多光谱图像
化学
食品科学
消化(炼金术)
色谱法
计算机科学
计算机视觉
作者
Chang Tan,Jiahe Zhu,Chenyang Shi,Xue Zhang,Lu Shan,Shan Wang,Chongting Guo,Chong Ning,Y. Y. Xue
出处
期刊:Food Chemistry
[Elsevier BV]
日期:2024-10-09
卷期号:464: 141586-141586
被引量:3
标识
DOI:10.1016/j.foodchem.2024.141586
摘要
Anthocyanins are susceptible to degradation owing to environmental factors. Combining them with proteins can improve their stability; however, the interaction mechanism is difficult to elucidate. This study used multispectral and molecular dynamics simulations and molecular docking methods to investigate the interaction mechanism between peanut protein isolate (PPI) and cyanidin-3-O-glucoside (C3G). The UV absorption peak and PPI turbidity increased, while the fluorescence intensity decreased with greater C3G content. Protein secondary structure changes suggested that PPI and C3G coexisted in spontaneous covalent and non-covalent interactions via static quenching. The complex structures were stable over time and C3G stably bound to the peanut globulin Ara h 3 cavity through hydrogen bonding and hydrophobic interactions. Furthermore, PPI enhanced the C3G antioxidant activity and bioaccessibility by increasing its retention rate during in-vitro simulated digestion. This study elucidates the binding mechanism of PPI and C3G and provides insight into applications of the complex in food development.
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