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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
