SHORT COMMUNICATIONS Preparative-scale fractionation of bovine, caprine and ovine whey proteins by gel permeation chromatography

Abstract

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.