Effect of succinylation on the oligomeric structure of glycinin.
By varying the ratio of succinic anhydride to the protein, glycinin, one of the major fractions of soybean proteins, is succinylated to various levels. Sedimentation velocity experiments indicate the dissociation of the protein due to succinylation. Viscosity increases and a blue shift occurs in the absorption spectrum. The rate of proteolysis increases. Both dissociation and denaturation of the protein appear to occur. The effect of syccinylation on glycinin and arachin, the major protein of groundnuts, appears to be different.
D010940:Plant Proteins / Q000378:metabolism*; D011487:Protein Conformation; D013025:Glycine max; D013057:Spectrum Analysis; D013386:Succinates / Q000494:pharmacology*; D013387:Succinic Anhydrides / Q000494:pharmacology*; D014783:Viscosity
D010940:Plant Proteins; D013386:Succinates; D013387:Succinic Anhydrides