In-situ analysis of the water distribution and protein structure of dough during ultrasonic-assisted freezing based on miniature Raman spectroscopy.

The effect of ultrasonic-assisted freezing (UAF) on the water distribution of dough and molecular structure of gluten was in-situ monitored by low field nuclear magnetic resonance (LF-NMR) and micro-miniature Raman spectroscopy in this research. The results showed that UAF treatment increased the bound water content between 5 min and 30 min, and weakened the signal intensity of hydrogen protons due to the ultrasound enhanced heat and mass transfer during the freezing process. In-situ Raman spectra analysis indicated that UAF delayed the transition from embedded to exposure of tyrosine and tryptophan residues during the freezing process. Meanwhile, UAF reduced the number of hydrogen bonds, gauche-gauche-gauche (g-g-g) conformation breakage, the degree of α-helix to random coil conversion and damage to the gluten network during the freezing process. UAF treatment reduced the water mobility and breakage of non-covalent bonds, which prevented a dramatic shift in the protein advanced conformation during the freezing process, thereby improving the quality of frozen dough.