等温滴定量热法
化学
没食子酸
没食子酸
没食子酸表没食子酸酯
表儿茶素没食子酸盐
生物化学
荧光
乳清蛋白
色谱法
滴定法
体外
核化学
抗氧化剂
多酚
有机化学
物理
量子力学
作者
Yanyun Cao,Youling L. Xiong
标识
DOI:10.1021/acs.jafc.7b03006
摘要
Preheated (80 °C for 9 min) whey protein isolate (HWPI) was reacted with 20, 120, and 240 μmol/g (protein basis) gallic acid (GA) or epigallocatechin gallate (EGCG) at neutral pH and 25 °C. Isothermal titration calorimetry and fluorometry showed a similar trend that GA binding to HWPI was moderate but weaker than EGCG binding. However, the shift of maximal fluorescence emission wavelength in opposite directions in response to GA (blue) and EGCG (red) suggests discrepant binding patterns. Electrophoresis results showed that EGCG induced formation of HWPI complexes while GA only had a marginal effect. Both free and phenolic-bound HWPI exhibited mild antiradical activity. However, when subjected to in vitro digestion, synergistic radical-scavenging activity was produced between the phenolics and peptides with the highest synergism being observed on 120 μmol/g phenolics.
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