First insights into the binding mechanism and colour effect of the interaction of grape seed 11S globulin with malvidin 3-O-glucoside by fluorescence spectroscopy, differential colorimetry and molecular modelling
Recently, the search for alternative proteins endogenous to grapes to be used as wine colour protecting agents became an important research trend. In this study, the molecular interaction between the grape seed 11S globulin from winemaking by-product and malvidin-3-O-glucoside was investigated by fl...
| Autores: | , , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión aceptada para publicación |
| Fecha de publicación: | 2023 |
| País: | España |
| Institución: | Universidad de Sevilla (US) |
| Repositorio: | idUS. Depósito de Investigación de la Universidad de Sevilla |
| OAI Identifier: | oai:idus.us.es:11441/153419 |
| Acceso en línea: | https://hdl.handle.net/11441/153419 https://doi.org/10.1016/j.foodchem.2023.135591 |
| Access Level: | acceso abierto |
| Palabra clave: | Colour Fluorescence quenching Grape seed 11S globulin Guided docking Malvidin3-O-glucoside Winemaking by-product |
| Sumario: | Recently, the search for alternative proteins endogenous to grapes to be used as wine colour protecting agents became an important research trend. In this study, the molecular interaction between the grape seed 11S globulin from winemaking by-product and malvidin-3-O-glucoside was investigated by fluorescence, differential colorimetry and molecular modelling. Fluorescence studies revealed the formation of grape seed protein- pigment complex whose KS was 8.5 × 104 M−1 and binding sites, n = 1.3. Malvidin-3-O-glucoside showed darker and more vivid bluish colour of in the presence of 11S globulin, suggesting the flavylium cation protection in a hydrophobic region of the protein. Docking analysis and molecular dynamics simulation indicated that malvidin-3-O-glucoside interacts mainly with the acidic subunit (40 kDa) of the 11S globulin monomer (60 kDa). An average of two hydrogen bonds and Van der Wall forces were the main interaction forces found for the protein-pigment complex, whose stability was confirmed by root-means-square deviation. © 2023 Elsevier Ltd |
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