关键词: 茶黄素, 表没食子儿茶素没食子酸酯, 表面等离子共振仪, 人唾液α-淀粉酶

Abstract:

Objective To explore the driving force of the oral astringency produced by the interaction of theaflavin（TF） and epigallocatechin-3-gallate（EGCG） to human salivary α-amylase（HSA）. Methods The constants of the rate, equilibrium of reaction（ka, kd , KA, and KD） and Langmuir, Freundlich adsorption isotherm（KL, Kf, and Mm） were determined by surface plasmon resonance（SPR） technique and adsorption kinetics. Results Both of Langmuir and Freundlich models could be used for describing the binding processes of TF and EGCG onto HSA surfaces, and there were no significant differences of the correlation coefficient of determination between these two models（P>0.05）. The constants of adsorption isotherm, the rate and equilibrium constants of the association for TF were higher than those of EGCG（P<0.05）. The rate and equilibrium constants of the dissociation for TF were lower than those of EGCG（P<0.05）. The affinity of TF to HSA was higher than that of EGCG. Conclusion The sorely oral astringency is much easily produced by TF from the black tea rather than EGCG from the green tea. The driving force of the oral astringency is attributed to the hydrogen bonds of hydroxyl groups and hydrophobic interaction of galloyl groups in polyphenolic structures.

Key words: theaflavin, epigallocatechin-3-gallate, surface plasmon resonance, human salivary α-amylase