Effects on Gluten of Heating at Different Moisture Contents. I. Changes in Functional Properties

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

doi:10.1006/jcrs.1994.1005

Cited by 88 publications

(50 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Free sulfhydryls were determined colorimetrically after reaction with 5,5c-dithio-bis(2-nitrobenzoic acid) (Elman reagent) by the procedure proposed by Lagrain et al [10]. Rheologically active disulfide bonds were determined by the method of Weegels et al [6] as modified by Hayta and Shofield [18].…”

Section: Methodssupporting

confidence: 40%

“…However, their mechanism of action in forming the gluten protein complex with its unique rheological properties is as yet unknown. Some researchers [4][5][6][7][8] have reported a direct dependence of gluten quality and dough physical properties on the content of disulfide bonds in the gluten proteins. Others [9][10][11][12] suggested that the gluten quality is determined not by the number of disulfide bonds but the rate of their rupture and reformation in thiol-disulfide exchange reactions.…”

mentioning

confidence: 46%

See 1 more Smart Citation

Rheological properties of Uzbekistan wheat gluten as a function of disulfide and h-bond contents during conditioning

Korableva

Kasymova

2010

Chem Nat Compd

View full text Add to dashboard Cite

Rheological properties of wheat gluten as a function of the presence of free sulfhydryls and disulfide bonds in addition to their ratio during various conditioning regimes were studied. It was shown that coagulation of the gluten as the temperature increased was accompanied by a decrease in the number of free sulfhydryls and an increase in the number of rheologically active disulfide bonds. Changes occurring in the gliadin and glutenin fractions during various conditioning regimes were seen using IR spectroscopy. It was found that the relative strength of absorption bands due to H-bonds increased as the treatment temperature was raised above 60°C. Significant changes in the protein molecule structure that caused substantial changes in its rheological properties because of thiol-disulfide exchange reactions and H-bond strength occurred during the conditioning.Wheat gluten is an unusually complicated complex of heterogeneous protein components that form a three-dimensional network of linearly cross-linked glutenin subunits and gliadin components through hydrogen, hydrophobic, and disulfide bonds [1]. It is known that the rheological properties of gluten and dough that determine the culinary value of wheat flour are closely related to the presence and quantitative ratio of disulfide and sulfhydryl groups in the wheat grain proteins in addition to the presence in the flour of low-molecular-weight thiols and disulfides [2]. Disulfide bonds fulfill important functions for maintaining the native conformation of the protein molecules [3]. However, their mechanism of action in forming the gluten protein complex with its unique rheological properties is as yet unknown. Some researchers [4][5][6][7][8] have reported a direct dependence of gluten quality and dough physical properties on the content of disulfide bonds in the gluten proteins. Others [9][10][11][12] suggested that the gluten quality is determined not by the number of disulfide bonds but the rate of their rupture and reformation in thiol-disulfide exchange reactions. Bogdanov et al. [8] analyzed the number of disulfide bonds and sulhydryl groups in wheat reserve proteins and concluded that gluten proteins of different quality were practically identical with respect to total content of disulfide bonds and that the gluten quality depended on only a certain part of the rheologically active disulfide bonds.Until now, published data have not allowed an accurate assessment of the distinguishing features of gluten protein fractions (gliadin and glutenin), the type of bonds between its components, and the forms of interactions in the protein complex on which the specific rheological properties of gluten that are responsible for its quality depend.Our goal was to demonstrate the influence of wheat grain moist-heat treatment (conditioning) on gluten and its fractions as related to the gluten rheological properties and content of free sulfhydryls and disulfide and H-bonds.Conditioning of wheat grain is an important stage in the processing scheme for producing flour that ca...

show abstract

Section: Methodssupporting

confidence: 40%

mentioning

confidence: 46%

Rheological properties of Uzbekistan wheat gluten as a function of disulfide and h-bond contents during conditioning

Korableva

Kasymova

2010

Chem Nat Compd

View full text Add to dashboard Cite

show abstract

“…The MW of gluten aggregates and protein extractability is dependent on the heating condition, hydrostatic pressure and moisture content attributed to oxidation of SH groups and SH-disulfide interchange reactions which forms intermolecular bonds (Kieffer et al, 2007;Lagrain et al, 2005;Singh and MacRitchie, 2004;Weegels et al, 1994). The formation or cleavage of disulfide bonds is stimulated by the application of redox agents (potassium bromate, potassium iodate and reducing agent dithiothreitol [DTT]) on the gluten proteins.…”

Section: Introductionsupporting

confidence: 40%

“…GS extractability in the glutenin fraction was found to be 4, 23 and 57% for the D-LMW-GS, HMW-GS and B/C-LMW-GS, respectively (Delcour and Hoseney, 2010;Wieser, 2007;Veraverbeke and Delcour, 2002). With thermomolding at 130 and 150°C in 5 and 25 min was a reduction and distribution in D-LMW-GS and HMW-GS as protein polymerization occurred due to the repetitive sequence of cysteine residue (Kieffer et al, 2007;Lagrain et al, 2005;Singh and MacRitchie, 2004;Weegels et al, 1994). There was increased extractabililty of B/C-LMW-GS with thermo-molding as the repetitive amino acid chains were broken down due to the thermal effects.…”

Section: Glutenin Composition and Extractabilitymentioning

confidence: 42%

The composition and extractability of thermo - molded wheat gluten bio-plastics

Fisseha¹

2016

Afr. J. Food Sci.

View full text Add to dashboard Cite

The study was aimed to evaluate the effect of thermo-molding on gluten and gluten fractions composition and its extractability with 1.0 ml 0.05 M sodium phosphate buffer (pH 6.8) with 2.0% sodium dodecyl sulfate (SDS) at 130 and 150°C for 5 and 25 min. The gluten, gliadin and glutenin composition as affected by thermo-molding was analysed with reverse phase high performance liquid chromatography (RP-HPLC) and amino acid was analysed with acid hydrolysis using high-performance anion-exchange chromatography with integrated pulsed amperometric detection (HPAEC-IPAD). The extractability and composition were significantly affected. Gluten extracts were found in equivalent proportions; gliadin (51%) and glutenins (49%). Gluten, gliadin and glutenin subunits (GS) extracts were significantly affected and a reduction with increased molding condition explains the occurrence of polymerization reactions due to SH-disulfide interchange reactions. The glutenin fraction contains 15% gliadin while the gliadin fraction contains 2.5% glutenin after extraction with 60% ethanol. The extractability of the gliadin types and GS decreased with increasing molding time and temperature.

show abstract

“…Reactivity studies based on pure gluten show a similar trend (Weegels, Verhoek, De Groot & Hamer, 1994), with major changes in the protein's solubility occurring when the gluten was heated at 80 ℃ at a moisture content of 25-30% (comparable to the conditions used when pasta drying is carried out at high temperatures). The main changes are accounted for by glutenin fractions, as gliadins only react at temperatures higher than 100 ℃ (Singh & MacRitchie, 2004).…”

Section: Dryingmentioning

confidence: 44%

Mechanism of reduction in starch digestion rate of Durum Wheat by protein

Zou¹

View full text Add to dashboard Cite

The aim of the project is to explore the mechanism of durum wheat proteins in slowing starch digestion; this reduction in digestion rate is nutritionally advantageous. The grains of three commercial durum wheat varieties (Jandaroi, Caparoi and Yawa) were employed, from which a range of pasta-derived cooked substrates were prepared: semolina (SE), whole pasta (spaghetti) (WP), powdered pasta (PP) and extracted starch (ST). SE contains inherent protein components; WP has an intact compact structure and gluten network formed by kneading and extruding the SE proteins; PP was ground from WP, thus breaking up the intact compact structure while the gluten network remained intact; and ST was extracted from SE with removal of proteins. To understand how pasta compact structure and proteins influence starch digestion, all these starch-containing samples with different protein composition and structure were subjected to in vitro digestion with various combinations of treatments mimicking gastric conditions with acid and pepsin, before the starch was digested with porcine α-amylase or pancreatin. After plotting the percentage of starch digested vs. time, first-order kinetics characterization through logarithm-of-slope analysis and morphological characterization by confocal microscopy were combined to reveal how the pasta compact structure and gluten network together slow starch digestion rate. Digested samples were collected at different times to characterize the weight distributions of branched starch molecules (wbr (logR h ), R h being hydrodynamic radius) using size-exclusion chromatography (SEC, also termed GPC). These distributions, together with the measured activity of α-amylase in the digestive solution, were used to explore the role that the compact structure and proteins in pasta play in retarding the evolution of starch molecular structure during digestion. Gluten powder (GP) extracted from SE was cooked and centrifuged to separate supernatant from gluten as a pellet, followed by the addition of α-amylase, to characterize to what extent α-amylase interacted with wheat proteins by measuring the activity of α-amylase, to elucidate if the protein components are capable of reducing enzymatic II activity; the analytical technique used was high performance liquid chromatography-mass spectrometry (LC-MS).The results showed that ST and SE were digested following simple first-order kinetics, while WP and PP followed two sequential first-order steps. The rate coefficients for these various steps were altered by pepsin hydrolysis. Confocal microscopy revealed that, following cooking, starch granules were completely swollen for ST, SE and PP samples. In WP, the granules were completely swollen in the external regions, partially swollen in the intermediate region and almost intact in the WP strand center. Gluten entrapment accounts for the sequential kinetic steps in the digestion of pasta starch; the compact microstructure of pasta also reduces digestion rates. A reduced activity of porcine α-amylase and retarded dig...

show abstract

Effects on Gluten of Heating at Different Moisture Contents. I. Changes in Functional Properties

Cited by 88 publications

References 0 publications

Rheological properties of Uzbekistan wheat gluten as a function of disulfide and h-bond contents during conditioning

Rheological properties of Uzbekistan wheat gluten as a function of disulfide and h-bond contents during conditioning

The composition and extractability of thermo - molded wheat gluten bio-plastics

Mechanism of reduction in starch digestion rate of Durum Wheat by protein

Contact Info

Product

Resources

About