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ARS Home » Midwest Area » Peoria, Illinois » National Center for Agricultural Utilization Research » Plant Polymer Research » Research » Publications at this Location » Publication #258076
Title: Production of composites by using gliadin as a bonding material

Author
item Kim, Sanghoon

Submitted to: Journal of Cereal Science
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 6/15/2011
Publication Date: 7/27/2011
Citation: Kim, S. 2011. Production of composites by using gliadin as a bonding material. Journal of Cereal Science. 54(1):168-172. DOI: 10.1016/j.jcs.2011.05.003

Interpretive Summary: Polymer composites have been manufactured by mixing the component materials at high temperature. As an alternative way of producing composites, this researcher previously introduced a technology to potentially replace existing petroleum based polymers. During the fabrication process, powder-type raw material was coated with a corn protein, zein, that has a strong adhesive property. It was then processed to form a rigid material. Since the market price of zein is very high, in this research a much cheaper wheat protein, gliadin, was chosen and characterized to see if it could be used instead of zein. Experimental results showed that the mechanical properties of the composites fabricated with gliadin were compatible with those fabricated with zein. This research provides an understanding of the behavior of gliadin in solution, and offers a new process for the production of degradable/non-degradable composite materials. Scientists/manufacturers in industry and academia developing new polymer materials would benefit.

Technical Abstract: In our previous papers, a new technology that produces biopolymer composites by particle-bonding was introduced. During the manufacturing process, micrometer-scale raw material was coated with a corn protein, zein, which is then processed to form a rigid material. The coating of raw-material particles with zein makes use of the unique property of zein in aqueous ethanol solution. In this paper, we show that the behavior of a wheat protein, gliadin, is very similar to zein in aqueous ethanol. Size variation of aggregates in 45-65% aqueous ethanol was investigated with a turbidimeter in conjunction with Size Exclution Chromatography. Confirming the resemblance of gliadin to zein in terms of aggregation behavior in the solution, composites were fabricated by particle-bonding and their mechanical property was measured with a Universal Testing Machine. Test results showed that gliadin could be used instead of zein in the production of composites.