Application of new methodology to canola protein isolation

Abstract

New methodology has been developed to isolate protein fractions from canola meal with almost complete elimination of the antinutritional factors. Modifications of a unique protein micellar mass (PMM) procedure developed initially for pulse storage proteins has resulted in extracts of approximately 83% protein. One of the modifications has involved the choice of an extraction buffer; selected through a screening process whereby the efficiencies of the buffers in removing antinutritional factors and preserving protein nativity have been graphically plotted and ranked, hence allowing the most efficient buffer to be chosen and used in the PMM process. Average extract phytic acid and gLucosinolate levels have been reduced to 24 and 7% of the original meal, respectively. In addition, the average phenolic compounds reduction in the extract has been found to be approximately 15% of the raw meal. Enthalpy of denaturation values ( H) as high as 9.67 J/g witn thermal denaturation (Td) temperatures of approximately 88-89*C reflect the mildness of the PMM approach. Analysis of the protein structure using SDS-PAGE and HPLC/gel filtration revealed four constituent polypeptide chains of the 12S storage globulin. Commercialization of this process may impact the economics of canola production; the value of the protein component would increase if it were suitable for human consumption.