ABSTRACT
Despite much research, there are very few commercial prolamin bioplastics. The major reason, apart from their high cost, is that they have inferior functional properties compared with synthetic polymer plastics. The inferior functional properties are because the prolamins are complex, each consisting of several classes and subclasses, and the functional properties of their bioplastics are greatly affected by water. Prolamin bioplastics are produced by controlled protein aggregation from a solvent or by thermoplastic processing. Recent research indicates that aggregation occurs by polypeptide self-assembly into nanostructures. Protein secondary structure in terms of α-helical and β-sheet structure seems to play a key but incompletely understood role in assembly. Also, there is inadequate knowledge as to how these nanostructures further assemble and organize into the various forms of prolamin bioplastics such as films, fibers, microparticles, and scaffolds. Many methods have been investigated to improve prolamin bioplastic functionality, including better solvation of the prolamins, plasticization, physical and chemical cross-linking, derivatization, and blending with synthetic and natural polymers, and some success has been achieved. The most promising area of commercialization is the biomedical field, in which the relative hydrophilicity, compatibility, and biodegradability of, particularly, zein and kafirin are advantageous. With regard to biomedical applications, “supramolecular design” of prolamin bioplastics through control over inter- and intramolecular weak interactions and disulfide/sulfhydryl interchange appears to have considerable potential.
