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FAIR-CT96-1979
Wheat Gluten as Biopolymer for the Production of Renewable and Biodegradable Materials |
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Type of Project | Shared Cost |
| Contract No | FAIR-CT96-1979 | |
| Total Cost | 1,559,705 ECU | |
| EC Contribution | 1,050,152 ECU | |
| Start Date | 01/12/96 | |
| Duration | 48 Months |
Wheat gluten as biopolymer for the production of renewable and biodegradable materials
Objectives
The increasing demand from consumers and industry for environmentally friendly and renewable polymers explains the great interest in plant macromolecules as substitutes of synthetic, petroleum-based polymers. Besides starch and cellulose that have been extensively studied, proteins exhibited great potential for biopackaging materials, plastic films, adhesives and disposables.
Technical Approach
The goal of the proposed research is to study these potentialities for wheat gluten, which is a protein available in large amount and at a reasonable cost in Europe.
Expected Results
I. Direct Results
II. Indirect Results
The production of new biodegradable materials would have a positive environmental impact and should lead to the appearance of a new integrated transformation chain of wheat.
Applications
This research should offer alternative possibilities to industry for manufacturing packaging, protective coatings, adhesives and disposables, made of less material or non-polluting material. This corresponds to an increasing demand of the consumers.
Results To Date
Using industrial gluten (native or deamidated) or gliadins enriched fractions, films could be prepared by casting in aqueous, alkaline or acidic/ethanolic conditions. From rheological properties of the film forming dispersions it could be assumed that the various polyol type plasticisers interact in a different manner with the proteins. Depending on plasticiser and protein/plasticiser ratio, the stress of gliadin films varied in the range 1-3.5 Mpa and the strain varied in the range 100 to 600%. For whole gluten, these values were between 1 and 1.5 Mpa and 375-450% respectively.
The glass transition temperature (Tg) for gluten was shown by modulated DSC to be dramatically dependent on the water content. Tg dropped from approximately 110°C to 10°C when the water mass fraction increased from 2 to 20%.
To improve water resistance properties of gluten materials, hydrophobisation by chemical reagents were performed and surface hydrophobicity of the proteins followed by fluorescence. By studying the ability of transglutaminase to modify wheat proteins, a very high insolubilisation of gluten was observed, due to crosslinking whereas treated gliadins became more soluble in the neutral pH region. Finally, homoblock polypeptides could be expressed in E. coli as a model of true peptidic polymers.
The feasibility of wet processing was also investigated by casting, spraying and brushing of aqueous dispersion of protein onto a solid substrate.


Strain test
Contacts
Coordinator
EC Scientific Officer
Participant
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by CPL Press:
03/07/2007
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