Inhibitory Activities of Protein Hydrolysates from Spotted Babylon Snails on Tyrosinase and Melanogenesis. Issue 7 (9th August 2018)

• Record Type: Journal Article
• Authors: Prakot, Phanuwat; Chaitanawisuti, Ninnaj; Sangtanoo, Papassara; Saisavoey, Tanatorn; Karnchanatat, Aphichart
• Is Part Of: Journal of aquatic food product technology. Volume 27:Issue 7(2018)
• Page Start: 811
• Page End: 829
• Publication Date: 2018-08-09
• Subjects: Protein hydrolysate -- spotted babylon -- Babylonia areolata -- anti-tyrosinase -- melanogenesis; Fishery processing -- Periodicals; Animal products -- Periodicals; Plant products -- Periodicals; 664.9405
• DOI: 10.1080/10498850.2018.1499687
• Languages: English
• ISSNs: 1049-8850

Abstract

ABSTRACT: The optimal conditions for protein hydrolysates preparation from spotted babylon Babylonia areolata exhibiting tyrosinase inhibitory activity and antioxidant activity using alkaline protease (Protease G6) were undiluted Protease G6 (5.8 × 10 5 DU/g) at 60 min of hydrolysis time and eightfold diluted Protease G6 (7.25 × 10 4 DU/g) at 240 min of hydrolysis time. These two conditions were fractioned using molecular weight (MW) cutoff values of 10, 5, and 3 kDa membranes, and their anti-melanogenic and antioxidant properties were further analyzed. Among the fractions, the MW < 3 kDa fraction exhibited high levels of inhibitory activity toward the mono- and diphenolase activities of tyrosinase, with IC50 values of 1.758 and 8.995 μg/mL, respectively. Kinetic studies revealed that this fraction behaved as an uncompetitive inhibitor. The results demonstrated that the MW < 3 kDa fraction suppressed melanin synthesis and decreased cellular tyrosinase activity with no cytotoxicity to B16F10 melanoma cells.