Protein network analysis — A new approach for quantifying wheat dough microstructure

Bernklau, Isabelle; Lucas, Isabelle; Jekle, Mario; Becker, Thomas

doi:10.1016/j.foodres.2016.10.012

Cited by 107 publications

(64 citation statements)

References 20 publications

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“…Higher protein area (indicating a low aperture area) and protein junction (related to the junction density and branching rate) values indicate that the gluten network has greater connectivity [37]. The lacunarity represents the amount of gaps and irregularities in a protein network and it is positively correlated with dough development time and dough stability time, whereas the protein endpoints and endpoint rate are negatively correlated with those properties [25].…”

Section: Linementioning

confidence: 99%

Effects of Nitrogen Application in the Wheat Booting Stage on Glutenin Polymerization and Structural–Thermal Properties of Gluten with Variations in HMW-GS at the Glu-D1 Locus

Song

Zhao

et al. 2020

Foods

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Wheat gluten properties can be improved by the application of nitrogen. This study investigates the effects of nitrogen application in the booting stage on glutenin polymerization during grain-filling and structural–thermal properties of gluten based on the high-molecular-weight glutenin subunits (HMW-GSs) using near-isogenic lines (Glu-1Da and Glu-1Dd). The nitrogen rate experiment included rates of 0, 60, 90, and 120 kg N ha−1 applied with three replicates. Nitrogen significantly improved the grain quality traits (wet gluten contents, Zeleny sedimentation values, and maximum resistance) and dough strength (dough development time, dough stability time, and protein weakening), especially in wheat with the Glu-1Da allele. Nitrogen increased the protein composition contents, proportions of glutenins and HMW-GSs, and disulfide bond concentration in the flours of Glu-1Da and Glu-1Dd, and accelerated the polymerization of glutenins (appearing as glutenin macropolymer) during grain-filling, where nitrogen enhanced the accumulation and polymerization of glutenins more for line containing Glu-1Da than Glu-1Dd. The β-sheets, α-helix/β-sheet ratio, microstructures, and thermal stability were also improved to a greater degree by nitrogen for gluten with Glu-1Da compared to Glu-1Dd. Nitrogen treatment was highly effective at improving the gluten structural‒thermal properties of wheat in the booting stage, especially with inferior glutenin subunits.

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Section: Linementioning

confidence: 99%

Effects of Nitrogen Application in the Wheat Booting Stage on Glutenin Polymerization and Structural–Thermal Properties of Gluten with Variations in HMW-GS at the Glu-D1 Locus

Song

Zhao

et al. 2020

Foods

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“…The quality of biscuit is closely related to properties of gluten proteins (gliadin and glutenin) owing to its unique viscoelasticity (Delcour et al., 2012). The gluten can form a continuous network in the dough when flour is mixed with water (Leon et al., 2010), which confers to water absorption capacity and gas retention of wheat dough (Bernklau, Lucas, Jekle, & Becker, 2016). Numerous studies have reported that higher protein levels in wheat flour induced more gluten network formation, which led to a smaller diameter and firmer textured biscuit (Pareyt, Wilderjans, Goesaert, Brijs, & Delcour, 2008; Pauly, Pareyt, Lambrecht, Fierens, & Delcour, 2013; Zhou et al., 2018).…”

Section: Introductionmentioning

confidence: 99%

“…The properties of gluten are determined by its microstructure and composition (Bernklau et al., 2016; Gao et al., 2018; Wang et al., 2014). The secondary structures of gluten were divided into intermolecular β‐sheets, antiparallel β‐sheets, α‐helices, β‐turns, and β‐sheets (Wang et al., 2014).…”

Section: Introductionmentioning

confidence: 99%

Relationships of protein composition, gluten structure, and dough rheological properties with short biscuits quality of soft wheat varieties

et al. 2020

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Understanding the contribution of protein composition and gluten structure to dough property and biscuit baking is crucial to improve soft wheat (Triticum aestivum L.) grain quality. Thus, the relationships of protein composition, gluten structure, and dough rheological properties with short biscuits quality was investigated using 10 Chinese soft wheat varieties. Content of grain protein, flour protein, gliadin, glutenin, and high and low molecular weight glutenin subunits were significantly positively correlated with hardness of biscuit, but negatively correlated with spread factor and sensory score. Gluten of wheat varieties with lower dough strength and better biscuit quality showed thinner walls of apertures and more regular apertures in its microstructure. The gluten with higher strength had more apertures and antiparallel β-sheets and fewer α-helices. Moreover, dough with a higher softening degree was easier to stretch and tended to produce biscuits with larger diameter and crispier taste during baking. In conclusion, main wheat quality characteristics that can be used to select grain samples suitable for making tasty biscuits were recommended as follows: flour protein content, wet gluten content and microstructure, Zeleny sedimentation value, and dough softening degree.

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“…Changes in the gluten microstructure are detectable at macroscopic scale as alterations in dough rheology (Jekle and Becker, 2013;Lee et al, 2001;Peighambardoust et al, 2006). The impact of water (Bernklau et al, 2016;Létang et al, 1999) and redox agents (Bernklau et al, 2017;Lucas et al, 2018a) on gluten microstructure in wheat dough has been investigated.…”

Section: Introductionmentioning

confidence: 99%

“…Although it is thus well known how gluten during heating changes on molecular scale, the impact of these changes on its microstructure remains unknown. We here used CLSM and protein network analysis (PNA) (Bernklau et al, 2016) to study heat induced changes in gluten in non-fermented dough on microscale and related the outcome of literature data on the corresponding molecular scale changes. The main originality of the study resides in the use of Aq1.…”

Section: Introductionmentioning

confidence: 99%

Microscopic investigation of the formation of a thermoset wheat gluten network in a model system relevant for bread making

Verbauwhede

Lambrecht

Jekle

et al. 2019

Int J of Food Sci Tech

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Although the impact of heat on molecular properties of wheat gluten is well understood, changes in its microstructure have rarely been studied. Here, formation of the thermoset gluten network in a model system relevant for bread baking was studied with confocal laser scanning microscopy and protein network analysis. From 65 °C onwards, gluten converts from thick aligned protein strands in a highly branched and homogeneous network of small thin protein threads. Neither gliadin incorporation in the network nor application of aqualysin 1, the thermo-active serine peptidase from Thermus aquaticus which recently has been reported to hydrolyze gluten proteins in dough only at temperatures exceeding 80 °C, impacts on the gluten microstructure. As starch causes structure setting itself and thereby decreases protein mobility, molecular scale changes in the gluten network at temperatures exceeding 80 °C brought about by aqualysin 1 do not impact its microstructure.

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Protein network analysis — A new approach for quantifying wheat dough microstructure

Cited by 107 publications

References 20 publications

Effects of Nitrogen Application in the Wheat Booting Stage on Glutenin Polymerization and Structural–Thermal Properties of Gluten with Variations in HMW-GS at the Glu-D1 Locus

Effects of Nitrogen Application in the Wheat Booting Stage on Glutenin Polymerization and Structural–Thermal Properties of Gluten with Variations in HMW-GS at the Glu-D1 Locus

Relationships of protein composition, gluten structure, and dough rheological properties with short biscuits quality of soft wheat varieties

Microscopic investigation of the formation of a thermoset wheat gluten network in a model system relevant for bread making

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