Fast protein liquid chromatography of camel α-lactalbumin fraction with radical scavenging activity

Abstract

The aim of this study was to investigate the radical-scavenging properties towards a stable radical cation, ABTS, of Camelus dromedarius whey proteins (CWP) separated onto a cation-exchanger by fast protein liquid chromatography. The highest activities were found for CWP and fraction F1 mainly composed of α-lactalbumin. Fractions F2, F3 and F4 contained a mixture of lactoferrin, immunoglobulins G and probably camel whey basic protein (CWBP). These three fractions displayed low radical-scavenging activities. Lactoferrin was eluted almost pure in the last fraction (F5) but did not possess detectable radical-scavenging activity. The present results suggested that the cation-exchange chromatography is of great interest to yield, in a single step, whey protein fractions with various biological activities, i.e. a highly-enriched α-lactalbumin fraction displaying efficient antioxidant activity, a fraction (pool of F2-F4) mainly composed of heavy-chain immunoglobulins potentially interesting for human therapy and a fraction of pure lactoferrin having numerous biological activities such as antimicrobial and immunomodulating properties.