Quantitative determination and localisation of thiol groups in wheat flour

Shewry, Peter R.; Tatham, Arthur S.; Antes, Susanne; Wieser, Herbert

doi:10.1039/9781847552372-00211

Cited by 12 publications

(8 citation statements)

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“…Tripeptide glutathione occurs in flour in the free reduced (GSH) and free oxidised (GSSG) forms, as well as in the form of protein/glutathione mixed disulfides (PSSG) . Although comprising only a small portion (10%) of total free SH groups, gluthatione, as being a low molecular weight (LMW) thiol, diffuse more rapidly in dough than higher molecular weight proteins . Therefore, it is considered to be rheologically more effective than HMW proteins .…”

Section: Discussionmentioning

confidence: 99%

Changes in the rheological properties of wheat dough during short‐term storage of wheat

Hadnađev

Pojić

et al. 2014

J Sci Food Agric

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Section: Discussionmentioning

confidence: 99%

Changes in the rheological properties of wheat dough during short‐term storage of wheat

Hadnađev

Pojić

et al. 2014

J Sci Food Agric

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“…The total cysteine content of gluten protein components can be determined by amino acid analysis, for example, after oxidation with performic acid, but a distinction between cysteine and cystine is not possible by this method (6) groups can be determined spectrophotometrically prior to and after reduction according to the methods of Ellman (7) and Henschen (8). The identification and localization of cysteine and cystine residues are, however, only possible after labeling of SH groups and subsequent partial enzymatic hydrolysis of gluten proteins and sequence analysis of the relevant peptides (6,9).…”

Section: Introductionmentioning

confidence: 99%

Characterization of Sulfur Speciation in Low Molecular Weight Subunits of Glutenin after Reoxidation with Potassium Iodate and Potassium Bromate at Different pH Values Using X-ray Absorption Near-Edge Structure (XANES) Spectroscopy

Prange

Birzele²,

Krämer³

et al. 2003

J. Agric. Food Chem.

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Sulfur speciation in low molecular weight (LMW) subunits of glutenin after reoxidation with potassium iodate and potassium bromate at different pH values, aged subunits of glutenin as well as gluten, and gliadin have been investigated in situ by S K-edge X-ray absorption near-edge structure (XANES) spectroscopy. XANES spectra were analyzed quantitatively using a least-squares fitting routine to provide relative percentage contribution of different sulfur species occurring in the samples. Using potassium iodate and potassium bromate for reoxidation of reduced LMW subunits of glutenin led not only to disulfide states but also to higher oxidation states (sulfoxide state, sulfonic acid state). Strongest oxidation occurred at low pH values. Higher oxidation states were also predominantly detected in the aged subunits of glutenin, whereas the disulfide state was the main sulfur species in gluten and gliadin samples. The results showed that the oxidation state of sulfur prior to oxidation (thiol, disulfide) strongly influences sulfur speciation after oxidation. The choice of the oxidizing reagent seems to be of minor importance.

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“…(), on average the concentration of free ‐SH groups of gluten samples amounted 2.10 μmol g −1 protein. In addition, Antes & Wieser () reported the variation of free ‐SH groups of bread wheat flour in the range of 1.0–1.5 μmol g −1 , where approximately 30% of them could be assigned to the glutenins. A lower concentration of free ‐SH groups in investigated bread and durum flours (ranged from 0.4 to 0.7 nmol mg −1 and from 0.6 to 0.7 nmol mg −1 , respectively) than those aforementioned might be explained either by the differences originating from varieties and/or by different employed growing conditions of varieties.…”

Section: Resultsmentioning

confidence: 99%

The polypeptide composition, structural properties and antioxidant capacity of gluten proteins of diverse bread and durum wheat varieties, and their relationship to the rheological performance of dough

Janković

Barać

Pešić

et al. 2015

Int J of Food Sci Tech

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Summary The aim of this study was to compare five bread and five durum wheat genotypes for gliadins and glutenins profiles, the concentration of free sulphhydryl groups and disulphide bonds, antioxidant capacity of gluten proteins and their bread‐making performance. On average, bread wheat had significantly higher concentration of total sulphur‐rich (S‐rich) and sulphur‐poor (S‐poor) subunits of gliadins, as well as total low molecular weight (LMW) and high molecular weight (HMW) subunits of glutenins than durum wheat. However, durum wheat had higher concentration of S‐rich γ‐gliadins and S‐poor D‐LMW‐glutenins, but did not possess S‐poor ω‐gliadins. The concentration of disulphide bonds and total cysteine was higher in the durum gluten than that in the bread gluten, as well as antioxidant capacity (on average 90.6 vs. 85.9 mmol Trolox Eq kg−1, respectively). In contrast to the bread wheat, the concentration of HMW‐glutenins was negatively associated with extensibility, as well as resistance to extension in durum wheat flour dough.

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Quantitative determination and localisation of thiol groups in wheat flour

Cited by 12 publications

References 0 publications

Changes in the rheological properties of wheat dough during short‐term storage of wheat

Changes in the rheological properties of wheat dough during short‐term storage of wheat

Characterization of Sulfur Speciation in Low Molecular Weight Subunits of Glutenin after Reoxidation with Potassium Iodate and Potassium Bromate at Different pH Values Using X-ray Absorption Near-Edge Structure (XANES) Spectroscopy

The polypeptide composition, structural properties and antioxidant capacity of gluten proteins of diverse bread and durum wheat varieties, and their relationship to the rheological performance of dough

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