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Puttaporn Pongkai,Tanatorn Saisavoey,Papassara Sangtanoo,Polkit Sangvanich,Aphichart Karnchanatat 한국식품과학회 2017 Food Science and Biotechnology Vol.26 No.5
Tyrosinase is a copper-containing enzyme that controls mammalian melanogenesis. Tyrosinase inhibitors are important for their potential application in cosmetic products. Chicken feather meal is a rich source of amino acids, which have been linked with tyrosinase inhibition activity. This study investigated the tyrosinase inhibitory properties of protein hydrolysates prepared from chicken feather meal. Protein hydrolysates prepared by pepsinpancreatin with MW \3 kDa exhibited strong tyrosinase inhibition activity for both monophenolase (IC50 5.780 ± 0.188 lg/mL) and diphenolase activities (IC50 0.040 ± 0.024 lg/mL) in a cell-free mushroom tyrosinase system. These samples were uncompetitive inhibitors with Ki values of 18.149 and 27.189 lg/mL in monophenolase and diphenolase activities, respectively. A cell culture model showed that this hydrolysate had the strongest inhibition on the viability of B16F10 cells (IC50 1.124 ± 0.288 lg/mL) and 0.210 lg/mL of the sample exhibited inhibition of tyrosinase activity by 50.493% and melanin synthesis by 14.680% compared to the control.