Coenzyme production using immobilized enzymes. I. Preparation, characterization, and laboratory-scale application of an immobilized NAD kinase |
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Authors: | L M Simon M Kotorm n and B Szaj ni |
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Institution: | 1 Department of Biochemistry, Attila József University, Szeged, Hungary * Reanal Factory of Laboratory Chemicals, Budapest, Hungary |
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Abstract: | NAD+ kinase (ATP: NAD+ 2-phosphotransferase, EC2.7.1.23) isolated from chicken liver was immobilized on a silica-based support possessing aldehyde functional groups. The highest catalytic activity achieved was 16 U g?1 solid. The optimal pH for the catalytic activity of the immobilized NAD+ kinase was pH 7.1–7.3. The apparent optimum temperature for the immobilized enzyme was about 5°C higher than that of the soluble enzyme. There were no significant differences in the Km app values. The immobilization improved the conformational stability of the enzyme. In preliminary experiments, a 95% conversion of NAD+ to NADP+ was achieved with use of the immobilized NAD+ kinase, which preserved its starting activity practically unchanged up to 36 days. |
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Keywords: | NAD+ kinase immobilized silica-based support NADP+ continuous production |
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