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. (C) 2015 Elsevier B.V. All rights reserved.