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Updated: Jun 7, 2025

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
Published on: September 12, 2019
Protein aggregation behavior during highland barley dough formation induced by different hordein/glutelin ratio
Xinyue Liu1, Hao Duan2, Gaigai Liu2
1Beijing Key Laboratory of Bioactive Substances and Functional Foods, Beijing Union University, Beijing, 100023, PR China; Engineering Research Center of Grain and Oil Functionalized Processing in University of Shaanxi Province, College of Food Science and Engineering, Northwest A&F University, 22 Xinong Road, Yangling 712100, Shaanxi, PR China.
Abstract:
To investigate why highland barley dough cannot form a gluten structure, the mechanism by which the ratio of hordein/glutelin affects protein aggregation behavior during the formation of barley dough was investigated. It was observed that the pasting properties of the reconstituted flour were markedly diminished (1154-1303 × 10-3 Pa•s). The 50Hordein-50Glutelin sample exhibited the highest farinograph quality number. The K, A22 (48.82-65.26 %), hardness, free -SH (0.76 %-0.95 %), random coil, and hydrogen bonding (0.091-0.179 g/100 g) exhibited a notable increase with a reduction in the hordein/glutelin ratio. Conversely, β-sheet (27.39 %-40.11 %) and fluorescence intensity declined pronouncedly. The 50H-50G facilitated the reinforcement of protein crosslinking and polymerization, enhanced the continuity and order of the protein network structure, and further augmented the dough's viscoelasticity. The results would regulate the macroscopic quality of barley and other miscellaneous grain products through endogenous components, establishing a foundation for enhancing their quality.
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