Isolation of lactoperoxidase, lactoferrin, alpha-lactalbumin, beta-lactoglobulin B and beta-lactoglobulin A from bovine rennet whey using ion exchange chromatography.
A mild and rapid method is described for isolating various milk proteins from bovine rennet whey. beta-Lactoglobulin from bovine rennet whey was easily adsorbed on and desorbed from a weak anion exchanger, diethylaminoethyl-Toyopearl. However, alpha-lactalbumin could not be adsorbed onto the resin. alpha-Lactalbumin and beta-lactoglobulin from rennet whey could also be adsorbed and separated using a strong anion exchanger, quaternary aminoethyl-Toyopearl. The rennet whey was passed through a strong cation exchanger, sulphopropyl-Toyopearl, to separate lactoperoxidase and lactoferrin. alpha-Lactalbumin and beta-lactoglobulin were adsorbed onto quaternary aminoethyl-Toyopearl. alpha-Lactalbumin was eluted using a linear (0-0.15 M) concentration gradient of NaCl in 0.05 M Tris-HCl buffer (pH 8.5). Subsequently, beta-lactoglobulin B and beta-lactoglobulin A were eluted from the column with 0.05 M Tris-HCl (pH 6.8), using a linear (0.1-0.25 M) concentration gradient of NaCl. The yields were 1260 mg alpha-lactalbumin, 1290 mg beta-lactoglobulin B and 2280 mg beta-lactoglobulin A from 1 l rennet whey.
Ye
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X
Department of Biochemistry, Faculty of Medicine, The Chinese University of Hong Kong, Hong Kong, People's Republic of China.
Yoshida
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Ng
T B
TB
D000818:Animals; D002417:Cattle; D002852:Chromatography, Ion Exchange; D012085:Chymosin; D004591:Electrophoresis, Polyacrylamide Gel; D007768:Lactalbumin / Q000302:isolation & purification*; D007781:Lactoferrin / Q000302:isolation & purification*; D007782:Lactoglobulins / Q000302:isolation & purification*; D007784:Lactoperoxidase / Q000302:isolation & purification*; D008892:Milk / Q000737:chemistry*
D007782:Lactoglobulins; D007768:Lactalbumin; C025350:rennet; D007784:Lactoperoxidase; D007781:Lactoferrin; D012085:Chymosin