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Submitted to: Journal of Agricultural and Food Chemistry
Publication Type: Peer Reviewed Journal Publication Acceptance Date: 5/29/1996 Publication Date: N/A Citation: N/A Interpretive Summary: The development of biofuels programs to improve environmental quality and reduce dependence on fossil resources promises to produce massive quantities of cheap protein byproducts. Use of these byproducts to substitute for petroleum-based materials could further reduce oil imports and improve the economics of biofuels processing. This work, a computational analysis, examined corn and wheat proteins for size and surface characteristics suited for use in new materials that might replace hydrocarbon polymers. Some seed proteins contain segments that are surprisingly like collagen in animal skin and connective tissue or like fibrogen that clots blood. Others that nearly duplicate silk are promising additives for bioplastics. Several segments identified in the work should form strong films and adhesives. The work also identified proteins with unusual distributions of chemically reactive amino acids, which could ultimately lead to novel derived materials. Knowledge that such segments exist provides guidance for producers of cereal protein fractions. Technical Abstract: Comparison of computed profiles for beta-sheet conformations of zein, glutelin, gliadin, glutenin, and other cereal or non-plant proteins disclose unusual distributions of volume, polarity, and chemical functionality as well as inter- and intra-specific surface analogies between dissimilar amino acid sequences. Volume and polarity surfaces of major cereal proteins are more like those of collagen or fibrinogen than those of silk or hydrocarbon polymers. Potentially useful segments occur non-randomly. A low-molecular weight glutenin fragment approximates two-thirds of human gamma- fibrinogen. Four others duplicate the polarity of 25 to 50 percent of collagen. Ten exceptionally asymmetric segments show potential for inclusion in film forming preparations and adhesives. Ultra- hydrophobic sequences in corn oil body oleosins approach the diameter of spider silk, match its uniformity, and exceed its hydrophobicity. |
