Purification and Some Properties of 2-Alkenal Reductase1 of Mucor griseo-cyanus AHU6044
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概要
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A 2-alkenal reductase, which catalyzes the reduction of sorbaldehyde (trans-2, trans-4- hexadienal) to trans-4-hexenal, was purified from Mucor griseo-cyanus by dialysis against an acidic buffer solution (pH 5.2), salting-out fractionation with ammoniumsulfate, chromatography on DEAE-Sephadex, preparative disc electrophoresis, and gel filtration on Bio-Gel P-75. A 2-alkenal reductase of a microorganismwas purified for the first time. The molecular weight was estimated to be 2.6 x 104 by SDS-disc electrophoresis, and the optimum pH was found to be 6.5. The enzyme was dependent on both NADPHand NADH, and was specific for cis-2-heptenal and -octenal in a series of 2-alkenals, trans-2-alkenals (C4, C6-C10 and C12), cis-2-alkenals (C7 and C8), acrolein, and trans-2-cinnamaldehyde.
- 社団法人 日本農芸化学会の論文
著者
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Tahara Satoshi
Department Of Agricultural Chemistry Faculty Of Agriculture Hokkaido University
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Mizutani Junya
Department Of Agricultural Chemistry Faculty Of Agriculture Hokkaido University
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Chiba Seiya
Department Of Agricultural Chemistry Faculty Of Agriculture Hokkaido University
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MATSUI Hirokazu
Department of Agricultural Chemistry, Faculty of Agriculture, Hokkaido University
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MIYAMURA Naohiro
Department of Agricultural Chemistry, Faculty of Agriculture, Hokkaido University
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