Milk Protein Hydrolysates and Bioactive Peptides

Abstract

The basic function of milk proteins has long been thought to be that of providing nitrogen and essential amino acids for young mammals (Hambræus, 1992). In addition, intact milk proteins have a range of biological activities, e.g., itnmunoglobulins have an immunoprotective effect, lactoferrin displays antibacterial activity while low concentrations of growth factors and hormones, mainly present in colostrum, appear to play a significant role in post-natal development (Schanbacher et al., 1998). Milk proteins also contain a large range of bioactive peptide sequences which are encrypted within their primary structures (Table 14.1, Meisel, 1998). These include opioid agonist and antagonist peptides, potential hypotensive peptides which inhibit angiotensin-I-converting enzyme (ACE), mineral binding, immunomodulatory, antibacterial and antithrombotic peptides (FitzGerald, 1998; Meisel, 1998; Schanbacher et al., 1998; Takano, 1998; Tomé and Debabbi, 1998; Meisel and Bockelmann, 1999).