Isolation and Purification of Bioactive Proteins from Bovine Colostrum

Bovine colostrum is the milk secreted by cows during the first few days after parturition. It contains many essential nutrients and bioactive components, including growth factors, immunoglobulins (Igs), lactoperoxidase (Lp), lysozyme (Lys), lactoferrin (Lf), cytokines, nucleosides, vitamins, peptides and oligosaccharides, which are of increasing relevance to human health. Much research work has been done on the structure and function of bovine colostrum proteins. IgG was widely utilised in the immunological supplementation of foods, specifically in infant formulate, and yielded sales of approximately US$100 million in 2007 (Gapper, et al., 2007). In the highly competitive and valuable international market for IgG-containing products, some of the products are usually priced based on IgG content. Another important protein from bovine colostrum is lactoferrin. Its diverse range of biological activities such as anti-infective activities toward a broad spectrum of species, antioxidant activities and promotion of iron transfer are expanding the demand in the market. It also exhibits the potential for chemoprevention of colon and other cancers as a natural gradient. Apart from the two kinds of bovine colostrum proteins, ┙-lactalbumin has been claimed as an important food additive in infant formula due to its high content in tryptophan and as a protective against ethanol and stress-induced gastric mucosal injury. ┚Lactoglobulin is commonly used to stabilize food emulsions for its surface-active properties. Bovine serum albumin (BSA) has gelation properties and it is of interest in a number of food and therapeutic applications (Almecija, et al., 2007). Therefore, fractionation for the recovery and isolation of these proteins has a great scientific and commercial interest. As a result of this growth in the commercial use of bovine colostrum proteins, there is great interest in establishing more efficient, robust and low cost processes to purify them. Although great deals of studies have been done for the separation and purification of colostrum proteins due to their wide application in food industry, medicine and as supplements, large scale production system for the downstream processing of recombinant antibodies still represents the major issue. Lu (Lu, et al., 2007) designed a two-step ultrafiltration process followed by a fast flow strong cation exchange chromatography to isolate LF from bovine colostrum in a production scale. A stepwise procedure for purification of the crude LF was conducted using a preparative-scale strong cation exchange