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Purification and characterisation of milk‐clotting and caseinolytic activities of pepsin isolated from adult sheep abomasa
Author(s) -
Slamani Rosa,
Labadi Redouane,
Brahim Errahmani Mohamed,
Bellal Mohand Mouloud
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 - 10.1111/1471-0307.12492
Subject(s) - chymosin , pepsin , casein , chemistry , skimmed milk , proteolysis , food science , chromatography , biochemistry , enzyme
Ovine pepsin was isolated and assessed for its milk‐clotting properties and caseinolytic activity in comparison with commercial chymosin. Ovine pepsin showed similar responses to variations in pH , temperature and CaCl 2 concentration of milk compared with chymosin, although its pH sensitivity was higher. SDS ‐ PAGE electrophoretic analysis of the casein fractions treated with ovine pepsin showed that alpha‐casein was more susceptible to proteolysis than beta‐casein, in contrast to chymosin. Curd‐firming properties of skim milk gels obtained with ovine pepsin and chymosin were evaluated by Gelograph under the same conditions. Curd produced using ovine pepsin was less firm than that made with chymosin.