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Immobilization of acetylcholinesterase and choline oxidase in/on pHEMA membrane for biosensor construction.

Immobilization of acetylcholinesterase and choline oxidase in/on pHEMA membrane for biosensor construction. Research Abstract Details 

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  • Immobilization of acetylcholinesterase and choline oxidase in/on pHEMA membrane for biosensor construction. Abstract Text:

    f n kokF N Kok,f bozogluF Bozoglu,v hasirciV Hasirci,

    In this study, acetylcholinesterase (AChE) and choline oxidase (ChO) were co-immobilized on poly(2-hydroxyethyl methacrylate) (pHEMA) membranes with the aim of using them in biosensor construction. pHEMA membranes were prepared with the addition of different salts in different HEMA: aqueous solution ratios and characterized in terms of porosity, thickness. permeability, and mechanical properties. Membranes prepared in the presence of SnCl4 were found to be superior in terms of porosity and permeability and were chosen as the immobilization matrix. Immobilization of the enzymes was achieved both by entrapment and surface attachment via epichlorohydrin (Epi) and Cibacron Blue F36A (CB) activation. The effect of immobilization on enzyme activity was evaluated by the comparison of Km and Vmax values for the free and immobilized bi-enzyme systems. The increase in Km was negligible (1.08-fold) for the bi-enzyme system upon immobilization on surface but was 2.12-fold upon entrapment. Specific activity of the free enzyme system was found to be 0.306 mV s(-1) microg(-1) ChO while it was 0.069 (4.43-fold decrease) for entrapped and 0.198 (1.54 fold decrease) for CB-Epi immobilized enzymes. The performance of immobilized enzymes in different buffer types, pH, and temperature conditions were evaluated. The best enzyme activity was obtained at pH 9.0. Activity of the enzymes was found to increase with increasing temperature (in the range 25-40 degrees C).

    Immobilization of acetylcholinesterase and choline oxidase in/on pHEMA membrane for biosensor construction. Publishing Authors By Initials

    fn kokFN Kok,f bozogluF Bozoglu,v hasirciV Hasirci,

    For similar inorganic chemicals: tin compounds research abstracts see: inorganic chemicals: tin compounds research

    PUBMED ID PMID:

    MEDLINE DATE:

    Immobilization of acetylcholinesterase and choline oxidase in/on pHEMA membrane for biosensor construction. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of biomaterials science. Polymer edition

    VOLUME: 12

    Page Numbers: 1161-76

    Journal Abbreviation:

    ISSN: 0920-5063

    DAY: 20

    MONTH: 02

    YEAR: 2001

    Immobilization of acetylcholinesterase and choline oxidase in/on pHEMA membrane for biosensor construction. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 9007393

    Immobilization of acetylcholinesterase and choline oxidase in/on pHEMA membrane for biosensor construction. Keywords Mesh Terms:

    KEYWORDS: Tin Compounds

    MESH TERMS: chemistry

    Chemical & Substance for Abstract: Immobilization of acetylcholinesterase and choline oxidase in/on pHEMA membrane for biosensor construction. Information

    Substance Name: Acetylcholinesterase

    Registry Number: EC 3.1.1.7

    Grant and Affiliation Information for Immobilization of acetylcholinesterase and choline oxidase in/on pHEMA membrane for biosensor construction.

    AFFILIATION: Middle East Technical University, Department of Biological Sciences and Biotechnology, Ankara, Turkey.

    Country: Netherlands

    Netherlands Research PublicationNetherlands Research Publication

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    GRANT:

    ACRONYM:

    MEDLINETA: J Biomater Sci Polym Ed

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