Impact of Meal Preparation Method and Extraction Procedure on Canola Protein Yield and Properties

Abstract

Screw-pressed and cold-milled, solvent-defatted canola meal was processed with a conventional Osborne sequence extraction method to obtain albumin, globulin, prolamin, and glutelin protein fractions. This extraction sequence was altered by isolating globulins prior to albumins, resulting in an increased globulin yield. The difference can be attributed to the presence of salts in canola meal flour, which increase globulin extraction during albumin isolation in the conventional method. An increase in the cumulative protein yield was observed when cold-milled canola meal flour was used instead of screw-pressed flour. Significant differences were also observed in the functional properties (water absorption, fat absorption, and emulsifying activity) of canola protein fractions with respect to both meal preparation method and protein isolation method. Results suggested that milling temperature and isolation method can have significant impacts on protein quality and yield.