Chicken Egg White—Advancing from Food to Skin Health Therapy: Optimization of Hydrolysis Condition and Identification of Tyrosinase Inhibitor Peptides
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...
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doaj-7481a7f3f6ae4849ae4318b45e0cd08f2020-11-25T03:24:55ZengMDPI AGFoods2304-81582020-09-0191312131210.3390/foods9091312Chicken Egg White—Advancing from Food to Skin Health Therapy: Optimization of Hydrolysis Condition and Identification of Tyrosinase Inhibitor PeptidesPei-Gee Yap0Chee-Yuen Gan1Analytical Biochemistry Research Centre, Universiti Sains Malaysia, Penang 11800, MalaysiaAnalytical Biochemistry Research Centre, Universiti Sains Malaysia, Penang 11800, MalaysiaActive 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 (<i>w</i>/<i>w</i>) 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 <i>w</i>/<i>w</i> and 2 h achieved 45.9% monophenolase activity inhibition whereas 100% trypsin, S/E 22.13:1 <i>w</i>/<i>w</i> 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.https://www.mdpi.com/2304-8158/9/9/1312bioactive peptidecrossed D-optimal designdiphenolase inhibitory activityegg whitemonophenolase inhibitory activitypigmentation |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Pei-Gee Yap Chee-Yuen Gan |
spellingShingle |
Pei-Gee Yap Chee-Yuen Gan Chicken Egg White—Advancing from Food to Skin Health Therapy: Optimization of Hydrolysis Condition and Identification of Tyrosinase Inhibitor Peptides Foods bioactive peptide crossed D-optimal design diphenolase inhibitory activity egg white monophenolase inhibitory activity pigmentation |
author_facet |
Pei-Gee Yap Chee-Yuen Gan |
author_sort |
Pei-Gee Yap |
title |
Chicken Egg White—Advancing from Food to Skin Health Therapy: Optimization of Hydrolysis Condition and Identification of Tyrosinase Inhibitor Peptides |
title_short |
Chicken Egg White—Advancing from Food to Skin Health Therapy: Optimization of Hydrolysis Condition and Identification of Tyrosinase Inhibitor Peptides |
title_full |
Chicken Egg White—Advancing from Food to Skin Health Therapy: Optimization of Hydrolysis Condition and Identification of Tyrosinase Inhibitor Peptides |
title_fullStr |
Chicken Egg White—Advancing from Food to Skin Health Therapy: Optimization of Hydrolysis Condition and Identification of Tyrosinase Inhibitor Peptides |
title_full_unstemmed |
Chicken Egg White—Advancing from Food to Skin Health Therapy: Optimization of Hydrolysis Condition and Identification of Tyrosinase Inhibitor Peptides |
title_sort |
chicken egg white—advancing from food to skin health therapy: optimization of hydrolysis condition and identification of tyrosinase inhibitor peptides |
publisher |
MDPI AG |
series |
Foods |
issn |
2304-8158 |
publishDate |
2020-09-01 |
description |
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 (<i>w</i>/<i>w</i>) 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 <i>w</i>/<i>w</i> and 2 h achieved 45.9% monophenolase activity inhibition whereas 100% trypsin, S/E 22.13:1 <i>w</i>/<i>w</i> 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. |
topic |
bioactive peptide crossed D-optimal design diphenolase inhibitory activity egg white monophenolase inhibitory activity pigmentation |
url |
https://www.mdpi.com/2304-8158/9/9/1312 |
work_keys_str_mv |
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