Casein is the main proteinaceous component of milk, where it accounts for ca. 80% of the total protein
inventory. Biologically active peptides can be produced from precursor milk proteins. The most common
way to produce bioactive peptides is through enzymatic hydrolysis of whole proteins.
The objectives of present study were to study the effect of enzymatic hydrolysis on the functional
properties of sodium caseinate. Gastrointestinal enzymes, such as chymotrypsin, have been utilized to
generate hydrolysates. Functional properties were limited to solubility, foaming capacity, and 2,2-diphenyl-
1-picryhydrazyl (DPPH) radical scavenging activity. These properties were evaluated and compared as a
function of hydrolysis degree.