Characterization of Biodegradable Films Obtained from Cysteine-Mediated Polymerized Gliadins

Abstract

This study focuses on the effect exerted by interchain disulfide bonds on the functional properties of films made from gliadins when cross-linked with cysteine. Gliadins were extracted from commercial wheat gluten with 70% aqueous ethanol, and cysteine was added to the film-forming solution to promote cross-linking between protein chains. The formation of interchain disulfide bonds was assessed by SDS-PAGE analysis. Gliadin films treated with cysteine maintain their integrity in water and become less extensible while their tensile strength increases as a consequence of the development of a more rigid network. The glass transition temperature of cross-linked films shifts to slightly higher values. The plasticizing effects of glycerol and moisture are also demonstrated. The mechanical behavior of cysteine-cross-linked gliadin films was compared to that of polymeric glutenins. Cross-linked gliadins displayed tensile strength values similar to those of glutenin films but achieved slightly lower elongation values. Cysteine-cross-linked gliadin films present the advantage that they are ethanol soluble, facilitating film fabrication or their application as a coating for food or for any other film or surface.

Wheat gluten fractions as wood adhesives—glutenins versus gliadins

“…3 However, extensive research has shown that the gliadin and glutenin fractions of wheat gluten possess very different properties and render different results in both food and nonfood applications. 5,6,9,[13][14][15] Inspired by these findings, it was hypothesized that the aforementioned differences also may result in different adhesive performance, possibly rendering one of the fractions superior to that of the others or to wheat gluten. The aim of this study is to compare the tensile shear strength of wood substrates bonded with glutenin and gliadin, respectively, and to investigate the influence of application method and degree of penetration of the proteins into the wood material.…”

Dynamic rheological properties of native and cross-linked gliadin proteins

“…They have excellent film forming character via solution casting using water and/or ethanol as co-solvent. In this sense, the unique physical and biochemical properties of gliadin make it suitable for numerous non-food applications such as biodegradable plastics, membranes and also as a material for biomedical applications [1][2][3][4][5][6][7][8].…”

“…Some of them have been associated with other analysis in order to develop a structural model [23] while others characterize and discuss the effect of heat, cold and denatured agents on conformers of a protein [3,4]. Indeed, all methods together provide the structural framework for the analysis of complex structures.…”

A novel globular protein electrospun fiber mat with the addition of polysilsesquioxane

“…These proteins are globular low molecular weight single-chains, readily soluble in aqueous ethanol. However, their solubility properties can be adjusted by using different solvents, which can promote kinetic intermediates which have been observed during folding from the unfolded state to the native state [1][2][3].…”