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Catalytic deamidation of canola protein in canola mea

Posted on:1993-02-21Degree:M.A.ScType:Thesis
University:University of Toronto (Canada)Candidate:Igor, Solomon OgheneochukoFull Text:PDF
GTID:2473390014497920Subject:Agricultural chemistry
Abstract/Summary:
Methanol-ammonia/hexane defatted-canola meal has a low protein extractibility of 58% (N x 6.25) at a pH of 12. A process for the partial deamidation of protein in canola meal was developed to increase its extractibility. This process involved the use of sodium dodecyl sulphate (SDS) as a catalyst, at various levels of temperature, pH, and time. A two-level four-factor factorial experimental design was used to initially investigate the protein extractibility. The process thus developed increased the protein extractibility of the two-phase extracted meal from 58.0% to 96.3%.;Optimum conditions, defined as those which give the highest protein yield most economically, were found to be a temperature of 90$spcirc$C, SDS concentration of 0.04 M, pH 2.5, and contact time of 30 minutes. The optimum conditions yielded protein solubility of 87.15% (N x 6.25), 38.58% deamidation and low peptide-bond hydrolysis (7.06%) of the crude protein present in the canola meal.;The functional properties of the protein isolates produced at the optimum condition were better than those of a commercial soy protein isolate (Supro 500E) obtained from Protein Technologies International, St. Louis, MO, U.S.A.
Keywords/Search Tags:Protein, Canola, Deamidation, Meal
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