Influence of glycosylation of deamidated wheat gliadin on its interaction mechanism with resveratrol

Food Chemistry

Volumn 221, Issue , 2017, Pages 431-438

  Qiu, Chaoying ^a,b   Wang, Yong ^a   Teng, Yinglai ^a   Zhao, Mouming ^c  

^a JINAN UNIVERSITY   (China)

^b SOUTH CHINA SEA FISHERIES RESEARCH INSTITUTE   (China)

^c SOUTH CHINA UNIVERSITY OF TECHNOLOGY   (China)

Author keywords

Fluorescence quenching; Gliadin; Glycosylation; Resveratrol; Solubility

Indexed keywords

BINS; FLUORESCENCE; GLYCOSYLATION; HYDROGEN BONDS; HYDROPHOBICITY; PROTEINS; QUENCHING; SOLUBILITY;

FLUORESCENCE QUENCHING; GLIADIN; HYDROPHOBIC INTERACTIONS; INTERACTION MECHANISMS; STRUCTURAL DIFFERENCES; SURFACE HYDROPHOBICITY; THERMODYNAMIC PARAMETER; WHEAT STORAGE PROTEINS;

RESVERATROL;

GLIADIN; RESVERATROL; STILBENE DERIVATIVE;

ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; DRUG PROTEIN BINDING; FLUORESCENCE; HYDROGEN BOND; HYDROPHOBICITY; PROTEIN GLYCOSYLATION; SOLUBILITY; THERMODYNAMICS; WHEAT; CHEMICAL PHENOMENA; GLYCOSYLATION; HUMAN; METABOLISM;

GLIADIN; GLYCOSYLATION; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; SOLUBILITY; STILBENES; TRITICUM;

EID: 84993971877     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2016.10.098     Document Type: Article

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