Effects on Gluten of Heating at Different Moisture Contents. II. Changes in Physico-Chemical Properties and Secondary Structure

Weegels, P.L.; Groot, A.M.G. de; Verhoek, J.A.; Hamer, R.J.

doi:10.1006/jcrs.1994.1006

Cited by 121 publications

(69 citation statements)

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“…Although it is accepted that gliadins contribute to flow and glutenins to elasticity [2], the molecular basis of the functionality of the protein network of gluten in unclear. The secondary structure of wheat proteins has generally been studied after solubilisation, sometimes involving the modification of the polypeptides [3,4]. 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].…”

Section: Introductionsupporting

confidence: 40%

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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Section: Introductionsupporting

confidence: 40%

Molecular flexibility in wheat gluten proteins submitted to heating

Hargreaves¹,

Popineau²,

Meste³

et al. 1995

FEBS Letters

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“…The gluten index values of TDWM and its mixtures with semolina were higher than those measured on doughs made of semolina only. In fact, the denaturation caused by heat treatment comes through the formation of disulfide linkages and cross-linking bonds (dityrosine formation) that strengthen the gluten network by increasing the molecular size of aggregates and thus the percentage of unextractable proteins (Lamacchia et al, 2010;Wagner & Anon, 1990;Weegels, de Groot, Verhoek, & Hamer, 1994). The yellow index (b*) of the mixtures dramatically decreased as the percentage of TDWM increased due to the presence of brown colored bran, non-volatile colored compounds of intermediate molecular mass, and brown substances of high molecular mass formed during Maillard reaction (Carpenter & Booth, 1973) consisting of unsaturated, nitrogenous polymers, and copolymers (Ames, 1992).…”

Section: Resultssupporting

confidence: 42%

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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“…These may be formed from oxidation of SH groups, but evidence for SH/SS interchange reactions has also been presented. 9,13,[28][29][30][31] Gliadin, on the other hand, more or less lacking free SH groups, is not prone to polymerize. However, glutenin has been shown to react with gliadin during heating at temperatures equal or above 90 C. 28,32,33 These polymerization and crosslinking reactions ought to decrease the mobility of the protein molecules and may also partly explain the differences in penetration behavior of glutenin, gliadin, and wheat gluten.…”

Section: Degree Of Wood Penetration Of Protein Dispersionsmentioning

confidence: 45%

Wheat gluten fractions as wood adhesives—glutenins versus gliadins

Nordqvist

Thedjil

Khosravi

et al. 2011

J of Applied Polymer Sci

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Plant proteins, such as wheat gluten, constitute attractive raw materials for sustainable wood adhesives. In this study, alkaline water dispersions of the protein classes of wheat gluten, glutenin, and gliadin were used as adhesives to bond together wood substrates of beech. The aim of the study is to measure the tensile shear strength of the wood substrates to compare the adhesive performance of glutenin and gliadin and to investigate the influence of application method and penetration of the dispersions into the wood material. A sodium hydroxide solution (0.1M) was used as dispersing and denaturing agent. Dispersions with different protein concentrations and viscosities were used, employing wheat gluten dispersions as references. Two different application methods, a press temperature of 110 C and a press time of 15 min, were employed. The tensile shear strength and water resistance of the wood substrates were compared, using a slightly modified version of the European Standard EN 204. The bond lines of the substrates were examined by optical microscopy to study the penetration and bond-line thickness. The results reveal that the adhesive properties of gliadin are inferior to that of both glutenin and wheat gluten, especially in terms of water resistance. However, the tensile shear strength and the water resistance of gliadin are significantly improved when over-penetration of the protein into the wood material is avoided, rendering the adhesive performance of gliadin equal to that of glutenin and wheat gluten. V C 2011 Wiley Periodicals, Inc. J Appl

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Effects on Gluten of Heating at Different Moisture Contents. II. Changes in Physico-Chemical Properties and Secondary Structure

Cited by 121 publications

References 0 publications

Molecular flexibility in wheat gluten proteins submitted to heating

Molecular flexibility in wheat gluten proteins submitted to heating

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

Wheat gluten fractions as wood adhesives—glutenins versus gliadins

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