Abstract
The total proteins and helianthinin (11S) from sunflower seeds were chemically modified by acetylation and succinylation. The extent of acetylation of the total proteins and helianthinin were 12%, 51%, 52%, 56% and 12%, 36%, 69%, 71%, respectively, while the extent of succinylation were 8%, 21%, 33%, 49% and 10%, 30%, 44%, 61%, respectively. The extent of modification was monitored by the availability of free lysyl residues in the proteins. The ultraviolet absorption maximum shifted to higher wavelengths in total proteins and in helianthinin; there was also an increase in absorbance in the 260 nm wavelength, as a function of increased chemical modification. The sedimentation velocity profile indicated the dissociation of the proteins to low molecular weight fraction (2S) through a 7S component. The dissociation occurred at low modification levels in both total proteins and in helianthinin. There was a gradual red shift and quenching in the fluorescence emission maximum at higher modification levels indicating the denaturation of the proteins as a result of this chemical modification. The change in absorbance as a function of temperature indicates minor changes suggesting that the conformation of the proteins is already altered to significant extents due to the chemical modification.