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

@article{Gorinstein2001CharacterizationOS,
  title={Characterization of soluble amaranth and soybean proteins based on fluorescence, hydrophobicity, electrophoresis, amino Acid analysis, circular dichroism, and differential scanning calorimetry measurements.},
  author={Shela Gorinstein and Efren Delgado-Licon and Elke Pawelzik and Herry Heriyati Permady and Moshe Weisz and Simon Trakhtenberg},
  journal={Journal of agricultural and food chemistry},
  year={2001},
  volume={49 11},
  pages={5595-601}
}
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… CONTINUE READING
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