Abstract
SummaryGliadin is an important protein present in cereals. Owing to its solubility in alcohol, gliadin contributes significantly to the field of food industry. However, at present, it is challenging to study the structural characteristics of gliadin at the molecular level because the exact 3‐D structure cannot be obtained using experimental methods. In this study, an α‐gliadin model was constructed by combining homology modelling, ab initio modelling, and threading methods to study the structural properties of gliadin in ethanol aqueous solution. Our results indicated that glutamine is a key element of α‐gliadin. Also, α‐gliadin exhibited relatively low hydrophilicity and high lipid solubility. Molecular dynamics simulations suggested that there are hydrogen bonds and van der Waals forces existed between α‐gliadin and ethanol molecules. This study has explored the structure of wheat gliadin and its conformation in different ethanol solutions and provides a deeper understanding towards the deacetylation mechanism and potential applications of α‐gliadin in the food industry.
Published Version
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