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

Abstract

Recombinant wheat endoplasmic reticulum oxidoreductin 1 (wEro1) with considerable ability was expressed in Escherichia coli. The functional roles of wEro1 in flour processing quality were investigated by farinographic, rheological, texture profile analysis, electrophoresis, size exclusion chromatography, scanning electron microscopy, and Fourier transform infrared spectroscopy. wEro1 exhibited an obvious oxidation activity of sulfhydryl groups in small molecule and protein. Addition of wEro1 could strengthen the processing quality of dough, indicated by the improved mixing characteristics, viscoelastic properties, and bread qualities. These improvement effects of wEro1 could be attributed to the formation of macromolecular gluten polymers and massive gluten networks by disulfide cross-linking. Additionally, the increased β-turn structure further demonstrated the enhancement of dough strength. Moreover, the amount of peroxide in dough was improved significantly from 2.36 to 2.82 μmol/g of flour with 0.15% wEro1 treatment. Therefore, the results suggested that wEro1 is a promising novel flour improver.

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

“…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].…”

“…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.…”

“…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.…”

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

“…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)…”

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

“…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.…”