Biological, functional and nutritional properties of caseinomacropeptide from sweet whey

Abstract

Bioactive peptides derived from bovine milk proteins have gained much attention due to their health promoting functions. All over the world, cheese industry generates high volumes of sweet whey that could be used as an alternative source of bioactive peptide in nutraceuticals and food industry. Caseinomacropeptide (CMP) is a bioactive peptide derived from ��-casein by the action of chymosin during cheese manufacturing. CMP consist of two forms which are glycosylated (gCMP) and non-glycosylated (aCMP). The predominant carbohydrate in gCMP is N-acetylneuraminic (sialic acid) which gives functional and biological properties to gCMP. Due to its unique composition and technological characteristics such as wide pH range solubility, emulsifying, gelling, and foaming ability, CMP has received special attention. Therefore, there is an increased interest in researches for isolation and concentration of CMP. However, the isolation and purification methods are not cost-effective. It would be easier to optimize the conditions for isolation, purification, and utilization of CMP in nutraceuticals and food industry through deeper understanding of the effective factors. In this review, the structure of CMP, biological activities, isolation, and purification methods, the factors affecting functional properties and application areas of CMP in food industry are discussed.