The whey proteins of the cow, goat and sheep have previously been fractionated on an analytical scale by reversed-phase HPLC (De Frutos et al. 1992), anion-exchange FPLC (Andrews et al. 1985; Manji et al. 1985; Laezza et al. 1991) and gel permeation FPLC (Andrews et al. 1985; Hill & Kakuda, 1990). Anion-exchange and gel permeation FPLC can readily be scaled up for laboratory preparation of whey protein fractions. There is some indication, however, that anion-exchange FPLC does not give complete separation of β-lactoglobulin and α-lactalbumin from the other minor whey protein fractions (Girardet et al. 1989).

In previous work it has been shown that gel permeation FPLC gives a satisfactory fractionation of the whey proteins of the cow (Law et al. 1993), goat (Law & Brown, 1994) and sheep (Law, 1995). In this paper we describe a scaled-up method of gel permeation that can be used for fairly rapid preparation or purification of four main whey protein fractions from the milks of these species.