REVIEW: ISOLATION AND PURIFICATION OF MILK WHEY GLYCOMACROPEPTIDE

Abstract

The objective of this work was to review the isolation and purification methods of glycomacropeptide (gmp). This peptide is formed during enzymatic coagulation of milk, using chymosin. Aspects such as structure, composition, biological activities and functional and technological properties of gmp are also covered. It was concluded that the various methods mentioned in this paper for gmp isolation and purification use isolated or combined processes, which can be classified in three categories: selective precipitation induced by adjustment of the physical properties of the solution; membrane filtration based mainly on different membrane sizes and load, and selective adsorption. Regarding the biological activities of gmp, this peptide can be understood as a promising compound, although additional research is necessary in order to define quantities, efficacy and to allow functionality claims. There is, however, little information regarding gmp’s addition in food, interaction with other components and chemical stability under different processing conditions.