Unraveling the Structural Puzzle of the Giant Glutenin Polymer-An Interplay between Protein Polymerization, Nanomorphology, and Functional Properties in Bioplastic Films

ACS Omega
Faiza RasheedEva Johansson

Abstract

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.

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Citations

Feb 23, 2020·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Faiza RasheedEva Johansson
Jan 11, 2021·International Journal of Biological Macromolecules·Monika C WehrliMario Jekle
Feb 20, 2021·The Application of Clinical Genetics·Nastaran AsriKamran Rostami

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