Isolation of lactoperoxidase, lactoferrin, alpha-lactalbumin, beta-lactoglobulin B and beta-lactoglobulin A from bovine rennet whey using ion exchange chromatography

Int J Biochem Cell Biol. Nov-Dec 2000;32(11-12):1143-50. doi: 10.1016/s1357-2725(00)00063-7.


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.

MeSH terms

  • Animals
  • Cattle
  • Chromatography, Ion Exchange
  • Chymosin
  • Electrophoresis, Polyacrylamide Gel
  • Lactalbumin / isolation & purification*
  • Lactoferrin / isolation & purification*
  • Lactoglobulins / isolation & purification*
  • Lactoperoxidase / isolation & purification*
  • Milk / chemistry*


  • Lactoglobulins
  • Lactalbumin
  • rennet
  • Lactoperoxidase
  • Lactoferrin
  • Chymosin