Functional properties of sodium caseinate hydrolysates as affected by the extent of chymotrypsinolysis

Daniela Pralea, Loredana Dumitrascu, Daniela Borda, Nicoleta Stănciuc

Volume 17, Issue 3;
Pages: 308-314;
ISSN: 2069-0053 (print) (former: ISSN:1453-1399), Agroprint;
ISSN (online):2068 – 9551
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.
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