Effects of acetylation and succinylation on the physicochemical properties of the canola 12S globulin. Part I

Chemical modification is a means of improving the functional properties of food proteins, which are directly related to the physicochemical characteristics. The objective of this study was to determine the effects of acetylation and succinylation on the physicochemical properties of canola proteins. Increasing acylation resulted in dissociation of the protein structure, as was evidenced by a decrease in molecular weight and enthalpy of denaturation. Acylation caused an overall decrease in isoelectric point, this effect being more pronounced with succinylation as compared to acetylation. Aromatic and aliphatic hydrophobicity increased significantly following acetylation. Aromatic hydrophobicity significantly decreased while aliphatic hydrophobicity showed an overall significant increase following succinylation. The amino acid profile remained unchanged with the exception of a slight decrease in lysine in the succinylated and acetylated proteins, and a decrease in proline in the succinylated proteins. These results indicate that acylation has a significant impact on the physicochemical properties, particularly molecular weight and net charge, of the canola 12S globulin. © 1997 Published by Elsevier Science Ltd