Literature DB >> 18163577

Reactivity of wheat gluten protein during mechanical mixing: radical and nucleophilic reactions for the addition of molecules on sulfur.

Rémi Auvergne1, Marie-Hélène Morel, Paul Menut, Olivia Giani, Stéphane Guilbert, Jean-Jacques Robin.   

Abstract

Mechanical properties of gluten-based biomaterials, such as break stress, were known to be influenced by temperature and shear stresses applied during processing. It is well documented in literature that these processing parameters promoted wheat gluten protein aggregation. Exchange between disulfide bonds and thiol groups oxidation are the postulated mechanisms that lead to gluten protein solubility loss in sodium dodecyl sulfate buffers. Both nucleophilic and radical reactions were postulated to act during gluten aggregation. To graft molecules on gluten, a study was carried out to explore the reactivity of its thiol and disulfide groups during thermomechanical mixing. A range of reactants able to react via radical or nucleophilic pathways with thiol groups were synthesized. Reactivity between gluten and functions was quantified by gluten solubility measurements. This investigation and literature observations allowed proposal of a general gluten aggregation mechanism during mixing.

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Year:  2007        PMID: 18163577     DOI: 10.1021/bm7009834

Source DB:  PubMed          Journal:  Biomacromolecules        ISSN: 1525-7797            Impact factor:   6.988


  1 in total

1.  Synthesis of ST7612AA1, a Novel Oral HDAC Inhibitor, via Radical 
Thioacetic Acid Addition.

Authors:  Gianfranco Battistuzzi; Giuseppe Giannini
Journal:  Curr Bioact Compd       Date:  2016-12
  1 in total

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