Atomistic Modeling of Peptide Aggregation and β-Sheet Structuring in Corn Zein for Viscoelasticity.

摘要: The structure-function relationships of plant-based proteins that give rise to desirable texture attributes in order mimic meat products are generally unknown. In particular, it is not clear how engineer viscoelasticity impart cohesiveness and proper mouthfeel; however, known intermolecular β-sheet structures have the potential enhance viscoelastic property. Here, we investigated propensity selected peptide segments within common corn α-zein variants maintain stable aggregates structures. Simulations on dimer systems showed stability was influenced by initial orientation presence contiguous small hydrophobic residues. using eight-peptide oligomers revealed sequences without proline had higher levels structuring. Additionally, identified with a hydrogen-bonding density >22% tended larger percent conformation. These results contribute understanding zein can be increased for use analogues.