In vitro anti-tyrosinase activity of protein hydrolysate from spotted babylon (Babylonia areolata)

Abstract

Melanin is secreted by melanocyte cells distributed in the basal layer of the dermis. Melanin plays an important role in protecting human skin from the harmful effects of ultra violet radiation. Tyrosinase is the key enzyme in melanin biosynthesis. In case of over-activity can lead to dermatological disorder. The aim of this study was to investigate new tyrosinase inhibitors of protein hydrolysate from spotted babylon. Protein hydrolysate was fractionated by ultrafiltration, MW < 5,000 Da showed the potency as tyrosinase inhibitor with IC₅₀ value of 0.075±0.004 μg/ml using L-DOPA as substrate which are strong about four times than the positive control kojic acid (IC₅₀ = 0.251±0.007 μg/ml). The tyrosinase inhibitory activity effect from retentate of 5 kDa membrane of spotted babylon protein hydrolysate was moderately thermostable (showed maximum tyrosinase inhibitory activity about 90°C with 68% for 30 min), showed 50% activity across a broad pH range of 3–12. In order to know the compounds responsible for tyrosinase inhibitory activities, the identification and characterization of protein hydrolysates of spotted babylon are currently underway in our laboratory. The search for more potent tyrosinase inhibitors from protein hydrolysate are still needed for the treatment of various dermatological disorders and are also applied as cosmetic whitening agents.