C. Virto et P. Adlercreutz, Two-enzyme system for the synthesis of 1-lauroyl-rac-glycerophosphate (lysophosphatidic acid) and 1-lauroyl-dihydroxyacetonephosphate, CHEM PHYS L, 104(2), 2000, pp. 175-184
A combination of two enzymes, phospholipase D (PL D) and C (PL C), was inve
stigated for the production of two lysophospholipids, 1-lauroyl-rac-glycero
phosphate (1-LGP) and 1-lauroyl-dihydroxyacetonephosphate (1-LDHAP). The hi
gh transphosphatidylation ability of phospholipase D from Streptomyces sp.
allowed the formation of 1-lauroyl-phosphatidylglycerol (1-LPG) and 1-lauro
yl-phosphatidyldihydroxyacetone (1-LPDHA) from phosphatidylcholine (PC) and
1-monolauroyl-rac-glycerol (1-MLG) and 1-lauroyl-dihydroxyacetone (1-MDHA)
, respectively. A two-phase system, diethyl ether/water, was chosen for the
convenience of the recovery of the water insoluble products. A similar two
-phase system was used for hydrolysis of the complex phospholipids by phosp
holipase C form Bacillus cereus, which released both lysophospholipids. Onl
y trace amounts of phosphatidic acid (PA) were detected showing that the en
zyme is highly selective for the release of the diacylglycerol and 1-lauroy
l-rac-glycerophosphate and 1-lauroyl-dihydroxyacetonephosphate. (C) 2000 El
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