Characterization of soluble amaranth and soybean proteins based on fluorescence, hydrophobicity, electrophoresis, amino Acid analysis, circular dichroism, and differential scanning calorimetry measurements.

Intrinsic fluorescence (IF), surface hydrophobicity (S(o)), electrophoresis, amino acid analysis, circular dichroism (CD), and differential scanning calorimetry (DSC) were used to study folded and unfolded soluble proteins from Amaranthus hypochondriacus (A. h.) and soybean (S). Globulin (Glo) and albumin subfractions (Alb-1 and Alb-2) were extracted from A. h. and S and denatured with urea. Electrophoretic and functional properties indicated a significant correlation between soluble protein fractions from soybean and amaranth. The protein fractions shared some common electrophoretic bands as well as a similar amino acid composition. The larger percent of denaturation in protein fractions, which is associated with enthalpy and the number of ruptured hydrogen bonds, corresponds to disappearance of alpha-helix. The obtained results provided evidence of differences in their secondary and tertiary structures. The most stable was Glo followed by the Alb-2 fraction. Predicted functional changes in model protein systems such as pseudocereals and legumes in response to processing conditions may be encountered in pharmaceutical and food industries. These plants can be a substitute for some cereals.