Influence of tea polyphenol and bovine serum albumin on tea cream formation by multiple spectroscopy methods and molecular docking

• Published in: Food chemistry 2020-12, Vol.333, p.127432-127432, Article 127432
• Main Authors: Yu, Xia, Cai, Xinghong, Luo, Liyong, Wang, Jie, Ma, Mengjun, Wang, Min, Zeng, Liang
• Format: Article
• Language: English
• Subjects: Fluorescence spectroscopy; Interaction; Molecular docking; Tea polyphenols; TOPSIS
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/j.foodchem.2020.127432

•The optimal solution (TPs = 800 mg/L, BSA = 40 mg/L) was gained by TOPSIS method.•EGCG and ECG had more bind abilities to interact with BSA than EGC and EC.•The quenching mechanism of BSA against EGCG, ECG, EGC, and EC is static quenching.•Hydrogen bonds were the main driving force between TPs and BSA in this condition. The sensory qualities and shelf life of tea beverage strongly affected by tea cream that forms by the interaction of polyphenols and protein. The study aimed to investigate the effects of the interactions between tea polyphenols (TPs) and bovine serum albumin (BSA) on tea cream formation at different concentrations. The tea cream formation increased with TPs and BSA concentration increased. The optimal concentration (TPs: 800 mg/L, BSA: 40 mg/L), for high clarities and contents of phytochemicals, was selected by the technique for order preference by similarity to ideal solution (C = 0.7572). The interaction mechanism of TPs-BSA was investigated by fluorescence spectroscopy, UV–visible absorption spectroscopy, synchronous fluorescence spectroscopy, and molecular docking. TPs interacted with BSA via static quenching process, affecting tryptophan and tyrosine residue microenvironment of BSA. Ester catechins had more binding affinity than non-ester catechins. Hydrogen bonds were the main interaction forces of TPs-BSA.