Different routes were screened for the preparation of superparamagnetic cation-exchange adsorbents for the capture of proteins using high-gradient magnetic fishing. Starting from a polyglutaraldehyde-coated base particle, the most successful of these involved attachment of sulphite to oligomers of epichlorohydrin formed on the particle surface. The resultant cation-exchanger had a maximum lysozyme binding capacity of 272 mg g(-1) and a dissociation constant of 0.73 muM. Using lysozyme as a model protein in small-scale studies, appropriate conditions were then selected for the capture of lactoperoxidase from sweet bovine whey. Subsequently, a high-gradient magnetic fishing process was constructed for the fractionation of whey, in which lactoperoxidase was purified 36-fold and concentrated 4.7-fold.