T2 - Journal of the Chemical Society, Perkin Transactions 1
JF - Journal of the Chemical Society, Perkin Transactions 1
The enzymatic glycosylation and phosphatidylation of biologically active compounds are described. Aromatic, monoterpene, and indole alcohols (benzyl alcohol and its related alcohols, geraniol, citronellol, f arnesol, geranyl-geraniol, and tryptophol) were glycosylated when these alcohols and cellobiose (or lactose) were incubated with Aspergillus niger R-glucosidase (or A, oryzae f-galactosidase), and all β-glycosylated compounds of these alcohols were odorless. A purified cyclo maltodextrin glucanotransferase (CGTase) from Bacillus stearothermophilus was found to catalyze the transfer reaction of the glucosyl residue from dextrin not only to CH2OH groups of the acceptors such as benzyl alcohol and its related alcohols, riboflavin (B2), pyridoxine (PN), thiamin (B1), and n-butyl alcohols with high efficiency, but also to the OH group at the inositol moiety of kasugamycin, at the C-4 positions of glucose moieties of ginsenosides Rc and. Rg1, and of n-octyl-a (Q) -glucoside at the C-3 position of fructose, and also to the OH group of sec- and tert-butyl alcohols, quercetin, and aromatic hydroxy compounds (vanillin, ethyl vanillin, phenol, pyrocatechol, pyrogallol, gallic acid, protocatechuicacid, sesamol) at a considerable efficiency, resulting all α-glucosides of these compounds except quercetin were isolated in crystalline and powder forms and characterized. B. stearothermophilus CGTase had relatively broad acceptor specificity. α-Glucosylated compounds of aromatic alcohols, vanillin, ethyl vanillin, and B1 were odorless. All glucosylated antioxidants were much more stable than aglycones against the oxidation by peroxidase in the presence of hydrogen peroxide. Phospholipase D from Streptomyces sp. (PLD) was observed to be highly active in transferring he dipalmitoylphosphatidyl (DPP-) residue from 1, 2-dipalmitoyl-3-sn-phosphatidylcholine (DPPC) to the CH2OH group in the acceptors such as vitamins (B1, B2, PN, pantothenic acid, B1 disulfide-related compounds), arbutin, kojic acid, genipin, and dihydroxyacetone in a biphasic system. DPP-arbutin and DPP-kojic acid showed the same inhibitory activity to tyrosinase as arbutin and kojic acid, respectively. DPP-genipin showed 6-52 times stronger cytotoxity than genipin to HeLa, HEL, and MT-4 cells. DPP-genipin was found to react with L-phenylalanine in organic solvents to give a clear blue solution having a similar color to an aqueous solution of the natural blue pigment "gardenia blue." This is the first example for the preparation of hydrophobic pigment from a phosphatidyl derivative of a water soluble compound. Moreover, the PLD was first found to bring about the transfer of DPP-residue from DPPC to aromatic hydroxy group of acceptors such as various phenols, naphthol, and 5-hydroxyindole in a biphasic system of an organic solvent with low water solubility and buffer. Immobilized PLD with Amberlite IRC-50 retained 74% of its initial activity after 10 times-repeated batch reaction for DPPcompound synthesis.
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