期刊
JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC
卷 117, 期 -, 页码 7-12出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.molcatb.2015.03.020
关键词
Lactic acid bacteria; Hydroxy fatty acid; Oxo fatty acid; Short-chain dehydrogenase/reductase
资金
- Industrial Technology Research Grant Program [07A08005a]
- New Energy and Industrial Technology Development Organization (NEDO) of Japan
- Centers of Excellence for Microbial-Process Development Pioneering Future Production Systems from the Ministry of Education, Culture, Sports, Science, and Technology of Japan [J13]
- Bio-Oriented Technology Research Advancement Institution of Japan
- Science and Technology Promotion Program for Agriculture Forestry, Fisheries and Food Industry from the Ministry of Agriculture, Forestry and Fisheries of Japan [26002A]
- Advanced Low Carbon Technology Research and Development Program of Japan
- Japan Society for the Promotion of Science for Young Scientists [26686, 1401985]
- [19780056]
- [16688004]
- [18208009]
- Grants-in-Aid for Scientific Research [15H02441, 14J00686] Funding Source: KAKEN
Hydroxy fatty acid dehydrogenase, which is involved in polyunsaturated fatty acid saturation metabolism in Lactobacillus plantarum AKU 1009a, was cloned, expressed, purified, and characterized. The enzyme preferentially catalyzed NADH-dependent hydrogenation of oxo fatty acids over NAD(+)-dependent dehydrogenation of hydroxy fatty acids. In the dehydrogenation reaction, fatty acids with an internal hydroxy group such as 10-hydroxy-cis-12-octadecenoic acid, 12-hydroxy-cis-9-octadecenoic acid, and 13-hydroxy-cis-9-octadecenoic acid served as better substrates than those with alpha- or beta-hydroxy groups such as 3-hydroxyoctadecanoic acid or 2-hydroxyeicosanoic acid. The apparent Km value for 10-hydroxy-cis-12-octadecenoic acid (HYA) was estimated to be 38 mu M with a k(cat) of 7.6 x 10(-3) s(-1). The apparent K-m value for 10-oxo-cis-12-octadecenoic acid (KetoA) was estimated to be 1.8 mu M with a k(cat) of 5.7 x 10(-1) s(-1). In the hydrogenation reaction of KetoA, both (R)- and (S)-HYA were generated, indicating that the enzyme has low stereoselectivity. This is the first report of a dehydrogenase with a preference for fatty acids with an internal hydroxy group. (C) 2015 Elsevier B.V. All rights reserved.
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