醇溶蛋白
共价键
化学
等温滴定量热法
有机化学
生物化学
贮藏蛋白
基因
作者
Yuanjing Sun,Zihao Wei
出处
期刊:Food Chemistry
[Elsevier]
日期:2024-04-10
卷期号:449: 139273-139273
被引量:1
标识
DOI:10.1016/j.foodchem.2024.139273
摘要
The objectives of this study were to modify hordein with gallic acid (GA) in alcohol-free media and to compare the impact of covalent and non-covalent binding on the properties of hordein. Covalent hordein-GA complexes (H-GA) and non-covalent hordein/GA complexes (H/GA) were distinguished by molecular weight, free sulfhydryl groups and free amino groups. Isothermal titration calorimetry (ITC) demonstrated that physical mixing induced non-covalent binding of GA to hordein via hydrogen bonding and hydrophobic interactions, with a lower binding efficiency than covalent ones. Both complexation types led to a structural shift of hordein toward disorder, while grafting of oligomeric GA and alkaline treatment resulted in lower surface hydrophobicity and higher antioxidant activity of H-GA compared to H/GA. The nanoparticles assembled from H-GA had smaller particle sizes and higher physical stability than those formed from H/GA. The results of this study may provide new insights into the modification of hordein by polyphenols.
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