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Proteolysis in miniature Cheddar‐type cheeses made using blends of chymosin and Cynara cardunculus proteinases as coagulant
Author(s) -
O'Mahony James A,
Sousa Maria J,
Mcsweeney Paul L H
Publication year - 2003
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 - 10.1046/j.1471-0307.2003.00078.x
Subject(s) - cynara , chymosin , chemistry , food science , proteolysis , casein , chromatography , enzyme , botany , biochemistry , biology
Miniature (20 g) Cheddar‐type cheeses were manufactured using blends of Cynara cardunculus proteinases and chymosin as coagulant (100 : 0, 50 : 50, 25 : 75 and 0 : 100 C. cardunculus proteinases : chymosin). There were no substantial differences between the compositions of cheeses made using any of the four coagulant blends. Cheeses manufactured with coagulant blends containing C. cardunculus proteinases exhibited higher levels of pH 4.6‐soluble nitrogen than cheese made using chymosin as coagulant. The extent of breakdown of α s1 ‐casein, as measured by urea‐polyacrylamide gel electrophoresis (urea‐PAGE), was greater in cheeses made using coagulant preparations containing C. cardunculus proteinases as a constituent than in cheese made using 100% chymosin as coagulant. Different reverse‐phase high‐performance liquid chromatography (RP‐HPLC) peptide profiles of the ethanol‐soluble and ‐insoluble fractions were obtained for cheeses made using either C. cardunculus proteinases or chymosin as coagulant. Principal component analysis and hierarchical cluster analysis of RP‐HPLC data confirmed that the inclusion of even small proportions (25%) of C. cardunculus proteinases with chymosin in the coagulant blend greatly altered the pattern and extent of proteolysis in miniature Cheddar‐type cheeses.