Separation of lactoperoxidase from bovine whey milk by cation exchange composite cryogel embedded macroporous cellulose beads

• A novel cation exchange composite cryogel embedded with cellulose beads was prepared.
• High purity lactoperoxidase (>98.0%) was obtained from bovine whey by the cryogel.
• The maximum recovery of 92% was observed by stepwise elution at pH 5.8.

Lactoperoxidase is one of important proteins in bovine whey and it has been known to play a key role in protection of the lactating mammary gland and the intestinal tract of newborn infants against pathogenic microorganisms. However, in industrial process the separation of this protein with a high purity is a challenging work due to the low content in whey. In this work, a cation exchange composite cryogel embedded with cellulose beads was prepared and employed to separate lactoperoxidase from bovine whey. High purity of lactoperoxidase (98.0–99.8%) was obtained with a stepwise elution using 0.075 M NaCl follow by 0.15 M and 1 M NaCl in 10 mM phosphate buffer and the maximum recovery of about 92% was obtained at pH 5.8, indicating that the present cation exchange composite cryogel could be potential and interesting in the separation of minor proteins like lactoperoxidase from bovine whey.