Physicochemical characterization of the structural stability of some plant globulins

• Published in: Food chemistry Vol. 56; no. 2; pp. 131 - 138
• Main Authors: Gorinstein, S., Zemser, M., Friedman, M., Rodrigues, W.A., Martins, P.S., Vello, N.A., Tosello, G.A., Paredes-López, O.
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 01.06.1996; Elsevier
• Subjects: Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts; Biological and medical sciences; Food industries; Fundamental and applied biological sciences. Psychology; Storage protein; Spectral properties; Corn; Soybean; Globulin; Thermal stability; Amaranth; Aminoacid; Plant protein; Chemical composition; Sorghum (food); Thermodynamic properties; Physicochemical properties; Rice
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/0308-8146(95)00144-1

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.