碩士 / 國立臺灣海洋大學 / 食品科學系 / 92 / D-arabinose dehydrogenase (D-arabinose : NADP+ 1-oxidoreductase EC 1. 1. 1. 117) was purified 295-fold from grouper liver with a recovery of 22.43 %. The enzyme was purified by a procedure involving a mmonium sulfate precipitation, DE-52 chromatography, Sepharose CL-6B chromatography, and Sephacryl S-300 chromatography. The purified enzyme gave one band with a molecular mass of 30.6 kDa on SDS-PAGE. The native enzyme had a molecular mass of 117.7 kDa as estimated by Sephacryl S-300 chromatography. The results suggest that this enzyme was a tetramer, comprising four identical 30.6kDa subunits. D-arabinose dehydrogenase used NADP+ as a coenzyme. The purified enzyme exhibited maximum activity at pH 9.2 and optimum temperature at 53℃. In addition, the enzyme was more unstable in the acidic pH and lost activity rapidly at temperature higher than 35℃. The apparent Km value was 0.14 mM for D-arabinose and 0.007 mM for NADP+. The Vmax values for D-arabinose and NADP+ were 0.47 μmole/min and 0.49 μmole/min, respectively. The activity of the enzyme was inhibited by Cr3+, Ni2+, Cu2+, Zn2+, Cd2+, Hg2+, NBS, PCMBS, and phnylglyoxal hydrate and NADPH caused feedback inhibition on D-arabinose dehydrogenase.
| Identifer | oai:union.ndltd.org:TW/092NTOU5253009 |
| Date | January 2004 |
| Creators | Hsin-Yi Huang, 黃欣怡 |
| Contributors | Pen-Hsing Tung, 童本興 |
| Source Sets | National Digital Library of Theses and Dissertations in Taiwan |
| Language | zh-TW |
| Detected Language | English |
| Type | 學位論文 ; thesis |
| Format | 82 |
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