Effect of Adding Acid-soluble Wheat Protein to Dough on the Quality Stabilization of Wheat Flour and Rice Flour Blend Bread

Abstract

The effect adding acid-soluble wheat protein (ASP), mainly composed of gliadin, to wheat flour and rice flour blend bread in mechanized bread-making was investigated using the following method. Rice flour was used to replace 40 % of the wheat flour, and wheat protein (gluten and ASP) was added to constitute 10 % of the total mixture, thus replacing 20 % to 40 % of the gluten with ASP. In the sponge and dough method, the addition of ASP improved the gas holding capacity of the sponge, and the dough development time shortened during the mixing process. In addition, molding conditions for mass production were improved due the suppression of changes in dough rheological properties caused by the time lag during the dividing process. Microstructural observation of sheeted dough showed that the gluten network of the dough extended in a uniform direction. Consequently, it was shown that the addition of ASP resulted in increased extensibility of the dough. As a result, the addition of ASP improved uneven crumb structure after baking and decreased the rate of crumb firmness during storage (20 ℃, 24-96 hours). In conclusion, the addition of ASP improved the stabilization of the bread-making process and increased the product quality of wheat flour and rice flour blend bread in mechanized bread-making.

Effects of japonica rice flour on the mesoscopic and microscopic properties of wheat dough protein

“…Protein content in wheat (8–15%) is relatively high compared to other major cereals (Li et al ., 2016). The structure and ratio of gliadin and glutenin in wheat flour give the dough high viscoelasticity, due to the non‐covalently bound gluten network, which plays an important role in determining the rheological properties and quality of dough (Arai et al ., 2018). Dough toughness is considered to be determined by protein–protein interactions within the gluten network, including sulfhydryl and disulphide bonds (Hu et al ., 2017).…”