Identification of Peptides from Ovine Milk Cheese Manufactured with Animal Rennet or Extracts of Cynara cardunculus as Coagulant
Abstract
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-, alphas1-, and alphas2-caseins than the plant rennet. The water-soluble extract (WSE) from cheese produced by plant rennet was constituted by fragments of ovine beta- and alphas2-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 alphas1-(f1-23) and alphas1-(f24-191) were produced by both rennets from ovine alphas1-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 alphas1-(f24-165) was produced only by plant rennet, whereas the peptide alphas1-(f120-191) was produced only by animal rennet. The peptides produced from bovine alphas2-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.
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Bands (a), (d) and (g) have electrophoretic mobilities similar to that of the primary product produced by proteinases from C. cardunculus on β-casein (β-I-casein) in bovine, ovine and caprine caseinates, via cleavage of the most susceptible bond Leu192-Tyr193 in bovine β-casein or Leu190-Tyr191 in ovine and caprine β-caseins.
“Those bands have electrophoretic mobilities similar to that of the primary product produced by proteinases from C. cardunculus on β-casein (i.e.β-I-casein) in bovine [48], ovine and caprine caseinates [56], via cleavage of the most susceptible bond Leu 192 -Tyr 193 in bovine β-casein or Leu 190 -Tyr 191 in ovine and caprine β-caseins (Fig. 1b).”
From Advances in the role of a plant coagulant ( <i>Cynara cardunculus</i> ) in vitro and during ripening of cheeses from several milk species (2002) · cites this paper as [56]
The main hydrolysis sites associated with C. cardunculus coagulant action are Leu127-Thr128, Leu165-Ser166 and Leu192-Tyr193 in bovine β-casein, Leu127-Thr128 and Leu190-Tyr191 in ovine β-casein, and Leu127-Thr128 and Leu190-Tyr191 in caprine β-casein.
“The main hydrolysis sites identified in association with said coagulant action were Leu 127 -Thr 128 , Leu 165 -Ser 166 and Leu 192 -Tyr 193 in bovine β-casein, Leu 127 -Thr 128 and Leu 190 -Tyr 191 in ovine β-casein [56], and Leu 127 -Thr 128 and Leu 190 -Tyr 191 in caprine β-casein.”
From Advances in the role of a plant coagulant ( <i>Cynara cardunculus</i> ) in vitro and during ripening of cheeses from several milk species (2002) · cites this paper as [56]
The peptides β-casein (f128-), β-casein (f166-) and β-casein (f191-) were produced by plant rennet only, whereas β-casein (f164-) and β-casein (f191-) were produced by animal rennet only.
“The peptides β-casein (f128-), β-casein (f166-) and β-casein (f191-) were produced by plant rennet only, whereas β-casein (f164-) and β-casein (f191-) were produced by animal rennet only [56].”
From Advances in the role of a plant coagulant ( <i>Cynara cardunculus</i> ) in vitro and during ripening of cheeses from several milk species (2002) · cites this paper as [56]
The peptide αs1-casein (f24-165) is present only in ovine cheese manufactured with C. cardunculus, whereas the peptide αs1-casein (f120-191) was only produced by animal rennet.
“These bands were identified as the peptide α s1 -casein (f24-165), which is present only in ovine cheese manufactured with C. cardunculus, whereas the peptide α s1casein (f120-191) was only produced by animal rennet [56].”
From Advances in the role of a plant coagulant ( <i>Cynara cardunculus</i> ) in vitro and during ripening of cheeses from several milk species (2002) · cites this paper as [56]
The peptides β-casein (f1-190) and αs-casein (f24-191) are the primary products originated by both coagulants from the corresponding caseins.
“The peptides β-casein (f1-190) and α s -casein (f24-191) were reported to be the primary products originated by both coagulants from the corresponding caseins [56];”
From Advances in the role of a plant coagulant ( <i>Cynara cardunculus</i> ) in vitro and during ripening of cheeses from several milk species (2002) · cites this paper as [56]
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Action of a cell wall proteinase (PI) from Streptococcus cremoris HP on bovine β-casein.
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Roseiro, L. B., Barbosa, M., Ames, J. M., & Wilbey, R. A. (2003) · International Journal of Dairy Technology · doi:10.1046/j.1471-0307.2003.00080.x · Cited by 200 · see citing works
Biochemistry of Cheese Ripening: Proteolysis
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Self-citationCardoon-Based Rennets for Cheese Production
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- Authors
- Sousa, M. J., & Malcata, F. X.
- Affiliations
- Escola Superior de Biotecnologia, Universidade Católica Portuguesa, Rua Dr. António Bernardino de Almeida, 4200 Porto, Portugal
- Universidade Católica Portuguesa (PT)
- Corresponding author
- Malcata, F. X.
- ORCID
- Malcata, F. X.
- Venue
- Journal of Agricultural and Food Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1998-09-24
- Volume
- 46
- Issue
- 10
- Pages
- 4034-4041
- ISSN
- 0021-8561 (ISSN-L)
- 1520-5118
- OpenAlex
- W2013911214
- Cited by
- 32
- References
- 2
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 1 · 2020: 1 · 2019: 1 · 2018: 1 · 2017: 3 · 2016: 2 · 2014: 2 · 2013: 1 · 2012: 2
- FWCI
- 0.12
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Agricultural and Food Chemistry (publishedVersion)
- Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Agricultural and Biological Sciences › Food Science › Food and Agricultural Sciences
- Keywords
- Cynara cardunculus, animal rennet, casein degradation, αs1-casein, αs2-casein, cheese proteolysis, cheese ripening, water-soluble extract, cheese microbiota
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