FTIR and NMR studies on the hydration of a high-Mr subunit of glutenin

Belton, Peter; Colquhoun, Ian J.; Grant, Alex; Wellner, Nikolaus; Field, Jacqueline; Shewry, Peter R.; Tatham, Arthur S.

doi:10.1016/0141-8130(95)93520-8

Cited by 183 publications

(120 citation statements)

References 31 publications

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“…Although it is now widely accepted that disulphidelinked glutenin chains provide an 'elastic backbone' to gluten, evidence from spectroscopic studies (using NMR and FTIR spectroscopy) of HMM subunits and of model peptides based on the repeat motifs suggests that non-covalent hydrogen bonding between glutenin subunits and polymers may also be important (Belton et al 1994(Belton et al , 1995(Belton et al , 1998Wellner et al 1996;Gilbert et al 2000). These studies have shown that the dry proteins are disordered with little regular structure, but that their mobility increases and β-sheet structures form on hydration.…”

Section: Hmm Subunit Structure and Gluten Elasticitymentioning

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

479

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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Section: Hmm Subunit Structure and Gluten Elasticitymentioning

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

479

336

View full text Add to dashboard Cite

show abstract

“…hydrogen bonds) between glutenin subunits and polymers may also contribute to elasticity. Evidence for this comes from nuclear magnetic resonance (NMR) and Fourier-transform infra-red (FT-IR) of high molecular weight subunits and model proteins and peptides [16][17][18][19] and may be summarised as follows:…”

Section: Subunit Interactions and Gluten Visco-elasticitymentioning

confidence: 99%

Wheat glutenin subunits and dough elasticity: findings of the EUROWHEAT project

Shewry

Popineau²,

Lafiandra³

et al. 2000

Trends in Food Science & Technology

228

137

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Detailed studies of wheat glutenin subunits have provided novel details of their molecular structures and interactions which allow the development of a model to explain their role in determining the visco-elastic properties of gluten and dough. The construction and analysis of near-isogenic and transgenic lines expressing novel subunit combinations or increased amounts of specific subunits allows differences in gluten properties to be related to the structures and properties of individual subunits, with potential benefits for the production of cultivars with improved properties for food processing or novel end users #

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“…However, recent attenuated total reflection infra-red (ATR-IR) studies on functional gluten indicated a decrease of intra-and mainly inter-molecular B-sheet conformation when proteins in a doughy state are solubilised [5,6]. An IR study on alkylated and unalkylated high molecular weight glutenin subunits showed an increase in/3-sheet type structure upon hydration, and an enhancement of low energy intermolecular interactions in the presence of disulfide bonds [7]. No difference was found by LH and 13C NMR spectroscopy between hydrated gluten, glutenin enriched fraction and gliadin enriched fractions at 30°C.…”

Section: Introductionmentioning

confidence: 99%

Molecular flexibility in wheat gluten proteins submitted to heating

Hargreaves¹,

Popineau²,

Meste³

et al. 1995

FEBS Letters

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Prolamin proteins are responsible for the network that gives wheat dough its viscoelastic properties. Non-prolamin depleted gluten was prepared under conditions that preserve its functionality. Electron Spin Resonance (ESR) was used to provide information about the dynamics of the protein at temperatures between 5 and 90°C by specific spin labelling of its cysteine residues. The spectra were of a composite type, resulting from at least two populations of spin labels largely differing in molecular mobility. The correlation time of the less mobile nitroxide radicals was determined by saturation transfer ESR. Upon heating there was a transfer from the slow to the fast moving population of radicals, and an increase of mobility of this last catagory that followed the Arrbenins law. The effect of temperature on molecular flexibility was reversible. This was not the case for purified, polymerised glutenin subunits extracted from gluten. Urea created similar modifications on gluten as heat.Key words: Prolamin; Gluten; ESR; ST-ESR; Temperature; Urea segmental mobility in the proteins in D20 was high (~65%) and increased with temperature.Electron spin resonance (ESR) spectroscopy can yield information about polymer networks by the use of a stable paramagnetic compound [9]. Spin probing informs about the solvent environment, whilst covalent spin labelling reflects the segmental mobility of labelled molecules. Previous work has proven the usefulness of ESR spectroscopy in understanding the properties of functional gluten. Spin probing showed a compartimentation of the liquid phase of hydrated gluten, namely, the existence of a lipid and of an aqueous phase [10,11], and of two different microenvironments in the water phase [12,13]. The polypeptide flexibility was found to depend on the gliadin/ glutenin ratio and on the organisation of glutens 00,11].To improve our understanding of the organisation of gluten and of the interactions in the protein network, we investigated, in this paper, the effect of temperature and chemical denaturation on the molecular flexibility of gluten and glutenin subunits by ESR and saturation transfer (ST)-ESR.

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FTIR and NMR studies on the hydration of a high-Mr subunit of glutenin

Cited by 183 publications

References 31 publications

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

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

Wheat glutenin subunits and dough elasticity: findings of the EUROWHEAT project

Molecular flexibility in wheat gluten proteins submitted to heating

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