| Abstract
| - Intrinsic fluorescence (IF), surface hydrophobicity (So), electrophoresis, amino acid analysis, circulardichroism (CD), and differential scanning calorimetry (DSC) were used to study folded and unfoldedsoluble proteins from Amaranthushypochondriacus (A. h.) and soybean (S). Globulin (Glo) andalbumin 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 proteinfractions from soybean and amaranth. The protein fractions shared some common electrophoreticbands as well as a similar amino acid composition. The larger percent of denaturation in proteinfractions, which is associated with enthalpy and the number of ruptured hydrogen bonds, correspondsto disappearance of α-helix. The obtained results provided evidence of differences in their secondaryand tertiary structures. The most stable was Glo followed by the Alb-2 fraction. Predicted functionalchanges in model protein systems such as pseudocereals and legumes in response to processingconditions may be encountered in pharmaceutical and food industries. These plants can be asubstitute for some cereals. Keywords: Amaranth; soybean; amino acids; proteins; electrophoresis; amino acids; fluorescence;calorimetry; denaturation; spectroscopy
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