Protein structural properties and proteomic analysis of rice during storage at different temperatures

• Published in: Food chemistry Vol. 361; p. 130028
• Main Authors: Zhao, Qingyu, Lin, Jiahui, wang, Chao, Yousaf, Laraib, Xue, Yong, Shen, Qun
• Format: Journal Article
• Language: English
• Published: Elsevier Ltd 01.11.2021
• Subjects: Data-independent acquisition; Proteomic; Rice; Storage proteins; Structural properties; Storage proteins; Structural properties; Data-independent acquisition; Proteomic; Rice
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/j.foodchem.2021.130028

•Storage promoted rice protein oxidation and surface hydrophobicity.•Storage altered the secondary structure of rice protein.•The aggregation of rice proteins was induced by high temperature.•157 and 395 differential proteins were found at 30 ℃ and 70 ℃, respectively.•Mechanisms of temperature effects on storage quality of rice were explored. Rice quality changes during storage, but there have been few studies of how rice proteins changes during aging. The present study characterized the structural properties of protein in stored rice and identified the mechanism of quality deterioration using proteomics. Compared with protein from newly harvested rice, the free sulfhydryl content of protein from stored rice was significantly reduced and the disulfide bond content and surface hydrophobicity was higher. Storage resulted in a loss of α-helix and β-sheet structures and increase in β-turn and random coil structures. High-molecular-weight protein subunits decomposed to produce low-molecular-weight subunits at 30 °C, while protein aggregation occurred at 70 °C. At 30 ℃ 157 differential proteins were found and 70 ℃ 395 such proteins occurred. Redox homeostasis, response to oxidative stress, glutathione metabolism, tricarboxylic acid cycle, glycolysis/gluconeogenesis, starch and sucrose metabolism, and fatty acid biosynthesis and degradation led to the different quality of stored rice.