Isolation of lactoperoxidase and lactoferrin from bovine milk rennet whey and acid whey by sulphopropyl cation exchange chromatography


Yoshida, S.; Y.X.uyun

Netherlands Milk & Dairy Journal 45(4): 273-280

1991


When rennet whey (pH 6.5) was passed through a Sulphopropyl Toyopearl column, lactoperoxidase (33.7 mg/l) and lactoferrin (Lf-a 10.4 mg/l and Lf-b 35.1 mg/l) were adsorbed and eluted from the column by a linear gradient of 0-0.55 M NaCl in 0.05 M phosphate buffer, pH 6.5. When acid whey (pH 4.5) was passed through a Sulphopropyl Toyopearl column, the lactoperoxidase (57.4 mg/l) and lactoferrin (Lf-a 23.1 mg/l and Lf-b 89.7 mg/l) remained on the column. The yields of lactoperoxidase and lactoferrin were higher from acid whey than from rennet whey, although the enzymatic activity of lactoperoxidase in rennet whey (212.9 U/l) was higher than that in acid whey (152.3 U/l).