Physicochemical and Functional Properties of Rapeseed Protein Isolate: Influence of Antinutrient Removal with Acidified Organic Solvents from Rapeseed Meal

The presence of antinutritional constituents in rapeseed protein products (RPI), such as polyphenols, phytates, allyl isothiocyanates, and glucosinolates, is a formidable constraint. The effect of antinutrient removal from rapeseed meal with an organic solvent mixture (methanol/acetone, 1:1 v/v, combined with an acid (hydrochloric, acetic, perchloric, trichloroacetic, phosphoric)) on the physicochemical and functional properties of RPI was investigated. The extraction resulted in a substantial reduction of antinutrients from RPI, especially polyphenols and phytates, with concomitant decreases in protein yield and solubility. Treatment harbored significant improvement in the degree of whiteness, which was highest in the perchloric acid case. Surface hydrophobicity and free sulfhydryl group of RPI changed considerably, with perchloric acid-treated samples showing higher values, whereas the disulfide content remarkably increased in trichloroacetic acid- and phosphoric acid-treated samples, signifying aggregation. Intrinsic emission fluorescence and FTIR spectra showed significant changes in proteins' tertiary and secondary conformations, and the changes were more pronounced in samples treated with higher concentrations of acids. No appreciable alteration appeared among the electrophoretic profiles of proteins from pristine meal and those treated with lower levels of acids. Interfacial surface properties of proteins were variably improved by the solvent extraction, whereas the converse was true for their extent of denaturation. The results suggest that the physicochemical and conformational properties of RPI are closely related to its functional properties.