HOME | LOGIN | MEMBER JOIN | CONTACT US | ENGLISH

Food Science and Biotechnology
→ Food Science and Biotechnology 2017 ; 26(5): 1199-1208
Effects of protein hydrolysate from chicken feather meal on tyrosinase activity and melanin formation in B16F10 murine melanoma cells
Puttaporn Pongkai1, Tanatorn Saisavoey2, Papassara Sangtanoo2, Polkit Sangvanich3, Aphichart Karnchanatat2
1Program in Biotechnology, Faculty of Science, Chulalongkorn University, 254 Phayathai Road, Pathumwan, Bangkok 10330, Thailand, 2Institute of Biotechnology and Genetic Engineering, Chulalongkorn University, 254 Phayathai Road, Pathumwan, Bangkok 10330, Thailand, 3Departmaent of Chemistry, Faculty of Science, Chulalongkorn University, 254 Phayathai Road, Pathumwan, Bangkok 10330, Thailand
ABSTRACT
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 pepsin-pancreatin with MW <3 kDa exhibited strong tyrosinase inhibition activity for both monophenolase (IC50 5.780 ± 0.188 µg/mL) and diphenolase activities (IC50 0.040 ± 0.024 µg/mL) in a cell-free mushroom tyrosinase system. These samples were uncompetitive inhibitors with Ki values of 18.149 and 27.189 µg/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 µg/mL) and 0.210 µg/mL of the sample exhibited inhibition of tyrosinase activity by 50.493% and melanin synthesis by 14.680% compared to the control.
KEYWORD
Chicken feather meal, Tyrosinase inhibition, Protein hydrolysates, Melanogenesis
Food Science and Biotechnology 2017 ; 26(5): 1199-1208
List