Title of article
Physicochemical characterization of the structural stability of some plant globulins
Author/Authors
Gorinstein، نويسنده , , S. and Zemser، نويسنده , , M. and Friedman، نويسنده , , M. and Rodrigues، نويسنده , , W.A. and Martins، نويسنده , , P.S. and Vello، نويسنده , , N.A. and Tosello، نويسنده , , G.A. and Paredes-Lَpez، نويسنده , , O.، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 1996
Pages
8
From page
131
To page
138
Abstract
The fluorescence properties of amaranth, soybean, rice, sorghum and maize globulins, and cassava globulin-like proteins were measured as a function of fluorescent light intensity, peak response and shift in the maximum of emission using the fluorescence of tryptophan at 295 nm. Application of differential scanning calorimetry (DSC) of these globulins gave a quantitative estimation of their thermal stabilities in solid state. The thermodynamic data associated with transition and the number of ruptured hydrogen bonds were calculated. Differences in secondary structure and α-helical content were observed. Relative structural stabilities of native plant globulins were also estimated by X-ray diffractometry and Fourier transform infrared (FT-IR) measurements.
Journal title
Food Chemistry
Serial Year
1996
Journal title
Food Chemistry
Record number
1946922
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