SCREENING ACTIVE NATURAL LIGANDS OF TYROSINASE FROM Aglaonema simplex BL. BY HPLC
Keywords:Aglaonema simplex, arbutin, ligand, tyrosinase inhibitor, HPLC-DAD
Ethanol extract of Aglaonema simplex rhizomes exhibited higher monophenolase inhibitory activity than arbutin, with IC50 values of 53.65 ± 0.80 and 138.15 ± 0.96 μg/mL respectively, while diphenolase inhibitory activity values were similar to arbutin at 6.35 ± 0.23 and 7.11 ± 0.16 μg/mL respectively. Arbutin was used as a binding ligand for screening tyrosinase inhibitors using high performance liquid chromatography with a diode-array detector (HPLC-DAD). The analytical method was validated. The calibration curve of arbutin standard generated the regression equation, y = 25.356x – 167.65, r2 = 0.9991. The accuracy was presented in term the percentage recovery and was showed 99.70 to 102.45 %. The LOD and LOQ values were 37.74 and 114.37 µg/mL, respectively. Intra–day and inter–day precisions were presented in term the percentage of relative standard deviations and were in the range 0.07–0.13% and 0.002–0.01%, respectively. The optimized ligand screening at 37 °C and 40 min. Five unknown tyrosinase inhibitor binding ligands were identified in the ethanol extract of A. simplex rhizomes using HPLC-DAD with retention times of 13.95, 19.64, 21.30, 38.98 and 43.90 min, respectively. The result suggested that the extract of A. simplex rhizomes could be contained the marker compounds for the development of the extract in cosmeceuticals.
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