Characteristics of enzymatic hydrolysis of thermal-treated wheat gluten

Functional, conformational and topographical changes of succinic acid deamidated wheat gluten upon freeze- and spray-drying: A comparative study

“…All samples (1.0 mg/mL) were extracted with a 0.05 mol/L sodium phosphate buffer (pH 4.4) and loaded (10 mL) on the column. The elution solvent was (1:1, v/v) acetonitrile (ACN)/water containing 0.5 mL/L trifluoroacetic acid, with the flow rate of 0.8 mL/min at 25.0 C according to the method described by (Wang, Wei, Li, Bian, & Zhao, 2009). The elution profiles were divided into two fractions using the lowest absorbance reading between the two peaks as the cut-off point.…”

Investigation of the susceptibility of acid‐deamidated wheat gluten to in vitro enzymatic hydrolysis using Raman spectra and free amino acid analysis

“…The enzymatic hydrolysis of proteins is affected by many factors including enzyme specificity and the extent of protein denaturation 7–10. Substrate structure also affects enzymatic hydrolysis; for example, the available binding surface of substrate to enzyme will influence hydrolysis rate 11, 12.…”

Extractability and Molecular Modifications of Gliadin and Glutenin Proteins Withdrawn from Different Stages of a Commercial Ethanol Fuel/Distillers Dried Grains with Solubles Process Using a Wheat Feedstock

“…The material is further concentrated into thin stillage or syrup, and then it is dried in a drum dryer at 145°C to yield the final DDGS product. Although the effects of temperature on the extractability and structure of gluten proteins have been studied (Schofield et al 1983;Wang et al 2009), little information is available on the effects of ethanol/DDGS processing on the extractability and structure of proteins throughout a commercial facility.…”