The Inoorporation of [35s]Oysteine into the Proteins of Dough by Disulphide-Sulphydryl Interohange

Art, PR Stew; Mauritzen, CM

doi:10.1071/bi9661125

Cited by 4 publications

(2 citation statements)

References 5 publications

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“…Possible explanations for the absence of thiol-disulfide interchange reactions may be the low water content and very short reaction times of extrusion. Studies in doughs have shown that the thiol-disulfide interchange reactions require longer periods of mixing time and also require sufficient water (Stewart andMauritzen 1966, Jones andCarnegie 1971).…”

Section: Sds-pagementioning

confidence: 99%

Changes in Disulfide and Sulfhydryl Contents and Electrophoretic Patterns of Extruded Wheat Flour Proteins

Anderson¹,

2000

Cereal Chem

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Cereal Chem. 77(3):354-359Twin-screw extrusion of wheat flour and the effects on the flour proteins were studied using flour samples containing 9, 20, and 30% protein. Vital gluten containing 70% protein was used to achieve the flour protein levels. The three flour samples were extruded with a twin-screw extruder at a combination of processing parameters (exit die temperatures of 120, 140, and 160°C, and screw speeds of 240, 320, and 400 rpm). Increasing extruder exit die temperatures resulted in increased sulfhydryl content of the 9 and 20% protein content flour samples, but appeared to have little or no effect on the 30% protein content flour sample. Similarly, disulfide content decreased, albeit disproportionately, following the same trend. Both sulfhydryl and disulfide contents of extruded samples were lower than those of the nonextruded samples and could imply denaturation of protein, aggregation through intermolecular disulfide bonds, or oxidation during extrusion processing. Total cysteine content of extruded samples decreased by ≈16% relative to nonextruded samples, but otherwise remained almost unchanged among all extruded samples. The loss of total cysteine in extruded samples could represent the generation of hydrogen sulfide, volatile organic compounds, or flavor compounds during extrusion. SDS-PAGE analysis of total proteins showed a shift from the higher to lower molecular weight regions for certain protein bands. Both depolymerization and protein aggregation occurred at higher shear forces during extrusion.

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Section: Sds-pagementioning

confidence: 99%

Changes in Disulfide and Sulfhydryl Contents and Electrophoretic Patterns of Extruded Wheat Flour Proteins

Anderson¹,

2000

Cereal Chem

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“…2). Sodium sulfite cleaves S-S bonds in WG (Stewart and Mauritzen, 1966). Negligible peaks were eluted at V 0 for film samples cast from solutions heated at 55, 75, and 95°C (Fig.…”

Section: Gel Permeation Chromatographymentioning

confidence: 99%

Physical and Molecular Properties of Wheat Gluten Films Cast from Heated Film‐Forming Solutions

Roy

Weller

Gennadios

et al. 1999

Journal of Food Science

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The effect of heating film-forming solutions on physical and molecular properties of cast wheat gluten (WG) films was determined. Glycerol-plasticized films were cast from alkaline (pH 10), heat-treated (55, 75, or 95°C for 10 min) solutions of WG in aqueous ethanol. Protein solubility (PS) of films in water decreased (P<0.05) with increasing temperature. Gel permeation chromatograms showed reduced extractability of protein fractions other than v-gliadins in WG films. This reduced extractability was due to disulfide (S-S) bond formation. SDS-PAGE patterns of native WG and WG film samples suggested increased cross-linking through covalent S-S bonds in films from solutions heated at 75 or 95°C. Water resistance in potential packaging applications of WG edible films could be modified by adjusting heat-treating temperature.

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Rheological activity of peptides, simple disulphides and simple thiols in wheaten dough

Jones

Carnegie

1969

J Sci Food Agric

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The disulphide peptides of flour have been separated into acidic (glutathione) and basic peptides, and their effects on the rheological properties of dough have been investigated. The only peptide normally present in flour to have marked activity in dough was glutathione.The other disulphide peptides of flour were only slightly active in that their sole effect was to diminish the tolerance of the dough to prolonged mixing. Their lack of activity probably results from their disulphide groups being non-reactive at the pH values found in dough. The same peptides in the thiol form were slightly more active in that they decreased development time and maximum resistance.All types of thiols tested were active in dough, but of the disulphides tested, only the acidic peptides GSSG (oxidised glutathione) and bis-y-glutamylcystine had significant activity. Possible modes of action of disulphide peptides in dough are discussed.

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The Inoorporation of [35s]Oysteine into the Proteins of Dough by Disulphide-Sulphydryl Interohange

Cited by 4 publications

References 5 publications

Changes in Disulfide and Sulfhydryl Contents and Electrophoretic Patterns of Extruded Wheat Flour Proteins

Changes in Disulfide and Sulfhydryl Contents and Electrophoretic Patterns of Extruded Wheat Flour Proteins

Physical and Molecular Properties of Wheat Gluten Films Cast from Heated Film‐Forming Solutions

Rheological activity of peptides, simple disulphides and simple thiols in wheaten dough

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