Abstract
Application of differential scanning calorimetry (DSC) and the susceptibility of amaranth globulins (A-G) to α-chymotrypsin gave a quantitative estimation of protein denaturation in solid state. To compare effects of size and crystal structure, A-G, quinoa globulins (Q-G), and bovine γ-globulins (γ-G) were examined at similar conditions for the extent of denaturation. A-G and Q-G showed similar data, but γ-G exhibited maximal conformational changes. The larger percentage of denaturation in globulins that is associated with enthalpy and the number of ruptured hydrogen bonds correspond to the smaller crystallinity determined by X-ray diffraction and disappearance of the α-helix in Fourier transform-infrared spectra.
Original language | English |
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Pages (from-to) | 100-105 |
Number of pages | 6 |
Journal | Journal of Agricultural and Food Chemistry |
Volume | 44 |
Issue number | 1 |
DOIs | |
State | Published - Jan 1996 |
Keywords
- Amaranth
- Calorimetry
- Denaturation
- Quinoa
- Spectroscopy