Identification of peptides from ovine milk cheese manufactured with animal rennet or extracts of Cynara cardunculus as coagulant

• Type: Article in International Scientific Journal
• Date: 1998

Authors

Sousa, MJ (Author) Other; F. Xavier Malcata (Author) Other

Journal

Title: Journal of Agricultural and Food Chemistry

Vol. 46

Pages: 4034-4041

ISSN: 0021-8561

Publisher: American Chemical Society

Indexing

ISI Web of Knowledge - 23 Citations

Scopus - 30 Citations

Other information

Authenticus ID: P-001-70H

DOI: 10.1021/jf980188u

Abstract (EN): 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 beta-, alpha(s1)-, and alpha(s2)-caseins than the plant rennet. The water-soluble extract (WSE) from cheese produced by plant rennet was constituted by fragments of ovine beta- and alpha(s2)-caseins; peptides beta-(f128-*), beta-(f166-*), and beta-(f191-*) were produced only by plant rennet, whereas peptides beta-(f164-*) and beta-(f191-*) were produced only by animal rennet. The peptide beta-(f1-190) was identified as the primary product of ovine beta-casein degradation in the WISE for both rennets. The complementary peptides alpha(s1)-(f1-23) and alpha(s1)-(f24-191) were produced by both rennets from ovine alpha(s1)-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 alpha(s1)-(f24-165) was produced only by plant rennet, whereas the peptide alpha(s1)-(f120-191) was produced only by animal rennet. The peptides produced from bovine alpha(s2)-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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 8