Alternating current electric field modifies structure and flavor of peanut proteins.

The impacts of intensity and treating time of alternating current (AC) electric field (EF) on structure and volatile compounds of peanut protein were investigated for low denaturation. The secondary and tertiary structures, polar and weakly polar volatiles were characterized qualitatively and quantitatively using ultraviolet and fluorescence photospectrometry, free sulfhydryl and disulfide groups determination, and combination of gas chromatography and mass spectrometry. The results showed that the ACEF affected significantly proportions of α-helices, β-sheets, β-turns, and random coils as evidenced by Fourier transform infrared spectrometry. Blue shifts of UV and fluorescence spectra, increased surface hydrophobicity and disulfide bonds could be observed after ACEF treatments. The DB-WAX and DB-5MS columns for the polar and weakly polar volatile compound separation revealed that ACEF caused either disappearance or emerging of volatile compounds. The PCA demonstrated that the two principal components contributed about 70 % or more to the flavor and PLS-DA discriminated 18 key compounds.