Abstract
Active fragments (bioactive peptides) from the chicken egg white proteins were expected to exert tyrosinase inhibitory activities in which skin hyperpigmentation could be prevented. Egg white was hydrolyzed by trypsin, chymotrypsin and the combination of both enzymes. The enzyme treatments achieved >50% degree of hydrolysis (DH) at substrate-to-enzyme (S/E) ratio of 10–30 (w/w) and hydrolysis time of 2–5 h. A crossed D-optimal experimental design was then used to determine the optimal enzyme composition, S/E ratio and hydrolysis time in order to yield hydrolysates with strong monophenolase and diphenolase inhibitory activities. The optimized conditions 55% trypsin, 45% chymotrypsin, S/E 10:1 w/w and 2 h achieved 45.9% monophenolase activity inhibition whereas 100% trypsin, S/E 22.13:1 w/w and 3.18 h achieved 48.1% diphenolase activity inhibition. LC/MS and MS/MS analyses identified the peptide sequences and the subsequent screening had identified 7 peptides (ILELPFASGDLLML, GYSLGNWVCAAK, YFGYTGALRCLV, HIATNAVLFFGR, FMMFESQNKDLLFK, SGALHCLK and YFGYTGALR) as the potential inhibitor peptides. These peptides were able to bind to H85, H94, H259, H263, and H296 (hotspots for active residues) as well as F92, M280 and F292 (stabilizing residues) of tyrosinase based on structure-activity relationship analysis. These findings demonstrated the potential of egg white-derived bioactive peptides as skin health therapy.
Highlights
The excess melanin production and deposition in the melanocytes and keratinocytes cause hyperpigmentation, leading to uneven skin tones
MW ranging from 11–48 kDa and >245 kDa were observed in control treatments (L1)
The >245 kDa bands were absent after enzymatic hydrolysis, suggesting the successful cleavage of large molecular weight proteins ovomucin and ovomacroglobulin into smaller protein fragments
Summary
The excess melanin production and deposition in the melanocytes and keratinocytes cause hyperpigmentation, leading to uneven skin tones. Tyrosinase (E.C. 1.14.18.1) plays a key role in melanin synthesis (melanogenesis) by catalyzing the rate-limiting hydroxylation of l-tyrosine to. The inhibition of tyrosinase using a nature-derived agent is of huge cosmeceutical demand, as some potent skin-lightening ingredients including hydroquinone and heavy metals have been ascribed with harmful side effects and banned for use in certain countries [2,3]. Since the discovery of a potential protein or peptide with tyrosinase inhibitory activity from lemon skin extract in 2006 [4], reports on peptide-based skin lightening agents has increased by leaps and bounds. The anti-pigmentation mechanisms of peptides include tyrosinase inhibition [5], copper chelation [6] and melanogenesis pathway regulation [7]. Peptide was incorporated as an active ingredient in commercial skin lightening products such as
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