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Crosslinks in wheat gluten films with hexagonal close-packed protein structures
Leuven Food Science and Nutrition Research Centre (LFoRCe), KULeuven, Belgium.
KTH, School of Chemical Science and Engineering (CHE), Fibre and Polymer Technology.
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2013 (English)In: Industrial crops and products (Print), ISSN 0926-6690, Vol. 51, 229-235 p.Article in journal (Refereed) Published
Abstract [en]

Wheat gluten/glycerol (WGG) films were extruded with aqueous ammonia/salicylic acid or urea to investigate the reactions contributing to their hexagonal close-packed protein structures and material properties. The addition of aqueous ammonia and salicylic acid increased the pH, which, in turn, increased the level of intermolecular disulfide and lanthionine cross-links in the WGG films. Increased protein cross-linking reactions resulted in higher material strength and tensile modulus. These cross-linking reactions and the resulting material properties were similar for WGG films with 7.5% and 10% aqueous ammonia. Added urea into WGG film partially degraded into cyanate and ammonium. Cyanate subsequently reacted with lysine and cysteine to ε-carbamyllysine and S-carbamylcysteine, respectively. Even though these reactions resulted in a more alkaline reaction environment, hereby favoring disulfide bond formation and decreasing protein extractability, they also prevented the involvement of cysteine and lysine in protein cross-linking. The alkylation of these reactive amino acids, together with the plasticizing effect of urea, led to lower material strength and elastic modulus with increasing levels of urea.

Place, publisher, year, edition, pages
2013. Vol. 51, 229-235 p.
Keyword [en]
Biofilms, Hexagonal close-packed structure, Homocitrulline, S-carbamylcysteine, Urea, Wheat gluten, Crosslinking reaction, Disulfide bond formation, Hexagonal close-packed, Plasticizing effects, Protein crosslinking, Alkalinity, Amino acids, Ammonia, Covalent bonds, Elastic moduli, Metabolism, Proteins, Strength of materials, Crosslinking, amino acid, ammonium, biodegradation, biofilm, pH, protein, salicylic acid, sulfide
National Category
Chemical Engineering
URN: urn:nbn:se:kth:diva-139982DOI: 10.1016/j.indcrop.2013.08.077ISI: 000330820800031ScopusID: 2-s2.0-84885445207OAI: diva2:689170

QC 20140120

Available from: 2014-01-20 Created: 2014-01-16 Last updated: 2014-03-06Bibliographically approved

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Delcour, Jan A.Türe, HasanHedenqvist, Mikael S.Kuktaite, Ramune
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