دورية أكاديمية
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Chicken Egg White-Advancing from Food to Skin Health Therapy: Optimization of Hydrolysis Condition and Identification of Tyrosinase Inhibitor Peptides.

التفاصيل البيبلوغرافية
العنوان: Chicken Egg White-Advancing from Food to Skin Health Therapy: Optimization of Hydrolysis Condition and Identification of Tyrosinase Inhibitor Peptides.
المؤلفون: Yap PG; Analytical Biochemistry Research Centre, Universiti Sains Malaysia, Penang 11800, Malaysia., Gan CY; Analytical Biochemistry Research Centre, Universiti Sains Malaysia, Penang 11800, Malaysia.
المصدر: Foods (Basel, Switzerland) [Foods] 2020 Sep 18; Vol. 9 (9). Date of Electronic Publication: 2020 Sep 18.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: MDPI AG Country of Publication: Switzerland NLM ID: 101670569 Publication Model: Electronic Cited Medium: Print ISSN: 2304-8158 (Print) Linking ISSN: 23048158 NLM ISO Abbreviation: Foods Subsets: PubMed not MEDLINE
أسماء مطبوعة: Original Publication: Basel, Switzerland : MDPI AG, [2012]-
مستخلص: 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.
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معلومات مُعتمدة: 1001/CABR/8011045 Universiti Sains Malaysia
فهرسة مساهمة: Keywords: bioactive peptide; crossed D-optimal design; diphenolase inhibitory activity; egg white; monophenolase inhibitory activity; pigmentation; tyrosinase
تواريخ الأحداث: Date Created: 20200923 Latest Revision: 20201020
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC7555751
DOI: 10.3390/foods9091312
PMID: 32961904
قاعدة البيانات: MEDLINE
الوصف
تدمد:2304-8158
DOI:10.3390/foods9091312