摘要

The glycolipid synthase MG517 from Mycoplasma genitalium catalyzes the glucosyl transfer from UDPGIc to diacylglycerol producing glycoglycerolipids (GGL) (Andres et at., 2011). The enzyme was functional in E. coli accumulating GGL in the plasma membrane. A metabolic engineering strategy for GGL production was evaluated using this microorganism. To increase the levels of GGL precursors, UDPGIc and diacylglycerol, GalU and PlsC enzymes involved in their biosynthesis were overexpressed. Seven engineered strains were obtained containing different combinations of the mg517 with gall and plsC genes. Diacylglycerol synthesis showed to be limiting and the strain overexpressing MG517 and PlsC achieved the highest GGL yield. The new lipids were mono, di- and triglucosyldiacylglycerol with different acyl combinations in each compound. It indicates that the successive glucosyl transferase activities of MG517 have different acyl chain specificity for the acceptor substrate. GGL represented up to 6 mg per g of dry weight.

  • 出版日期2012-9

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