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Proteolysis and antioxidant activity of peptic, tryptic and chymotryptic hydrolysates of cow, buffalo, goat and camel caseins
Author(s) -
Assem Fayza M,
Abd ElGawad Mona A M,
Kassem Jihan M,
Abd ElSalam Mohamed H
Publication year - 2018
Publication title -
international journal of dairy technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.061
H-Index - 53
eISSN - 1471-0307
pISSN - 1364-727X
DOI - 10.1111/1471-0307.12400
Subject(s) - pepsin , casein , trypsin , hydrolysate , hydrolysis , chymotrypsin , chemistry , proteolysis , camel milk , food science , biochemistry , chromatography , enzyme
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.