دورية أكاديمية

Structural modifications and augmented affinity for bile salts in enzymatically denatured egg white

التفاصيل البيبلوغرافية
العنوان: Structural modifications and augmented affinity for bile salts in enzymatically denatured egg white
المؤلفون: Chunjie Liu, Yating Wu, Guoguo Jin, Baocai Xu, Lin Mei
المصدر: Food Chemistry: X, Vol 23, Iss , Pp 101577- (2024)
بيانات النشر: Elsevier, 2024.
سنة النشر: 2024
المجموعة: LCC:Nutrition. Foods and food supply
LCC:Food processing and manufacture
مصطلحات موضوعية: Egg white protein, Bile salts binding ability, In vitro simulation of gastrointestinal digestion, Structure-activity relationship, Nutrition. Foods and food supply, TX341-641, Food processing and manufacture, TP368-456
الوصف: Protein binding to bile salts (BSs) reduces cholesterol levels, but the exact mechanism is unclear. In this study, we performed simulated gastrointestinal digestion of egg white protein hydrolysate (EWPHs) and included an unenzyme digestion group (CK) to investigate the changes in BSs binding capacity before and after digestion, as well as the relationship between egg white protein (EWP) structure and BSs binding capacity. In addition, peptidomics and molecular docking were used to clarify EWP's binding mechanism. We found that the BSs binding ability of EWPHs was slightly decreased after digestion, but significantly higher than that of the CK group and the digested CK group (D-CK). Particle size analysis and electrophoresis demonstrated that smaller particles and lower molecular weights exhibited enhanced binding capacity to BSs. Fourier Transform infrared spectroscopy (FTIR) results revealed that a disordered structure favored BS binding ability enhancement. Peptides FVLPM and GGGVW displayed hypocholesterolemic efficacy.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 2590-1575
Relation: http://www.sciencedirect.com/science/article/pii/S2590157524004656; https://doaj.org/toc/2590-1575
DOI: 10.1016/j.fochx.2024.101577
URL الوصول: https://doaj.org/article/b4853d13d9344169bf755349bafc6a4b
رقم الأكسشن: edsdoj.b4853d13d9344169bf755349bafc6a4b
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:25901575
DOI:10.1016/j.fochx.2024.101577