Immobilization of catalase via adsorption onto l-histidine grafted functional pHEMA based membrane
| Autor: | Sinan Akgöl, Yasemin Kaçar, Handan Yavuz, Adil Denizli, Serpil Özkara, M. Yakup Arica |
|---|---|
| Přispěvatelé: | Kırıkkale Üniversitesi |
| Rok vydání: | 2001 |
| Předmět: |
chemistry.chemical_classification
Chromatography Aqueous solution biology Immobilized enzyme Chemistry Process Chemistry and Technology catalase Chemical modification Bioengineering Biochemistry Catalysis Enzyme assay Membrane Adsorption Enzyme adsorption Catalase immobilization biology.protein pHEMA membrane L-histidine Nuclear chemistry |
| Zdroj: | Journal of Molecular Catalysis B: Enzymatic. 15:197-206 |
| ISSN: | 1381-1177 |
| DOI: | 10.1016/s1381-1177(01)00029-7 |
| Popis: | Kacar, Yasemin/0000-0002-8682-9228; Akgol, Sinan/0000-0002-8528-1854; AKGOL, Sinan/0000-0003-2836-7181 WOS: 000171658200011 Poly(2-hydroxyethylmethacrylate) (pHEMA) based flat sheet membrane was prepared by UV-initiated photopolymerization technique. The membrane was then grafted with L-histidine. Catalase immobilization onto the membrane from aqueous solutions containing different amounts of catalase at different pH was investigated in a batch system. The maximum catalase immobilization capacity of the pHEMA-histidine membrane was 86 mug cm(-2). The activity yield was decreased with the increase of the enzyme loading. It was observed that there was a significant change between V-max value of the free catalase and V-max value of the adsorbed catalase on the pHEMA-histidine membrane. The K-m value of the immobilized enzyme was higher 1.5 times than that of the free enzyme. Optimum operational temperature was 5 degreesC higher than that of the free enzyme and was significantly broader. It was observed that enzyme could be repeatedly adsorbed and desorbed without loss of adsorption capacity or enzyme activity. (C) 2001 Elsevier Science B.V. All rights reserved. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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