A combination of
genotype, cultivation environment, and protein
separation procedure was used to modify the nanoscale morphology,
polymerization, and chemical structure of glutenin proteins from wheat.
A low-polymerized glutenin starting material was the key to protein–protein
interactions mainly via SS cross-links during film formation, resulting
in extended β-sheet structures and propensity toward the formation
of nanoscale morphologies at molecular level. The properties of glutenin
bioplastic films were enhanced by the selection of a genotype with
a high number of cysteine residues in its chemical structure and cultivation
environment with a short grain maturation period, both contributing
positively to gluten strength. Thus, a combination of factors affected
the structure of glutenins in bioplastic films by forming crystalline
β-sheets and propensity toward the ordered nanostructures, thereby
resulting in functional properties with high strength, stiffness,
and extensibility.