Effects of acetylation and succinylation on the functional properties of the canola 12S globulin

The canola 12S globulin was isolated by the protein micellar mass procedure (PMM) and modified by acetylation and succinylation in order to obtain a canola protein concentrate with improved functional properties. The solubility profile differed from that of the PMM in that protein solubility below the isoelectric point was impaired, but solubility at neutral to alkaline pH values was greatly enhanced. In comparison with the PMM foaming capacity and emulsifying activity were significantly increased by acylation. Foam stability decreased significantly upon acylation. Emulsion stability significantly increased initially, then decreased at the highest levels of modification. Following acylation, the fat absorption capacity was significantly elevated. In addition, gelation properties of canola proteins were mainly improved by acylation. Furthermore, the acylated concentrates were significantly lighter in colour than the original PMM. Overall, the acylated concentrates possessed improved functionality as compared to the PMM, making them more suitable as a food ingredient.