Abstract：
:Plant proteins are biopolymers with interesting technological applications for the food industry due to their ability to interact with phenolic compounds such as anthocyanins. The 3D structure of the 7S globulin from grape seed was elucidated for the first time using a homology model. The constructed 3D model showed that grape seed 7S globulin is rich in α-helices and β-sheets stabilized by six disulfide bridges. The interaction with the major grape anthocyanin malvidin-3-glucoside was also assessed by Docking and Molecular Dynamic simulation. Theoretical results demonstrated that 7S globulin interacts with Mv3glc through hydrogen, alkyl and π-alkyl bonds and the flavylium cation is oriented towards a hydrophobic region of the protein, being protected from hydration. Results provide valuable insights for understanding the mechanisms involved in the molecular interaction of grape anthocyanins with grape seed proteins that could be relevant to use them as potential color protecting agents in food industry applications.
journal_name
Food Chemjournal_title
Food chemistryauthors
Chamizo-González F,Gordillo B,Heredia FJdoi
10.1016/j.foodchem.2021.129014subject
Has Abstractpub_date
2021-01-09 00:00:00pages
129014eissn
0308-8146issn
1873-7072pii
S0308-8146(21)00015-7journal_volume
347pub_type
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