Effect of extrusion on the polymerization of wheat glutenin and changes in the gluten network
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ORIGINAL ARTICLE
Effect of extrusion on the polymerization of wheat glutenin and changes in the gluten network Feng Jia1 • Jinshui Wang1 • Qi Wang1 • Xia Zhang1 • Di Chen1 • Yu Chen1 Changfu Zhang1
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Revised: 22 December 2019 / Accepted: 2 April 2020 Ó The Author(s) 2020
Abstract The changes in the gluten network during extrusion treatment were studied by assessing the polymerization behavior of glutenin. Gluten samples were extruded at different barrel temperatures, screw speeds, and flow rates. The results indicated that high molecular weight glutenin subunits increased while free sulfhydryl groups and low molecular weight glutenin subunits decreased as the screw speeds and flow rates increased during extrusion treatment. Specific b-sheet structures of gluten clearly increased, while a-helices and b-turns fluctuated during extrusion processing, thus forming a tight gluten network. The characteristics of the protein network were evaluated by confocal laser scanning microscopy. The results showed that a homogeneous and denser gluten network was formed at higher extrusion temperatures during the extrusion process, which may be related to the polymerization of lowmolecular-weight glutenin subunits. This study provides a theoretical basis for the improvement and regulation of extrusion quality during the gluten extrusion process. Keywords Glutenin Extrusion Polymerization Gluten network Microstructure
Introduction Gluten may include two major types gliadins and glutenins, which are on the basis of their solubility in aqueous alcohol (Wieser 2007). Gliadins are mainly monomeric, but & Jinshui Wang [email protected] 1
College of Biological Engineering, Henan University of Technology, Zhengzhou 450001, People’s Republic of China
glutenins consist of very large disulfide-linked polymers made up of high molecular weight (HMW) and low molecular weight (LMW) glutenin subunits (Verbauwhede et al. 2019). Glutenins are one of the main major components, which are in charge of imparting strength and elasticity of dough (Yazar et al. 2017), while gliadins confer viscous properties (Bruneel et al. 2010). Although gluten proteins vary from between soft and hard wheat (Jia et al. 2019b), the reactions between gliadin and glutenin have a pivotal role in the formation of wheat gluten network (Li and Gai 2010). Two types of sulfhydryl–disulfide (SH–SS) reactions are crucial during the network formation of gluten. In one, the free-SH groups oxidize into SS bonds (Yue et al. 2019). In the other, there is SH–SS exchange that relates to the reformation or cleavage of SS bonds. The formation of gluten network is vitally important for many wheat-based food products, like Chinese steam bread (Li and Gai 2010), breads (Wang et al. 2017), and pasta noodles (Yue et al. 2019). The cross-linking of the gluten network is predominantly based on disulfide bonds, although non-disulfide bonds also contribute to the gluten network at higher molding temperatures (Sheng and Huang 2002). The polymerization mechanism of wheat gluten depends on
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