Effects of different freezing temperatures on the molecular structure of gluten proteins.

In this paper, the effects of different freezing temperatures on the molecular structure of the gluten protein were investigated. Nonfermented dough was rapidly frozen at − 40 °C for 45 min and then stored at − 6 °C, − 12 °C, − 18 °C, − 24 °C and − 30 °C. The molecular structure changes of gluten were analyzed at 10, 20 and 30 days of storage. The results showed that the content of disulfide bonds in gluten protein was higher at a freezing temperature of − 12 °C, indicating that the content of the free sulfhydryl content decreased. The highest surface hydrophobicity of the gluten protein was found at the lowest freezing temperature (− 30 °C) and the highest freezing temperature (− 6 °C) with the same amount of frozen storage time, indicating that the gluten protein network was damaged at these temperatures. The content of wet gluten in the dough was not affected by different freezing temperatures. In short, the molecular structure of the gluten protein varies greatly under different freezing temperatures. Higher or lower freezing temperatures may lead to the deterioration of gluten molecular structure due to the influence of water migration during freezing storage. The correlation analysis between the change in gluten protein structure and the quality of dough and flour products under different freezing temperatures still requires further study. [ABSTRACT FROM AUTHOR]