Characterization of beta-galactosidase immobilized into poly(hydroxyethylmethacrylate) membranes

Date

1998-05-01

Author

Adalı, Orhan
Arica, MY

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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

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Department of Biology, Article

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Characterization of β-galactosidase immobilized into poly(hydroxyethyl methacrylate) membranes Adalı, Orhan; Arica, M.y. (1998-01-01) 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) va...
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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Citation Formats

O. Adalı and M. Arica, “Characterization of beta-galactosidase immobilized into poly(hydroxyethylmethacrylate) membranes,” BIOCHEMICAL ARCHIVES, pp. 123–129, 1998, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/56039.