Effect of grape seed power on the structural and physicochemical properties of wheat gluten in noodle preparation system. (1st September 2021)

• Record Type: Journal Article
• Authors: Chen, Sheng-Xiong; Ni, Zhi-Jing; Thakur, Kiran; Wang, Shaoyun; Zhang, Jian-Guo; Shang, Ya-Fang; Wei, Zhao-Jun
• Is Part Of: Food chemistry. Volume 355(2021)
• Publication Date: 2021-09-01
• Subjects: GSP Grape seed powder -- WA Water absorption -- ST Stability time -- DDT Dough development time -- SD Softening degree -- ANS The 8-anilino-1-naphthalenesulfonic acid -- SEM Scanning electron microscope -- AFM Atomic force microscopy; Wheat gluten, PubChem SID: 135, 322, 122; Grape seed power -- Wheat -- Gluten -- Physicochemical properties -- Molecular interaction -- Structure; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2021.129500
• Languages: English
• ISSNs: 0308-8146

Abstract

Graphic abstract: Highlights: Wheat flour was prepared with 1%, 3%, and 5% grape seed power (GSP). 1% GSP promoted the aggregation of gluten proteins, thus enhanced the noodle quality. 3% and 5% GSP addition disrupted the disulfide bonds between gluten protein molecules. We emphasized the interaction between wheat proteins and GSP in noodle making dough. Abstract: Noodles were prepared using wheat flour supplemented with 1%, 3%, and 5% grape seed power (GSP). The farinograph properties of wheat flour, the textural properties of the dough, and thermal properties of the gluten were determined. The microstructure was analyzed by scanning electron and atomic force microscopy, and the effects of the addition of GSP on the physicochemical and structural properties (free sulfhydryl content, surface hydrophobic region, and secondary structure) of wheat gluten protein were analyzed. 1% GSP promoted the aggregation of gluten proteins by promoting hydrophobic interactions and hydrogen bonding, thus enhanced the noodle quality. Whereas, 3% and 5% GSP addition disrupted the disulfide bonds between gluten protein molecules and formed macromolecular aggregates linked to gluten proteins through non-covalent bonds and hydrophobic interactions, which prevented the formation of the gluten protein reticulation structure. Our study emphasized the interaction between wheat proteins and GSP in noodle making dough.