Effect of temperature, time and wheat gluten moisture content on wheat gluten network formation during thermomolding

Jansens, Koen J.A.; Lagrain, Bert; Rombouts, Ine; Brijs, Kristof; Smet, Mario; Delcour, Jan A.

doi:10.1016/j.jcs.2011.08.008

Cited by 58 publications

(61 citation statements)

References 27 publications

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“…Free thiol content was measured colorimetrically using DTNB (5,5'-dithiobis-(2-nitrobenzoic acid) according to the reported method (Jansens et al, 2011) with some modifications. A dispersion of the samples (2 mg/ml) was prepared in sample buffer [0.05 M phosphate buffer (pH 6.5) containing 2% (w/v) SDS, 3.0 M urea and 1.0 mM EDTA (Ethylenediaminetetraacetic acid)].…”

Section: Determination Of Free Thiol (Sh) Contentmentioning

confidence: 99%

“…Gluten has very low solubility in water due to its low content of amino acids with charged side chains and high content of hydrophobic amino acid proline (Jansens et al, 2011). Consequentially, the highest Ho was recorded for samples sheared or unsheared at room temperature at control pH (6.6) ( Table 1).…”

Section: Surface Hydrophobicity (Ho)mentioning

confidence: 99%

“…Among the gluten proteins, a/b, and !-gliadins contain six and eight cysteine residues, respectively, in their C terminal domains, all of which form homologous intra-chain disulphide bonds, whereas in glutenin fractions cysteine forms both intra and interchain disulphide bonds and a low level of cysteine remains free (Jansens et al, 2011). The amount of free thiol can be influenced by various conditions such as pH, temperature and hydrostatic pressure (Kieffer, Schurer, Köhler, & Wieser, 2007;Singh & MacRitchie, 2004).…”

Section: Thiol Contentmentioning

confidence: 99%

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Shear, heat and pH induced conformational changes of wheat gluten – Impact on antigenicity

2016

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Section: Determination Of Free Thiol (Sh) Contentmentioning

confidence: 99%

Section: Surface Hydrophobicity (Ho)mentioning

confidence: 99%

Section: Thiol Contentmentioning

confidence: 99%

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Shear, heat and pH induced conformational changes of wheat gluten – Impact on antigenicity

2016

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“…In order to lower the water uptake and permeability of wheat gluten materials, one way is to add hydrophobic additives 19,20 . Another way is to avoid using a plasticizer, which requires that WG is strengthened, for example, by adding macromolecular-crosslinkers into WG 9,10,[21][22][23] . Despite some successful strategies against increasing water permeability, the effects of water on the hierarchical structure of WG are still not clear 24 .…”

Section: Introductionmentioning

confidence: 99%

Structural Changes of Gluten/Glycerol Plastics under Dry and Moist Conditions and during Tensile Tests

Chen

et al. 2016

ACS Sustainable Chem. Eng.

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“…38,39 Among those proteins, 56 wt % are gliadins and 44 wt % are glutenin (Table I). The residual starch content is quite high (19.4 wt %).…”

Section: Characterization Of Wg and Its Fractionsmentioning

confidence: 99%

Dynamic mechanical analysis of the multiple glass transitions of plasticized wheat gluten biopolymer

Duval

Molina-Boisseau

Chirat

et al. 2015

J of Applied Polymer Sci

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Glass transition of thermo-molded biomaterials made from wheat gluten and its main protein classes is studied by dynamic mechanical analysis (DMA). The materials are plasticized with variable contents of glycerol (30-40 wt %) and water (0-20 wt %). For all materials, three successive relaxation phases are systematically detected. Their positions shift to lower temperature as the plasticizer content of materials increases. Composition in gluten, glycerol and water of each relaxation phase is estimated using the Couchman-Karasz model. Irrespective of the plasticizer content or composition, the relaxation phases shows rather constant plasticizer volume fractions. The low-, middle-, and high relaxation phases include respectively around 30, 60 and 80 vol % of gluten protein. These relaxations are assigned to the segmental motion of the surface amino-acid side groups, to the collective motion of packed gluten proteins, and to the gain in protein conformational mobility as a 2D network of interacting plasticizer molecules forms.

show abstract

Effect of temperature, time and wheat gluten moisture content on wheat gluten network formation during thermomolding

Cited by 58 publications

References 27 publications

Shear, heat and pH induced conformational changes of wheat gluten – Impact on antigenicity

Shear, heat and pH induced conformational changes of wheat gluten – Impact on antigenicity

Structural Changes of Gluten/Glycerol Plastics under Dry and Moist Conditions and during Tensile Tests

Dynamic mechanical analysis of the multiple glass transitions of plasticized wheat gluten biopolymer

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