Influence of glycosylation of deamidated wheat gliadin on its interaction mechanism with resveratrol
文献类型： 外文期刊
作者： Qiu, Chaoying 1 ; Wang, Yong 1 ; Teng, Yinglai 1 ; Zhao, Mouming 3 ;
作者机构： 1.Jinan Univ, Dept Food Sci & Engn, Guangzhou 510632, Guangdong, Peoples R China
2.Chinese Acad Fishery Sci, South China Sea Fisheries Res Inst, Minist Agr, Key Lab Aquat Prod Proc, Guangzhou 510300, Guangdong, Peoples R China
3.South China Univ Technol, Dept Food Sci & Engn, Guangzhou 510641, Guangdong, Peoples R China
关键词： Gliadin;Glycosylation;Resveratrol;Fluorescence quenching;Solubility
期刊名称：FOOD CHEMISTRY （ 影响因子：7.514； 五年影响因子：7.516 ）
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年卷期：
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收录情况： SCI
摘要： Gliadin is a main composition of wheat storage protein with unique characteristics. Polyphenol with health benefits tends to form complex with protein. In this study, glycosylation of deamidated wheat gliadin (gliadin) was carried out. Fluorescence quenching was applied to evaluate their binding mechanisms with resveratrol. Results showed that glycosylation could increase the solubility and decrease the surface hydrophobicity of gliadin. Both gliadin and glycosylated gliadin have strong affinity with resveratrol. The thermodynamic parameters of binding process indicated that complexation of resveratrol with gliadin was mainly driven by hydrophobic interaction, while by hydrogen bonds with glycosylated gliadin. The hydrosolubility of resveratrol was dramatically increased especially in the presence of glycosylated gliadin. This was consistent with the higher binding constant of glycosylated gliadin with resveratrol. Therefore, gliadin and glycosylated gliadin are both effective to carry resveratrol or other bioactive compounds, and their binding mechanisms are different due to structural difference. (C) 2016 Elsevier Ltd. All rights reserved.
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