operational, thermal and storage stability of β-galactosidase were found to increase with immobilization. Immobilized enzyme preparation was reused in 15 cycles without significant loss in activity.
Subject Keywords
Immobilization
,
β-galactosidase
URI
https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0031836814&origin=inward
https://hdl.handle.net/11511/74384
Journal
Biochemical Archives
Collections
Department of Biology, Article
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Characterization of beta-galactosidase immobilized into poly(hydroxyethylmethacrylate) membranes
Adalı, Orhan; Arica, MY (1998-05-01)
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, respec...
Comparison of beta-galactosidase immobilization by entrapment in and adsorption on poly(2-hydroxyethylmethacrylate) membranes
Baran, T; Arica, MY; Denizli, A; Hasırcı, Vasıf Nejat (1997-12-01)
beta-Galactosidase was immobilized in/on poly(2-hydroxyethyl methacrylate) (pHEMA) membranes by two different methods: adsorption on Cibacron F3GA derivatized pHEMA membranes (pHEMA-CB), and entrapment in the bulk of the pHEMA membranes. The maximum beta-galactosidase adsorption on pHEMA-CB membranes was obtained as 95.6 mu g cm(-2) in 2.0 mg cm(-3) enzyme solution. The adsorption phenomena appeared to follow a typical Langmuir isotherm. In the entrapment, an increase in beta-galactosidase loading resulted ...
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Preparation of Chitosan-Coated Magnetite Nanoparticles and Application for Immobilization of Laccase
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In this study, immobilization of laccase (L) enzyme on magnetite (Fe(3)O(4)) nanoparticles was achieved, so that the immobilized enzyme could be used repeatedly. For this purpose, Fe(3)O(4) nanoparticles were coated and functionalized with chitosan (CS) and laccase from Trametes versicolor was immobilized onto chitosan-coated magnetic nanoparticles (Fe(3)O(4)-CS) by adsorption or covalent binding after activating the hydroxyl groups of chitosan with carbodiimide (EDAC) or cyanuric chloride (CC). For chitosa...
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O. Adalı and M. y. Arica, “Characterization of β-galactosidase immobilized into poly(hydroxyethyl methacrylate) membranes,”
Biochemical Archives
, pp. 123–129, 1998, Accessed: 00, 2021. [Online]. Available: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0031836814&origin=inward.
