Abstract:

Fourier transform infrared(FTIR) spectroscopy combined with 2D correlation spectroscopy was used to offer some information about the structural stability of ovomucin. Temperature has been chosen as the perturbation to monitor the infrared behavior of ovomucin. The results indicate that the sharp changes in the peak position and the intensity in the infrared spectra of ovomucin occur basically between 55℃ and 65℃. Two-dimensional correlation analysis further showed that the sugar chain in ovomucin is more sensitive to temperature perturbation than the amide area of peptide since it was more likely to change prior to peptide during the heat treatment. The presence of sugar chain in ovomucin molecule was helpful to maintain the stability of protein conformation. The order of secondary structural changes in ovomucin as induced by temperature was α-helix, β-sheet, β-turn and random coil. These results provide preliminary information about the mechanism of ovomucin conformational changes as induced by variable temperature perturbation.

Key words: Ovomucin, Temperature, Fourier transform infrared spectroscopy, 2D Correlation analysis