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• W4366352948 abstract "Plasmalogens are a subclass of glycerophospholipids that have a vinyl-ether bond at the sn-1 position and are thought to have several physiological functions. The creation of non-natural plasmalogens with functional groups is desired for the establishment of the prevention of diseases caused by the depletion of plasmalogens. Phospholipase D (PLD) has both hydrolysis and transphosphatidylation activities. In particular, PLD from Streptomyces antibioticus has been investigated extensively due to its high transphosphatidylation activity. However, it has been difficult to stably express recombinant PLD in Escherichia coli and to express it as a soluble protein. In this study, we used the E. coli strain, SoluBL21™, and achieved stable PLD expression from the T7 promoter and increased soluble fraction in the cell. We also improved the purification method of PLD using His-tag at the C terminus. We obtained PLD with ∼730 mU mg-1 protein of specific activity, and the yield was ∼420 mU l-1 culture, corresponding to 76 mU per gram of wet cells. Finally, we synthesized a non-natural plasmalogen with 1,4-cyclohexanediol bound to the phosphate group at the sn-3 position by transphosphatidylation of the purified PLD. This method will contribute to the expansion of the chemical structure library of non-natural plasmalogens." @default.
• W4366352948 created "2023-04-21" @default.
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• W4366352948 date "2023-04-01" @default.
• W4366352948 modified "2023-09-29" @default.
• W4366352948 title "Improvement of solubility of phospholipase D from <i>Streptomyces antibioticus</i> in recombinant <i>Escherichia coli</i> and its application for the enzymatic synthesis of a non-natural plasmalogen" @default.
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• W4366352948 doi "https://doi.org/10.1093/lambio/ovad049" @default.
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• W4366352948 hasPublicationYear "2023" @default.
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