The effect of heat on wheat gluten and the involvement of sulphydryl-disulphide interchange reactions

Schofield, J. D.; Bottomley, Robin C.; Timms, Michael F.; Booth, Michael R.

doi:10.1016/s0733-5210(83)80012-5

Cited by 344 publications

(238 citation statements)

References 5 publications

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“…Gluten proteins have a relatively large amount of -SH containing amino acids. These residues form intrachain S-S bonds that suffer different changes depending on the thermal food quantitative extraction of the proteins and affecting its further analysis [3]. The most common sample treatment involves extraction of gluten prolamins using a 60 % ethanol solution.…”

Section: Introductionmentioning

confidence: 99%

Sensitive gluten determination in gluten-free foods by an electrochemical aptamer-based assay

Amaya-González

de‐los‐Santos‐Álvarez

Miranda‐Ordieres

et al. 2015

Anal Bioanal Chem

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Enzyme-immune assays are currently the methods of choice for gluten control in foods labelled as "gluten free", providing a mechanism for assessing food safety for consumption by coeliac and other allergic patients. However, their limitations, many of them associated to the reactivity of the different antibodies used and their degree of specificity, have prevented the establishment of a standardized method of analysis. We explore new methods for quantitatively determine gluten content in foods based on the use of two recently described aptamers, raised against a 33-mer peptide recognised as the immunodominant fragment from α2-gliadin. The assays use the target peptide immobilized onto streptavidin-coated magnetic beads in combination with a limited amount of biotin-aptamer in a competitive format, followed by streptavidin-peroxidase labelling of the aptamer that remains bound to the magnetic beads. The enzyme activity onto the beads, measured by chronoamperometry in disposable screen-printed electrodes, is inversely related to the target concentration in the test solution. We find that while the assay using the aptamer with the highest affinity towards the target (Gli 4) achieves low detection limits (~0.5 ppm) and excellent analytical performance when challenged in samples containing the intact protein, gliadin, it fails in detecting the peptide in solution. This problem is circumvented by employing another aptamer (Gli 1), the most abundant one in the SELEX pool, as a receptor. The proposed assays allow the convenient detection of the allergen in different kind of food samples, including heat-treated and hydrolysed ones. The obtained results correlate with those of commercially available antibody-based assays, providing an alternative for ensuring the safety and quality of nominally gluten-free foods.

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Section: Introductionmentioning

confidence: 99%

Sensitive gluten determination in gluten-free foods by an electrochemical aptamer-based assay

Amaya-González

de‐los‐Santos‐Álvarez

Miranda‐Ordieres

et al. 2015

Anal Bioanal Chem

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“…These proteins are divided into four main classes, of which the albumins and globulins are minor fractions, compared to the monomeric gliadins and the polymeric glutenins. The very large polymeric glutenin proteins composed of high-molecular weight glutenin (HMW) and low-molecular weight glutenin (LMW) subunits are linked together by disulphide bridges (Schofield et al 1983). Payne et al (1984) demonstrated that an allelic variation in the composition of the LMW prolamins was strongly correlated with the pasta makingquality characteristics.…”

Section: Introductionmentioning

confidence: 99%

Studies on effect of additives on protein profile, microstructure and quality characteristics of pasta

2011

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Wheat storage proteins play a vital role in pasta making quality. In the present study, SDS-PAGE, Gel filtration chromatography and Scanning electron microscopy techniques were employed to understand the changes in the wheat protein fractions and their interactions with additives namely Sodium Steroyl Lactate (SSL), Glycerol Monostearate (GMS) and Hydroxy Propyl Methyl Cellulose (HPMC) during processing of pasta. SDS-PAGE studies indicated changes in High Molecular Weight Glutenin (HMW) fractions during drying stages of pasta preparation and in cooked pasta samples. In uncooked pasta, gel filtration patterns showed four peaks corresponding to different storage proteins whereas in the case of cooked pasta, these peaks were merged into three peaks. Pasta quality characteristics studies indicated that pasta with HPMC was found to have minimum percentage of cooking loss (5.6%), increased cooked weight (82 g), firmness (2.97 N) and high overall quality score (27) than GMS, SSL and control. Microstructure studies confirm the beneficial effect of HPMC. The present study indicated that HPMC is better additive for pasta manufacture followed by GMS. This could be due to interaction of HPMC with starch and protein matrix is different from that of GMS and SSL.

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“…Drying increases the protein molecular size since the heating of glutenin above 55 8C or gliadins above 70 8C induces disulfide/sulfydryl exchange reactions (Payne, Jackson, & Holt, 1984;Schofield, Bottomley, Timms, & Booth, 1983). Temperatures around 65 8C influence particularly the S-S structure of highmolecular weight (HMW) albumins (and perhaps their linkage to glutenin oligomers) whereas higher temperatures affect low-molecular weight (LMW) albumins and gliadins .…”

Section: Introductionmentioning

confidence: 99%

“…Heat treatments cause the formation of new non-starch linkages, mainly b-1!4 and 1!6 anomers (Laurentı´n, Ca´rdenas, Ruales, Pe´rez, & Tovar, 2003) that, by reducing the enzymic access of several adjacent aglucosidic bonds, determine a decrease of starch digestibility and the formation of the so called ''resistant starch''. Thermal treatments are also responsible for protein denaturation, causing conformational changes in gliadins and low-molecular weight albumins and globulins (Guerrieri, Alberti, Lavelli, & Cerletti, 1996;Schofield et al, 1983), formation of aggregates in glutenins and other changes of the secondary and tertiary structures (Michon, Wang, Ferrasson, & Gueguen, 1999;Tilley et al, 2001) through sulfhydryl (SH)-disulfide interchange reactions, strong crosslinking bonds and the exposure of hydrophobic groups on the surface making the proteins insoluble and preventing their successive hydration and dough formation (Riganakos & Kontominas, 1994).…”

Section: Introductionmentioning

confidence: 99%

Effects of the addition of a meal deriving from toasted durum wheat kernels on dough properties and spaghetti cooking behavior Efectos de la adición de una harina derivada de granos tostados de trigo duro en las propiedades de masa y comportamiento para el cocido de espaguetis

Baiano¹,

Lamacchia²,

Terracone³

2011

CyTA - Journal of Food

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The effect of heat on wheat gluten and the involvement of sulphydryl-disulphide interchange reactions

Cited by 344 publications

References 5 publications

Sensitive gluten determination in gluten-free foods by an electrochemical aptamer-based assay

Sensitive gluten determination in gluten-free foods by an electrochemical aptamer-based assay

Studies on effect of additives on protein profile, microstructure and quality characteristics of pasta

Effects of the addition of a meal deriving from toasted durum wheat kernels on dough properties and spaghetti cooking behavior Efectos de la adición de una harina derivada de granos tostados de trigo duro en las propiedades de masa y comportamiento para el cocido de espaguetis

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