PHYSICOCHEMICAL CHARACTERIZATION OF THE STRUCTURAL STABILITY OF SOME PLANT GLOBULINS

The fluorescence properties of amaranth, soybean, rice, sorghum and ma ize globulins, and cassava globulin-like proteins were measured as a f unction of fluorescent light intensity, peak response and shift in the maximum of emission using the fluorescence of tryptophan at 295 nm. A pplication of differential scanning calorimetry (DSC) of these globuli ns gave a quantitative estimation of their thermal stabilities in soli d state. The thermodynamic data associated with transition and the num ber of ruptured hydrogen bonds were calculated. Differences in seconda ry structure and cu-helical content were observed. Relative structural stabilities of native plant globulins were also estimated by X-ray di ffractometry and Fourier transform infrared (FT-IR) measurements. Copy right (C) 1996 Elsevier Science Ltd