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Isolation of bovine immunoglobulins and lactoferrin from whey proteins by gel filtration techniques
1Department of Food Science, University of British Columbia, Vancouver, Canada.
Whey is a suitable source of immunoglobulins and lactoferrin to enrich infant formulas. Gel filtration on Sephacryl S-300 and on Fractogel TSK HW-55 was used to isolate immunoglobulins from colostral whey, acid whey, and Cheddar cheese whey. The SDS-PAGE and immunoelectrophoresis techniques indicated that the purity of the fractions from fractionation on Sephacryl S-300 was better than that by fractionation on TSK HW-55 column. Biological activity of fractions from the Sephacryl S-300 column as assessed by immunochemical analysis was 99, 83.3, and 92% for colostral, acid, and sweet wheys. The well-proven antimicrobial agent, lactoferrin, was isolated from sweet whey by heparin-attached Sepharose. Lactoferrin selectively adsorbed to the column was subsequently eluted with 5 mM Veronal-HCl containing .5 M NaCl, pH 7.4. Purity of the isolated protein was confirmed by SDS-PAGE and immunoelectrophoresis.
Whey is a suitable source of immunoglobulins and lactoferrin to enrich infant formulas. Gel filtration on Sephacryl S-300 and on Fractogel TSK HW-55 was used to isolate immunoglobulins from colostral whey, acid whey, and Cheddar cheese whey. The SDS-PAGE and immunoelectrophoresis techniques indicated that the purity of the fractions from fractionation on Sephacryl S-300 was better than that by fractionation on TSK HW-55 column. Biological activity of fractions from the Sephacryl S-300 column as assessed by immunochemical analysis was 99, 83.3, and 92% for colostral, acid, and sweet wheys. The well-proven antimicrobial agent, lactoferrin, was isolated from sweet whey by heparin-attached Sepharose. Lactoferrin selectively adsorbed to the column was subsequently eluted with 5 mM Veronal-HCl containing .5 M NaCl, pH 7.4. Purity of the isolated protein was confirmed by SDS-PAGE and immunoelectrophoresis.