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Occurrence of trans monounsaturated and polyunsaturated fatty acids in Colwellia psychrerythraea strain 34H
Author(s) -
Hashimoto Mikako,
Orikasa Yoshitake,
Hayashi Hidenori,
Watanabe Kentaro,
Yoshida Kiyohito,
Okuyama Hidetoshi
Publication year - 2015
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.201400815
Subject(s) - psychrophile , polyunsaturated fatty acid , biochemistry , strain (injury) , docosahexaenoic acid , fatty acid , bacteria , enzyme , chemistry , biology , food science , genetics , anatomy
Colwellia psychrerythraea strain 34H is an obligately psychrophilic bacterium that has been used as a model cold‐adapted microorganism because of its psychrophilic growth profile, significant production of cold‐active enzymes, and cryoprotectant extracellular polysaccharide substances. However, its fatty acid components, particularly trans unsaturated fatty acids and long‐chain polyunsaturated fatty acids (LC‐PUFAs), have not been fully investigated. In this study, we biochemically identified Δ9‐ trans hexadecenoic acid [16:1(9t)] and LC‐PUFAs such as docosahexaenoic acid. These results are comparable with the fact that the strain 34H genome sequence includes pfa and cti genes that are responsible for the biosynthesis of LC‐PUFAs and trans unsaturated fatty acids, respectively. Strain 34H cells grown under static conditions at 5 °C had higher levels of 16:1(9t) than those grown under shaken conditions, and this change was accompanied by an antiparallel decrease in the levels of Δ9‐ cis hexadecenoic acid [16:1(9c)], suggesting that the cis ‐to‐ trans isomerization reaction of 16:1(9c) is activated under static (microanaerobic) culture conditions, that is, the enzyme could be activated by the decreased dissolved oxygen concentration of cultures. On the other hand, the levels of LC‐PUFAs were too low (less than 3% of the total), even for cells grown at 5 °C, to evaluate their cold‐adaptive function in this bacterium.