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Authors
Advisor(s)
Abstract(s)
Urea-PAGE of the water-insoluble extract (WISE) of ovine raw milk cheeses manufactured with
proteinases of Cynara cardunculus or with commercial animal rennet indicated that the animal
rennet acts more intensively, in quantitative terms, on ovine â-, Rs1-, and Rs2-caseins than the plant
rennet. The water-soluble extract (WSE) from cheese produced by plant rennet was constituted by
fragments of ovine â- and Rs2-caseins; peptides â-(f128-*), â-(f166-*), and â-(f191-*) were produced
only by plant rennet, whereas peptides â-(f164-*) and â-(f191-*) were produced only by animal
rennet. The peptide â-(f1-190) was identified as the primary product of ovine â-casein degradation
in the WISE for both rennets. The complementary peptides Rs1-(f1-23) and Rs1-(f24-191) were
produced by both rennets from ovine Rs1-casein; however, the bond Phe23-Val24 was cleaved by as
early as 7 days in cheese manufactured with C. cardunculus, whereas 28 days had to elapse before
that could be detected in the case of animal rennet. The peptide Rs1-(f24-165) was produced only
by plant rennet, whereas the peptide Rs1-(f120-191) was produced only by animal rennet. The
peptides produced from bovine Rs2-casein in cheese could not be traced as deriving from the action
of proteinases from either rennet, so their existence is likely due to proteinases or peptidases released
in cheese as a result of its indigenous microflora.
Description
Keywords
Thistle flower Cheese-making Cheese ripening Proteolysis Enzyme activity
Pedagogical Context
Citation
SOUSA, M. J.; MALCATA, F. X. - Identification of peptides from ovine milk cheese manufactured with animal rennet or extracts of Cynara Cardunculus as coagulant. Journal of Agricultural and Food Chemistry. ISSN 0021-8561. Vol. 46 n.º 10 (1998), p 4034–4041
Publisher
American Chemical Society