The impact of heating on the unfolding and polymerization process of frozen-stored gluten

Wang, Pei; Zou, Min Ming; Tian, Mengqi; Gu, Zhenxin; Yang, Runqiang

doi:10.1016/j.foodhyd.2018.07.019

Cited by 78 publications

(32 citation statements)

References 29 publications

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“…However, high-molecular-weight glutenin subunits participating in the depolymerization reaction facilitate a weakened gluten network, resulting in decreased resistance to extension. Additionally, gluten secondary structure plays an important role in the gluten network (Nawrocka et al, 2018;Wang et al, 2018) and affects the extensographic properties of dough. Wellner et al (2005) revealed that glutenins primarily contributed to β-structures (β-sheets and β-turns), while gliadins primarily contributed to the α-helix structure.…”

Section: Extensograph Properties Of Steamed Bread Doughmentioning

confidence: 99%

Effect of baked wheat germ on the rheology and fermentation properties of steamed bread dough

Zhan

Wang

et al. 2021

J. Food Process. Preserv.

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Effect of baked wheat germ (BWG) on the extensional properties, water mobility, and fermentation properties of steamed bread dough was investigated. The extensograph properties analysis revealed that dough containing BWG exhibited a decreasing trend (p < .05) in extensibility and resistance to extension, indicating that the structure of the gluten network was weakened. Analysis of water mobility revealed that the T 22 and T 23 dramatically reduced as the level of BWG increased, decreasing water availability to the gluten matrix and reducing gluten strength. The analysis of fermentation properties showed that the presence of BWG decreased the maximum dough height, indicating that added BWG destroyed the continuous starch-gluten matrix and prevented the free expansion of wheat dough during the proofing stage.However, the total gas production of dough containing BWG was significantly higher than that of the wheat dough, revealing that the increase in levels of BWG facilitated yeast activity for the production of CO 2 . Novelty Impact StatementWe investigated the external properties, water mobility, and fermentation properties of BWG-enriched dough. The results showed that BWG decreased the extensibility and water availability, resistance to extension of dough by forming weakened gluten network structure, causing a small steamed bread volume. Our ultimate aim was to improve the utilization of wheat germ and the nutrition of BWG-enriched steamed bread. Highlights• BWG can decrease the extensibility and resistance to extension of dough by forming weakened gluten network structure.• Gluten secondary structure changes may be combined to explain the dough extensogaph properties.• BWG can decrease water availability to gluten matrix and reduced gluten strength.• BWG can prevent the free expansion of fermented dough and cause a small steamed bread volume. | INTRODUC TI ONChinese steamed bread has been a traditional staple food in China for many centuries, and the increasingly popular trend in healthy eating has led to a growing interest in several healthy foods, including bran and germ. Indeed, several studies have revealed that the addition of wheat germ enhances the nutritional value of steamed bread by increasing the concentration of minerals, proteins, and fat compared with steamed bread prepared from pure wheat flour (Fatma et al., 2018;

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Section: Extensograph Properties Of Steamed Bread Doughmentioning

confidence: 99%

Effect of baked wheat germ on the rheology and fermentation properties of steamed bread dough

Zhan

Wang

et al. 2021

J. Food Process. Preserv.

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“…Increasing the temperature to more than 60–90°C significantly increased G ′ and G ″, possibly attributed to numerous reasons such as aggregate formation consolidation of attractive forces (Van der Waals forces and hydrogen bonding) between protein aggregates (Hua, Cui, Wang, Mine, & Poysa, 2005; Spotti et al, 2014) and covalent (SS) cross‐linking generation (Savadkoohi & Farahnaky, 2012; Wang, Zou, Tian, et al, 2018). The fluorescence peak intensity once increased to 354.5 nm with the increase in the gelling temperature from 60 to 90°C.…”

Section: Physical Modificationmentioning

confidence: 99%

“…Glutenin may be polymerized upon the oxidation of sulfhydryl groups while sulfhydryl‐disulfide interchange may be the main mechanism for the cross‐linking of gliadin (Singh & MacRitchie, 2004). According to the results of nonreducing SDS‐PAGE, high molecular gluten aggregates are formed with low solubility in the sample buffer in accordance with the reduced intensity band of HMW‐GS due to oxidation and the subsequent polymerization of glutenin upon sulfhydryl (SH)‐SS exchange (Wang, Zou, Tian, et al, 2018).…”

Section: Physical Modificationmentioning

confidence: 99%

“…Meanwhile, the cryo shrinking process of the gluten and glutenin network prevents ice recrystallization, attributed to the minimized interstitial areas of the protein separating adjacent ice crystals (Wang, Chen, et al, 2014; Wang, Tao, et al, 2014; Wang, Xu, et al, 2014); (iii) water redistribution is accelerated by the incorporation of solutes such as salt and sucrose due to the decrease in the ice melting temperature and increased unfrozen water content of dough (Laaksonen & Roos, 2001; Wang, Chen, et al, 2014; Wang, Tao, et al, 2014; Wang, Xu, et al, 2014); nonetheless, natural additives, namely surfactants, dairy whey proteins, and certain enzymes have been utilized to control the water redistribution problem in the dough structure during the storage condition (Asghar, Anjum, & Allen, 2011); (iv) the temperature fluctuation; (v) breakage of SS bonds and increased SH content, and (vi) high amounts of gliadin, possibly facilitating the disaggregation of GMP during the frozen storage as a result of the barrier role of glutenin network formation (Melnyk, Dreisoerner, Marcone, & Seetharaman, 2012; Wang, Xu, et al, 2014; Zhao et al, 2012). Wang, Zou, Gu, et al (2018) and Wang, Zou, Tian, et al (2018) reported that that disulfide‐mediated polymerization of frozen‐stored gluten was suppressed upon heating at 95°C. Meanwhile, the polymerization ability of gliadin was higher than glutenin following frozen‐stored gluten.…”

Section: Physical Modificationmentioning

confidence: 99%

See 1 more Smart Citation

Physical modifications of wheat gluten protein: An extensive review

Abedi

Pourmohammadi²

2020

J Food Process Engineering

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Gluten protein, as plant resource, is susceptible to physical, genetic, chemical, and enzymatic treatments. In this study, we reviewed physical modifications such as heating‐ freezing, irradiation, high pressure, ultrasonication, shear, and extrusion of gluten. The mode of action of each modification process was investigated. Conformational changes (secondary and tertiary structure) of gluten protein upon physical modification process were described. Functional, morphological, textural, and rheological properties of gluten and their subunits through physical modification were studied. Among physical modifications, the gluten structure was affected by extrusion (heating‐shearing) process. The combination of additives (oxidative and reducing compounds) and alkaline pH upon the extrusion process result in concomitantly dissociation or/and aggregation of gluten via various interactions mainly covalent (disulphide, isopeptides bonds, and dityrosine), noncovalent (hydrogen, ionic, and hydrophobic bonds) interactions and other bonds, such as, dehydroalanine (DHA), lanthioalanine (LAN), and lysinoalanine (LAL). Practical applications Attaining an environment friendly and resource protecting provide global value chain and keep on economic development, which has properly been the major target of the most countries. The physical modifications of protein structure are more widely employed since it is safer and without impurities, which have strong effects on different component functionalities. Today, there is a highly increased demand for applying modification‐using technologies; such as ultrasound, extrusion cooking, high hydrostatic pressure, irradiation, which do not rely on chemical treatment for altering ingredient functional and reological properties. We underscored the importance of filling the gaps of knowledge concerning various kinds of physical modification research to alter the disulphide and other interactions, which modified gluten will be suitable in different food and nonfood applications. The additional point is that a better understanding of the correlation between structure and functionality of gluten proteins when they undergo physical modification in combination with additives, such as dough improvers, gums, and surfactant.

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“…Gluten may be regarded as highly nutritious as it contains a small quantity of starch, fat and mineral substances [2][3] . Gluten protein has been used as an additive in food, fodder and other industries [4] . The enrichment of hydrophobic amino acids (such as glutamic acid, leucine, proline) in gluten protein facilitates the formation of a larger hydrophobic interaction area in gluten protein [5][6] .…”

Section: Introductionmentioning

confidence: 99%

Improvement of Foaming and Emulsifying Properties of Gluten by Conjugation with Fructose through Maillard Reaction

Song¹,

Qin²,

Yang³

et al. 2018

Grain & Oil Sci. and Technol.

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Tuning the optical properties of BODIPY dye through Cu(I)catalyzed azide-alkyne cycloaddition(CuAAC)reaction SCIENTIA SINICA Chimica 42, 231 (2012); Tuning the optical properties of BODIPY dye through Cu(I) catalyzed azide-alkyne cycloaddition (CuAAC) reaction SCIENCE CHINA Chemistry 55, 125 (2012);Abstract: Gluten has poor emulsifying and foaming ability due to its amino acid composition. In this study, Maillard reaction was used to improve the emulsifying and foaming properties of gluten. The processing conditions for the preparation of gluten-fructose conjugates were optimized by using Box-Behnken model to achieve optimum foaming and emulsifying activity, respectively. The results showed that glycated gluten exhibited enhanced emulsifying activity compared to native control. The processing conditions for the preparation of gluten-fructose conjugates with optimum emulsifying activity were as follows: the temperature was 48˝C, reaction time was 72 h, and maltose/gluten (W/W) ratio was 125%. Under such condition, the average emulsifying activity was 66.54%, being improved by about 2.5 times compared with that of native control. The Foaming properties of gluten also increased significantly by glycation modification. The optimum conditions of response were as below: the temperature was 48˝C, reaction time was 66 h, and maltose/gluten ratio (W/W) was 110%. Under such condition, the average foaming property was 158.57%, and it was three folds higher than that of the control.

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The impact of heating on the unfolding and polymerization process of frozen-stored gluten

Cited by 78 publications

References 29 publications

Effect of baked wheat germ on the rheology and fermentation properties of steamed bread dough

Effect of baked wheat germ on the rheology and fermentation properties of steamed bread dough

Physical modifications of wheat gluten protein: An extensive review

Improvement of Foaming and Emulsifying Properties of Gluten by Conjugation with Fructose through Maillard Reaction

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