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Changes in the hier...
Changes in the hierarchical protein polymer structure : Urea and temperature effects on wheat gluten films
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- Kuktaite, Ramune (author)
- Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Agrosystem,SLU Swedish University of Agricultural Sciences, Sweden
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- Plivelic, Tomás (author)
- Lund University,Lunds universitet,MAX IV-laboratoriet,MAX IV Laboratory,Lund University, Sweden
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- Türe, Hasan (author)
- KTH,Polymera material,KTH Royal Institute of Technology, Sweden
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- Hedenqvist, Mikael S. (author)
- KTH,Polymera material,KTH Royal Institute of Technology, Sweden
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- Gällstedt, Mikael (author)
- RISE,Innventia
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- Marttila, Salla (author)
- Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Växtskyddsbiologi,Department of Plant Protection Biology,SLU Swedish University of Agricultural Sciences, Sweden
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- Johansson, Eva (author)
- Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Agrosystem,SLU Swedish University of Agricultural Science, Sweden
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(creator_code:org_t)
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- Royal Society of Chemistry (RSC), 2012
- 2012
- English.
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In: RSC Advances. - : Royal Society of Chemistry (RSC). - 2046-2069. ; 2:31, s. 11908-11914
- Related links:
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http://dx.doi.org/10...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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https://lup.lub.lu.s...
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https://res.slu.se/i...
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Abstract
Subject headings
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- Understanding bio-based protein polymer structures is important when designing new materials with desirable properties. Here the effect of urea on the wheat gluten (WG) protein structure in WG-urea films was investigated. Small-angle X-ray scattering indicated the formation of a hexagonal close-packed (HCP) hierarchical structure in the WG-urea materials. The HCP structure was influenced significantly by the urea concentration and processing conditions. The interdomain distance d I between the HCP scattering objects increased with increasing content of urea and the objects seemed to be oriented in the extrusion direction. Additionally, the effect of temperature on the HCP structure was studied and it was shown that at ≥55°C the HCP structure disappeared. Transmission electron microscopy revealed a rather denatured pattern of both HMW-glutenins and gliadins in the WG-urea films. The molecular packing of the WG protein polymer can be highly affected by an additive and the processing method used.
Subject headings
- TEKNIK OCH TEKNOLOGIER -- Kemiteknik -- Polymerteknologi (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Chemical Engineering -- Polymer Technologies (hsv//eng)
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
- TEKNIK OCH TEKNOLOGIER -- Materialteknik -- Annan materialteknik (hsv//swe)
- ENGINEERING AND TECHNOLOGY -- Materials Engineering -- Other Materials Engineering (hsv//eng)
- NATURVETENSKAP -- Biologi -- Annan biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Other Biological Topics (hsv//eng)
- NATURVETENSKAP -- Kemi -- Polymerkemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Polymer Chemistry (hsv//eng)
Keyword
- Effect of temperature
- Hcp structure
- Hexagonal close-packed
- Hierarchical structures
- Inter-domain
- Molecular packings
- Processing condition
- Processing method
- Protein polymers
- Protein structures
- Scattering objects
- Small angle X-ray scattering
- Wheat gluten
- Wheat gluten films
Publication and Content Type
- ref (subject category)
- art (subject category)
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