明胶
化学
右旋糖酐
石英晶体微天平
酪蛋白
卵清蛋白
美拉德反应
色谱法
有机化学
高分子化学
吸附
免疫系统
免疫学
生物
作者
Yunfeng Yan,Jinhua Hu,Ping Yao
出处
期刊:Langmuir
[American Chemical Society]
日期:2008-12-03
卷期号:25 (1): 397-402
被引量:47
摘要
Tea polyphenols (TPPs) can bind with proteins and peptides through hydrophobic interaction and hydrogen bonding. Casein, ovalbumin, and dextran were used to investigate their influence on the interactions between TPP and gelatin and, therefore, to investigate their influence on TPP taste. Casein-g-dextran (CgD) and ovalbumin-g-dextran (OgD) grafting conjugates were prepared through the Maillard reaction. Dispersible CgD/OgD−TPP complexes formed in acidic pH solution even after a heating process. At the same weight ratio of protein to TPP, about 20−30% of TPP was bound to the proteins. TPP affinity for dextran is much lower. Gelatin, a model of the salivary proteins in buccal cavity, was immobilized on quartz crystal sensor surface through covalent bond. By use of a quartz crystal microbalance with dissipation, we found that the complexation of TPP with gelatin causes a dehydration and collapse of the gelatin layer on the sensor surface that is similar to the sensation of dryness and constriction on oral membranes caused by polyphenols. The complexation between TPP and casein/ovalbumin/dextran can decrease the interaction between TPP and gelatin by decreasing the free TPP molecules and shielding gelatin surface from TPP. Casein has stronger binding ability on the gelatin surface compared to ovalbumin and dextran, and therefore casein is more effective to decrease the sensation of astringency caused by TPP.
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