Structural Changes of Legumin from Faba Beans (Vicia faba L.) by Succinylation

• Published in: Journal of agricultural and food chemistry Vol. 46; no. 6; pp. 2080 - 2086
• Main Authors: Schwenke, Klaus Dieter, Knopfe, Constanze, Mikheeva, Larissa M, Grinberg, Valerij Y
• Format: Journal Article
• Language: English
• Published: American Chemical Society 01.06.1998
• Subjects: ANALYTICAL METHODS; CHEMICAL COMPOSITION; CHEMICAL REACTIONS; CHEMICAL STRUCTURE; COMPOSICION QUIMICA; COMPOSITION CHIMIQUE; ESTABILIDAD; ESTRUCTURA QUIMICA; FABA BEANS; FEVE; GLOBULINAS; GLOBULINE; GLOBULINS; HABA; HIDROFOBICIDAD; HYDROPHOBICITE; HYDROPHOBICITY; MOLECULAR CONFORMATION; REACCIONES QUIMICAS; REACTION CHIMIQUE; STABILITE; STABILITY; STRUCTURE CHIMIQUE; SUCCINIC ANHYDRIDE; TECHNIQUE ANALYTIQUE; TECNICAS ANALITICAS; VISCOSIDAD; VISCOSITE; VISCOSITY
• ISSN: 0021-8561; 1520-5118
• DOI: 10.1021/jf970984k

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