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Effect of Thermal and High Electric Fields on Secondary Structure of Peanut Protein

This study evaluated the effect of the thermal and high electric field stresses on the secondary structure conformation of peanut protein using Fourier transform infrared spectroscopy. The amide I region between the wavelengths 1700–1600 cm–1 of the spectra were studied for different thermal and high electric field treatments. Within thermal treatments, both hot air roasting and microwave processing treatments were evaluated. Hot air treatments were performed at temperatures of 50, 75, and 100°C from 15, 30, and 45 min while the microwave treatments were conducted at the same temperatures, but for 5, 10, 15, and 20 min. Three experimental conditions were evaluated for the electric field intensity of 10, 15, and 20 kV for 60, 120, and 180 min. Changes were observed at 1654–1650 cm–1, indicating conformational changes in the α-helix secondary structure. Similar changes were observed at various other wavelengths indicating changes in the 3/10 helix, β-sheets and random coils present in the protein. With an increase in the treatment time, the secondary structure reorganizations increased with the creation of new random coils and aggregated strands. Curve-fitting using Gaussian band shapes further supported the observations. In vitro protein digestibility studies were also performed and the protein changes also supported the observations from the spectra.