The effect of progressive succinylation upon the conformation of faba bean legumin has been studied using chemical analysis, viscometry, analytical ultracentrifugation, UV and fluorescence spectroscopy, and differential scanning calorimetry (DSC). The protein dissociates gradually into 3 S subunits forming a 7 S intermediate. DSC measurements revealed a continuous loosening of the spacial structure with increasing degree of succinylation. Viscometric and spectroscopic studies indicate the presence of a particular conformational state at 60−80% succinylation, whereas a largely expanded structure was shown to exist in exhaustively succinylated legumin due to a cumulative effect of N- and O-succinylation. Keywords: Legumin; faba bean protein; succinylation; conformational changes

The effect of progressive acetylation upon the conformation of the 11S globulin legumin from faba bean has been studied using chemical analysis, UV, fluorescence and CD spectroscopy, viscometry and analytical ultracentrifugation. The modification did not induce complete dissociation of the oligomeric protein. Only 30% of the protein was found to be a dissociated 3S subunit after excessive acetylation, whereas 70% was a dimeric legumin aggregate with a molecular mass of about 700 kDa. The aggregation of the highly modified legumin in high‐ionic‐strength buffer solution leads to soluble higher legumin oligomers. The acetylation resulted in a moderate molecular expansion of legumin due to a changed tertiary structure, whereas the far‐UV circular dichroism spectra did not provide definitive evidence of a decrease in domain‐stabilizing β‐sheet conformations in their secondary structure. © 2000 Society of Chemical Industry

No abstract

No abstract