Recombinant Wheat Endoplasmic Reticulum Oxidoreductin 1 Improved Wheat Dough Properties and Bread Quality

Liu, Guang; Wang, Jing Jing; Hou, Yi; Huang, Yanbo; Zhang, Yaping; Li, Cun-Zhi; Li, Lin; Hu, Song-Qing

doi:10.1021/acs.jafc.6b05192

Cited by 18 publications

(30 citation statements)

References 47 publications

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“…It is believed that PDI is the physiological substrate of mammalian Ero1, and the oxidation of PDI is mainly under the assistance of Ero1 [69]. However, the oxidation of plant PDI may also require the assistance of plant Ero1 [70,71].…”

Section: Oxidoreductase Activitymentioning

confidence: 99%

“…In another study, recombinant wheat Ero1 (wEro1) was expressed and purified in Escherichia coli, and the wEro1 was added to wheat dough. By analyzing the rheological properties of the dough, such as viscoelasticity, it was found that wEro1 may promote the cross-linking of disulfide bonds, leading to the formation of gluten polymers [70]. They further investigated the properties of recombinant wEro1 containing FAD cofactor and its influence on Chinese steamed bread qualities.…”

Section: Proposed Catalytic Mechanism Of Wpdimentioning

confidence: 99%

“…These may cause a big difference between the PDI-Ero1 pathways of different species. However, since Ero1 family proteins are widely found in eukaryotes, and in wheat it was demonstrated to promote the gluten crosslinking, it could be inferred that wheat employs a similar, though not identical, PDI-Ero1 pathway to aid the reoxidation of wPDI [70]. Namely, Ero1 in wheat ER "transfers" its disulfide bonds to wPDI, and then further shuffles wPDI to the substrate protein to ensure its oxidation activity.…”

Section: Proposed Catalytic Mechanism Of Wpdimentioning

confidence: 99%

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PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly

Gao

Liang

et al. 2020

Molecules

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Disulfide bonds play a pivotal role in maintaining the natural structures of proteins to ensure their performance of normal biological functions. Moreover, biological molecular assembly, such as the gluten network, is also largely dependent on the intermolecular crosslinking via disulfide bonds. In eukaryotes, the formation and rearrangement of most intra- and intermolecular disulfide bonds in the endoplasmic reticulum (ER) are mediated by protein disulfide isomerases (PDIs), which consist of multiple thioredoxin-like domains. These domains assist correct folding of proteins, as well as effectively prevent the aggregation of misfolded ones. Protein misfolding often leads to the formation of pathological protein aggregations that cause many diseases. On the other hand, glutenin aggregation and subsequent crosslinking are required for the formation of a rheologically dominating gluten network. Herein, the mechanism of PDI-regulated disulfide bond formation is important for understanding not only protein folding and associated diseases, but also the formation of functional biomolecular assembly. This review systematically illustrated the process of human protein disulfide isomerase (hPDI) mediated disulfide bond formation and complemented this with the current mechanism of wheat protein disulfide isomerase (wPDI) catalyzed formation of gluten networks.

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Section: Oxidoreductase Activitymentioning

confidence: 99%

Section: Proposed Catalytic Mechanism Of Wpdimentioning

confidence: 99%

Section: Proposed Catalytic Mechanism Of Wpdimentioning

confidence: 99%

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PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly

Gao

Liang

et al. 2020

Molecules

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“…This result implies that acid hydrolysis generally leads to a more elastic gluten system. An increase in G 0 and a decrease in tand indicated that the quality of the gluten had improved because increased elasticity prevents gas cell breakage during fermentation (Liu et al 2017)…”

Section: Dynamic Oscillatory Testsmentioning

confidence: 99%

Effects of different molecular weight water-extractable arabinoxylans on the physicochemical properties and structure of wheat gluten

Wang

et al. 2018

J Food Sci Technol

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The effects of water-extractable arabinoxylans (WEAXs) with different molecular weights on the physicochemical properties and structure of wheat gluten were studied, a transition between b-turns in b-leaves in the structure of gluten has been demonstrated by Fourier transform infrared spectroscopy when WEAX samples were added. The ratio of weakly hydrogen-bonded b-sheets to strongly hydrogen-bonded b-sheets tended to decrease with increasing WEAX content. FT-Raman analysis demonstrated other changes in the structure of gluten concerning b-structures, the conformation of the disulfide bridges, and aromatic amino acid environments; these changes were dependent on the molecular weight of the WEAX. Native WEAXs of different molecular weights that are present as discrete fragments of the cell wall have had a negative effect on the properties of gluten. However, low molecular weight WEAX has helped gluten maintain the left-left conformation of its disulfide bonds. In addition, the gluten elasticity was reduced by the native WEAX to make it softer, but the WEAX low molecular weight impeded this process and improved the gluten network.

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“…Previous research showed that wheat endoplasmic-reticulum oxidoreductin 1 (wEro1), glucose oxidase, and pyranose oxidase could enhance mixing characteristics and viscoelastic properties of dough. 8,11 It was reported that wheat glutaredoxin together with wheat thioredoxin has a positive effect on flour and dough properties and bread making. 12 Catalase (EC 1.11.1.6), which catalyzes the decomposition of hydrogen peroxide, mostly exists in aerobic living organisms to protect the cells from oxidative stress triggered by overproduced hydrogen peroxide.…”

Section: ■ Introductionmentioning

confidence: 99%

Characterization and Exploration of Recombinant Wheat Catalase for Improvement of Wheat-Flour-Processing Quality

Zhang

Chen

et al. 2019

J. Agric. Food Chem.

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The wheat catalase gene (wcat1) was cloned and overexpressed in Pichia pastoris. The purified wCat1 exhibits its highest activity at pH 7.5 and 35 °C with K m and V max of 22.95 mM and 0.24 μmol/min, respectively. wCat1 could markedly improve the farinographic properties of dough, with the stability time increasing and degree of softening decreasing, and enhance the rheological properties of dough. wCat1 could also elevate bread-making quality, with increased specific volume of the bread and decreased hardness, gumminess, and chewiness, which are attributable to increased amounts of SDS-insoluble protein in dough, resulting in extended glutenin networks and thus larger pores in the fermented dough and bread crumb. The decrease of hydrogen peroxide and increase of free thiol groups in wCat1-treated dough suggest that the decomposition of hydrogen peroxide by wCat1 likely promotes disulfide-bond formation and thus the cross-linking of dough proteins.

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Recombinant Wheat Endoplasmic Reticulum Oxidoreductin 1 Improved Wheat Dough Properties and Bread Quality

Cited by 18 publications

References 47 publications

PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly

PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly

Effects of different molecular weight water-extractable arabinoxylans on the physicochemical properties and structure of wheat gluten

Characterization and Exploration of Recombinant Wheat Catalase for Improvement of Wheat-Flour-Processing Quality

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