دورية أكاديمية
أعرض في EDS

Study on the interaction and functional properties of Dolichos lablab L. protein-tea polyphenols complexes.

التفاصيل البيبلوغرافية
العنوان: Study on the interaction and functional properties of Dolichos lablab L. protein-tea polyphenols complexes.
المؤلفون: Yang J; School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China., Zhao Y; School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China., Shan B; College of Animal Science and Technology, Nanjing Agricultural University, Nanjing 210095, China., Duan Y; School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China; Institute of Food Physical Processing, Jiangsu University, Zhenjiang 212013, China; Nourse Pet Nutrition Jiangsu Research Institute, Zhenjiang 212013, China. Electronic address: dyq101@ujs.edu.cn., Zhou J; School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China., Cai M; School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China., Zhang H; School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China. Electronic address: zhanghh@ujs.edu.cn.
المصدر: International journal of biological macromolecules [Int J Biol Macromol] 2023 Oct 01; Vol. 250, pp. 126006. Date of Electronic Publication: 2023 Jul 29.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Elsevier Country of Publication: Netherlands NLM ID: 7909578 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-0003 (Electronic) Linking ISSN: 01418130 NLM ISO Abbreviation: Int J Biol Macromol Subsets: MEDLINE
أسماء مطبوعة: Publication: Amsterdam : Elsevier
Original Publication: Guildford, Eng., IPC Science and Technology Press.
مواضيع طبية MeSH: Polyphenols*/chemistry , Dolichos*, Tea/chemistry ; Antioxidants/chemistry ; Binding Sites
مستخلص: Tea polyphenols (TP) and plant proteins are significant materials in the food industry, the interactions between them are beneficial for their stability, functional properties, and biological activity. In this study, the mechanism and interaction between Dolichos lablab L. protein (DLP) obtained from nine treatments and three tea polyphenol monomers (EGCG, ECG, and EGC) were investigated. The results showed that the fluorescence of DLP was noticeably quenched and exhibited static quenching after the addition of polyphenols. DLP exhibited 1-2 binding sites for EGCG and ECG, but weakly binding to EGC (<1). The binding sites of DLP-TP were found to be in close proximity to the tyrosine residues, primarily interacting through hydrophobic interactions, van der Waals forces, and hydrogen bonds. The antioxidant capacity of DLP-TP compound was significantly improved after digestion. ECG showed a strong resistance to intestinal digestion. Compared with ECG (653.456 μg/mL), the content of free tea polyphenols of 20/40 kHz-ECG after digestion was 732.42 μg/mL. DLP-TP complexes significantly improved the storage stability, thermal stability, and bioaccessibility of tea polyphenols. The interaction between TP and DLP, as a protein-polyphenol complex, has great potential for application in preparing emulsion delivery systems due to their antioxidant activity and improved stability.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2023 Elsevier B.V. All rights reserved.)
فهرسة مساهمة: Keywords: Antioxidant capacity; Dolichos lablab L. protein; Protein-polyphenol complex; Stability; Tea polyphenol
المشرفين على المادة: 0 (Polyphenols)
0 (Tea)
0 (Antioxidants)
تواريخ الأحداث: Date Created: 20230730 Date Completed: 20231023 Latest Revision: 20231023
رمز التحديث: 20240628
DOI: 10.1016/j.ijbiomac.2023.126006
PMID: 37517754
قاعدة البيانات: MEDLINE
الوصف
تدمد:1879-0003
DOI:10.1016/j.ijbiomac.2023.126006