Abstract
Phospholipase D (EC 3.1.4.4) from Streptomyces sp. Catalyzed the transfer reaction of the dipalmitoylphosphatidyl residue from 1, 2-dipalmitoyl-3-sn-phosphatidylcholine (DPPC) to both arbutin and kojic acid in a biphasic system, to afford 1, 2-dipalmitoyl-3-sn-phosphatidylarbutin (DPP-arbutin) and 1, 2-dipalmitoyl-3-sn-phosphatidylkojic acid (DPP-kojic acid), respectively. The transfer reaction of DPPC was accompanied by hydrolysis to phosphatidic acid, and the ratio was significantly affected with organic solvents used in the biphasic system. DPP-arbutin and DPP-kojic acid showed almost the same inhibitory activity to tyrosinase (EC 1.14.18.1) from mushroom as arbutin and kojic acid, respectively.
