Proteolysis and antioxidant activity of peptic, tryptic and chymotryptic hydrolysates of cow, buffalo, goat and camel caseins

Abstract

Caseins of cow, buffalo, goat and camel milks were hydrolysed using pepsin, trypsin and chymotrypsin. The rate and degree of casein hydrolysis and the antioxidant activity (AA) of the casein hydrolysates (CH) were followed. Camel casein showed the highest rate and degree of hydrolysis with pepsin and trypsin, while cow casein was more rapidly hydrolysed with chymotrypsin than other caseins studied. The AA of all CH increased to a maximum after 24 h of hydrolysis. The AA of tryptic hydrolysates was higher (P < 0.002) than that of peptic hydrolysates. Camel CH exhibited higher AA than hydrolysates of other caseins.