Abstract
Purpose: To investigate the effects of ozone treatment on chemical and physical properties of wheat ( Triticum aestivum L.) gluten, glutenin and gliadin. Methods: Wheat proteins isolated from wheat flour were treated with ozone gas. The physical and chemical properties of gluten proteins were investigated after treatment with ozone gas, with 5 g/h produced as a function of time (0, 30, and 60 min) in the study. To check whether the process of ozonation promoted changes in the quality of gluten proteins, sulfhydryl groups (SH), differential scanning calorimetry (DSC), secondary structure, SDS-PAGE, and rheology analyses were performed. Results: Sulfhydryl group contents of wheat proteins ranged from 1.1 to 7.12 μmol/g. Sulfhydryl group content for all ozonated proteins was significantly lower than that of the control samples. Gluten proteins showed reduced SDS-PAGE band intensities of both high (HMW) gluten and glutenin subunits with increasing ozone gas treatment. The denaturation temperatures (Td) of ozonated gluten proteins were higher (99.80–106.79 °C) and the enthalpies of the ozonated gluten proteins were lower than those of the control samples. The storage moduli (G') and loss moduli (G”) of gluten and glutenin tended to increase from 7.84 to 10.20 KPa and 43.19 to 48.28 KPa, and from 3.33 to 4.06 KPa and 20.74 to 22.56 KPa, respectively, as ozone exposure increased from 0 to 30 min. Conclusion: Ozone gas can oxidize wheat proteins. Exposing wheat proteins to ozone gas for an extended time (60 min) deteriorated wheat protein quality. Keywords: Ozone treatment, Gluten proteins, Chemical changes, Rheological studies, CD spectroscopy, Thermal properties
Highlights
Wheat (Triticum aestivum L.) gluten is very important for bread making
The physiochemical properties of proteins isolated from non-ozone-treated flour were examined by studying chemical characteristics using SDSPAGE, free sulfhydryl groups (SH) groups, differential scanning calorimetry (DSC) parameters, secondary structure, and rheological measurements
Fourier transforms infrared (FTIR) spectra were recorded on an FTIR spectrophotometer (NEXUS, Thermo., US) with single-reflection diamond attenuated total reflection (ATR) and mercury-cadmium-telluride (MCT) detectors
Summary
Wheat (Triticum aestivum L.) gluten is very important for bread making. Grain proteins are classically divided into two fractions. The physiochemical properties of proteins (i.e., gluten, glutenin, and gliadin) isolated from non-ozone-treated flour were examined by studying chemical characteristics using SDSPAGE, free SH groups, differential scanning calorimetry (DSC) parameters, secondary structure, and rheological measurements. Gliadin was extracted from 20 g of a 60 % gluten sample for 30 min, vortexed for 1 min every 10 min, and centrifuged for 10 min at 3000 rpm. Proteins (gluten, glutenin, and gliadin) isolated from non-ozone-treated flour were treated with ozone gas using an ozone generator The protein–buffer mixtures were vortexed for 2 min and allowed to stand at room temperature for 2 h They were centrifuged at 35,714 rpm for 20 min at 4 °C, and the supernatant was heated for 3 min at 90 °C in a boiling water bath. The significance level was defined as p < 0.05
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