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篇目详细内容

【篇名】 Distributions of phospholipid and glycolipid fatty acids in two strains of different functional Erythrobacter sp. isolated from South China Sea
【刊名】 Frontiers of Earth Science in China
【刊名缩写】 Front. Earth Sci. China
【ISSN】 1673-7385
【EISSN】 1673-7490
【DOI】 10.1007/s11707-009-0009-5
【出版社】 Higher Education Press and Springer-Verlag
【出版年】 2009
【卷期】 3 卷1期
【页码】 91-99 页,共 9 页
【作者】 Huan YANG; Xiangru MA1; Qiang LI; Nianzhi JIAO; Shucheng XIE;
【关键词】 AAPB; PLFA; GLFA; hydroxy fatty acids; Erythrobacter

【摘要】
The comparison of the fatty acids between aerobic anoxygenic phototrophic bacteria (AAPB) and their phylogenetic relatives has been a fascinating but yet enigmatic topic, enhancing our understanding of physiological variations between these evolutionarily related microorganisms. Two strains of marine bacteria, both phylogenetically falling into Erythrobacter sp., were isolated from the South China Sea, and demonstrated, respectively, to be an aerobic anoxygenic phototrophic bacteria (AAPB) (JL475) which is capable of anoxygenic photosynthesis via BChl a, and an obligate heterotroph (JL316) with a lack of BChl a, on the basis of phylogenetic analysis and pure culture cultivation. Phospholipid fatty acids (PLFA) and glycolipid fatty acids (GLFA) of the two strains were extracted and analyzed by gas chromatography-mass spectrometry. The PLFA in JL475 AAPB are characterized by C18∶1, C18∶2ω7,13 and C18∶0, with the C18∶2ω7,13 being a specific compound for AAPB and in particular for Erythrobacter longus and some of its phylogenetically closely related relatives. The JL316 strain is characterized in PLFA by the presence of C18∶1, C16∶1 and C16∶0, and in particular C17∶1. GLFA do not show any discrimination between the two strains. Four α,ω-dicarboxylic acids, including 1,8-octanedioic acid, 1,9-nonanedioic acid, 1,10-decanedioic acid and 1,11-undecanedioic acid, are present only in JL316 GLFA, presumably derived from metabolic products. C14—C16 2-hydroxy fatty acids were found in the two strains, probably assuming a similar function of their LPS in outer membranes.
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