Biotechnology of Breadmaking: Unraveling and Manipulating the Multi-Protein Gluten Complex

Shewry, Peter R.; Tatham, Arthur S.; Barro, Francisco; Barceló, P.; Lazzeri, P. A.

doi:10.1038/nbt1195-1185

Cited by 262 publications

(225 citation statements)

References 24 publications

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“…Gliadins and glutenins are important for the formation of a continuous proteinaceous network (gluten), conferring the unique physicochemical properties such as elasticity and viscous flow to doughs [20]. The structural characteristic (β-spiral) of HMM glutenin may be important for bread-making quality [27]. Therefore, developing an alternative method is desired.…”

Section: Discussionmentioning

confidence: 99%

Identification of major wheat allergens by means of the Escherichia coli expression system

Maruyama

Ichise

Katšube

et al. 1998

European Journal of Biochemistry

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Wheat proteins were fractionated into salt-soluble, glutenin-rich, and gliadin-rich fractions. Reactivities of these protein fractions with sera of patients with wheat-associated allergies were examined under various conditions. The relative reactivity of the fractions was generally in the order glutenin-rich Ͼ gliadin-rich ӷ salt-soluble fractions, although their reactivities were variable among patients and among the reaction conditions, indicating that the kind, the number and the epitope of allergens were variable among patients. To identify major allergens, A-, γ-and ω-gliadin, and low-molecular-mass (LMM)-and high-molecular-mass (HMM)-glutenin genes were expressed in Escherichia coli by means of a pET vector. Recombinant gliadins and glutenins were partially purfied on the basis of the solubilities of prolamin and glutelin. The partially purified recombinant proteins were reacted with the patients' sera. LMM glutenin containing many Gln-Gln-Gln-Pro-Pro motifs, which was identified to be IgE-binding epitope [Tanabe, S., Arai, S., Yanagihara, Y., Mita, H., Takahashi, K. & Watanabe, M. (1996) Biochem. Biophys. Res. Commun. 219, 290Ϫ293], exhibited the highest reactivity. The next highest reactivities were observed on A-gliadin and γ-gliadin, which had not been identified as allergens.

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Section: Discussionmentioning

confidence: 99%

Identification of major wheat allergens by means of the Escherichia coli expression system

Maruyama

Ichise

Katšube

et al. 1998

European Journal of Biochemistry

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“…Consequently, the gluten proteins have been widely studied over a period in excess of 250 yr, in order to determine their structures and properties and to provide a basis for manipulating and improving end use quality (see Shewry et al 1995).…”

Section: Introductionmentioning

confidence: 99%

The structure and properties of gluten: an elastic protein from wheat grain

Shewry

Halford

Belton

et al. 2002

Phil. Trans. R. Soc. Lond. B

487

336

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The wheat gluten proteins correspond to the major storage proteins that are deposited in the starchy endosperm cells of the developing grain. These form a continuous proteinaceous matrix in the cells of the mature dry grain and are brought together to form a continuous viscoelastic network when flour is mixed with water to form dough. These viscoelastic properties underpin the utilization of wheat to give bread and other processed foods. One group of gluten proteins, the HMM subunits of glutenin, is particularly important in conferring high levels of elasticity (i.e. dough strength). These proteins are present in HMM polymers that are stabilized by disulphide bonds and are considered to form the 'elastic backbone' of gluten. However, the glutamine-rich repetitive sequences that comprise the central parts of the HMM subunits also form extensive arrays of interchain hydrogen bonds that may contribute to the elastic properties via a 'loop and train' mechanism. Genetic engineering can be used to manipulate the amount and composition of the HMM subunits, leading to either increased dough strength or to more drastic changes in gluten structure and properties.

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“…The x-type proteins possess four cysteine residues whereas the y-type ones have seven (Gupta and MacRitchie 1994;Shewry et al 1995). Cysteine residues are important determinants of the structure and properties of the gluten complex, because they are responsible for the formation of the critical inter-and intra-subunit disulfide bonds (Shewry et al 1995).…”

Section: Introductionmentioning

confidence: 99%

The Chinese bread wheat cultivar Xiaoyanmai 7 harbours genes encoding a pair of novel high-molecular-weight glutenin subunits inherited from cereal rye

et al. 2016

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The high-molecular-weight glutenin subunits (HMW-GS) represent a major component of the endosperm storage protein in the grains of wheat and its related species. Their technological importance results from their ready formation of intermolecular disulfide bonds, which underlie much of the visco-elasticity displayed by gluten and hence the processing quality of the flour. Here, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) analysis revealed that the Chinese wheat cultivar Xiaoyanmai 7 formed four distinct HMW-GS, two of which are likely the product of a known allele at the Glu-B1 locus, whereas the other two did not match any known HMW-GS. A combined analysis based on reversed-phase high-performance liquid chromatography (RP-HPLC), N-terminal sequencing and mass spectrometry confirmed that the two novel proteins were genuine HMW-GS. Inspection of the DNA sequences showed that one of the novel HMW-GS was encoded by an x-type and the other by a y-type secalin gene. A karyotypic analysis confirmed that six of the seven pairs of Xiaoyanmai 7’s D genome chromosomes (the exception was chromosome 2D) had been replaced by rye chromosomes. The y-type HMW secalin present in Xiaoyanmai 7 differed from the standard By and Dy HWM-GS by the presence of an additional cysteine residue in its C-terminal domain.

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Biotechnology of Breadmaking: Unraveling and Manipulating the Multi-Protein Gluten Complex

Cited by 262 publications

References 24 publications

Identification of major wheat allergens by means of the Escherichia coli expression system

Identification of major wheat allergens by means of the Escherichia coli expression system

The structure and properties of gluten: an elastic protein from wheat grain

The Chinese bread wheat cultivar Xiaoyanmai 7 harbours genes encoding a pair of novel high-molecular-weight glutenin subunits inherited from cereal rye

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