Abstract
The effect of a high electric field on secondary structure conformation of fully hydrated (45.65% wet basis) gluten protein was studied by Fourier transform infrared spectroscopy. Three experimental conditions were evaluated including electric field intensity of 0 kV (no treatment), 3.5 kV, and 7kV and treatment time of 30, 60, and 90 min. Fourier transform infrared spectra of treated and non-treated hydrated gluten protein revealed that high electric field treatment resulted in irreversible changes in the secondary structures. For the 30 min treatment no variation was observed for electric field intensities 0 and 7 kV; but at 3.5 kV it showed slight reorganization and structural conversion of secondary structures. No variation in spectral pattern was observed for all the high electric field treatments for 60 min but major secondary structure reorganization took place for high electric field treatment at 90 min. Curve-fitting using Gaussian band shapes and principal component analysis further supported the results.
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