The Structure of the Gluten Network in Dough: a Study using Environmental Scanning Electron Microscopy

Bache, I. C.; Donald, Athene M.

doi:10.1006/jcrs.1997.0176

Cited by 79 publications

(40 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…[21][22][23] Conventional scanning electron microscopy (SEM) observations of dough and gluten, [24][25][26] cryo-SEM 3,27-31 examination of dough as well as confocal scanning laser microscopy investigations [32][33][34] of dough and gluten revealed a gluten network at a micron scale. However, the three-dimensional fibrous network of gluten could not be observed by environmental SEM (ESEM), 35,36 which revealed a continuous gluten phase with collapsed structure. As is evident, the view for the microstructure of hydrated gluten is not yet conclusive.…”

Section: Introductionmentioning

confidence: 91%

“…Bache and Donald 35 proposed that a fibrous network might exist at shorter length scale, i.e., at the molecular level. Cryo- Fig.…”

Section: Microstructurementioning

confidence: 99%

“…The model proposed from studies using ESEM 35,36 is that gluten forms into sheets as opposed to fibers. Bache and Donald 35 proposed that a fibrous network might exist at shorter length scale, i.e., at the molecular level.…”

Section: Microstructurementioning

confidence: 99%

See 2 more Smart Citations

Calorimetric and Microstructural Investigation of Frozen Hydrated Gluten

Kontogiorgos

Goff

2006

Food Biophysics

View full text Add to dashboard Cite

The thermal and microstructural properties of frozen hydrated gluten were studied by using differential scanning calorimetry (DSC), modulated DSC, and lowtemperature scanning electron microscopy (cryo-SEM). This work was undertaken to investigate the thermal transitions observed in frozen hydrated gluten and relate them to its microstructure. The minor peak that is observed just before the major endotherm (melting of bulk ice) was assigned to the melting of ice that is confined to capillaries formed by gluten. The Defay-Prigogine theory for the depression of melting point of fluids confined in capillaries was put forward in order to explain the calorimetric results. The pore radius size of the capillaries was calculated by using four different empirical models. Kinetic analysis of the growth of the pore radius size revealed that it follows firstorder kinetics. Cryo-SEM observations revealed that gluten forms a continuous homogeneous and not fibrous network. Results of the present investigation showed that is impossible to assign a T g value for hydrated frozen gluten because of the wide temperature range over which the gluten matrix vitrifies, and therefore the construction of state diagrams is not feasible at subzero temperatures for this material. Furthermore, the gluten matrix is deteriorated with two different mechanisms from ice recrystallization, one that results from the growth of ice that is confined in capillaries and the other from the growth of bulk ice.

show abstract

Section: Introductionmentioning

confidence: 91%

“…Bache and Donald 35 proposed that a fibrous network might exist at shorter length scale, i.e., at the molecular level. Cryo- Fig.…”

Section: Microstructurementioning

confidence: 99%

See 1 more Smart Citation

Calorimetric and Microstructural Investigation of Frozen Hydrated Gluten

Kontogiorgos

Goff

2006

Food Biophysics

View full text Add to dashboard Cite

show abstract

“…Increasingly, the commonly accepted view of dough microstructure is being challenged by recent observations on hydrated gluten utilizing environmental-SEM and cryo-SEM. These revealed a continuous gluten phase with a collapsed structure forming a network arranged in sheets rather than fibers (Bache & Donald, 1998;Kontogiorgos & Goff, 2006;Nicolas et al, 2003;Roman-Gutierrez, Guilbert, & Cuq, 2002).…”

Section: Electron Microscopy Of Flour-water Mixturesmentioning

confidence: 98%

Effect of aging and ice-structuring proteins on the physical properties of frozen flour–water mixtures

2008

View full text Add to dashboard Cite

“…When the cross-links are predominantly formed by disulphide bonds, occurring both within single polypeptide chains and between polypeptides, the gluten shows good technological characteristics (Bache & Donald 1998). Thus, the …”

Section: Sds-page Of Gluten Proteinsmentioning

confidence: 99%

Composition, protein contents, and microstructural characterisation of grains and flours of emmer wheats (Triticum turgidum ssp. dicoccum) of the central Italy type

Giacintucci¹,

Guardeño²,

Puig³

et al. 2014

Czech J. Food Sci.

View full text Add to dashboard Cite

Giacintucci V., Guardeño L., Puig A., Hernando I., Sacchetti G., Pittia P. (2014) The microstructural characteristics were evaluated of two types of Italian Farro (Triticum turgidum ssp. dicoccum) with spring and autumn growth habits, the former with a vitreous tendency and the latter with a floury tendency. Common wheat flours and grains (Triticum aestivum) were used as controls. Protein fractions such as glutenin and gliadin were extracted from Triticum turgidum ssp. dicoccum flours and studied by SDS-PAGE in order to make a comparison between the electrophoretic analyses and microstructural studies which were conducted on the same samples using Scanning Electron Microscopy (SEM and Cryo-SEM). The results obtained by SDS-PAGE showed that the gliadin patterns of both emmer samples were similar, while the common wheat gliadins showed a band at 90 kDa that was not present in the gliadin fraction of emmer. When the glutenin patterns were analysed, the autumn emmer did not show the low molecular weight protein bands (16-23 kDa) whilst spring emmer wheat appeared more similar to common wheat. Regarding the microstructural characteristics of the kernels, spring (vitreous tendency) emmer showed starch granules covered by protein to a higher extent than autumn emmer. These differences were also observed in flours. The gluten of spring emmer wheat was observed as a homogeneous structure showing similarities with common wheat gluten, while autumnal emmer gluten appeared more heterogeneous and lacking in structure.

show abstract

The Structure of the Gluten Network in Dough: a Study using Environmental Scanning Electron Microscopy

Cited by 79 publications

References 0 publications

Calorimetric and Microstructural Investigation of Frozen Hydrated Gluten

Calorimetric and Microstructural Investigation of Frozen Hydrated Gluten

Effect of aging and ice-structuring proteins on the physical properties of frozen flour–water mixtures

Composition, protein contents, and microstructural characterisation of grains and flours of emmer wheats (Triticum turgidum ssp. dicoccum) of the central Italy type

Contact Info

Product

Resources

About