Specificity and kinetics of the milk-clotting enzyme from cardoon (Cynara cardunculus L.) toward bovine .kappa.-casein
Open accessAbstract
The action of Cynara cardunculus L. protease on whole bovine K-casein, over a 3-h period at pH 6.4, \nwas investigated. RpHPLC of the 3% trichloroacetic acid (TCA)-solublefraction of the K-casein digestion \nmixture showed three peptide peaks, which were identified by amino acid analysis and N-terminal \nanalysis as the 106-169 fragment [caseinomacropeptide (CMP)]. Upon selective precipitation with \n12% TCA, one glycosylated and two nonglycosylated forms of CMP were distinguished. Analysis of \nthe whole digestion mixture showed no additional peptides. The kinetics of hydrolysis of the PhelO5- \nMet106 bond was studied by spectrofluorometry, using fluorescein isothiocyanate-labeled K-casein (FTC- \nK-casein). The values obtained for kat, k, and k were 1.04 s-l, 0.16 pM, and 6.5 pM-l s-l, respectively. \nThe proteolytic coefficient is of the same order of magnitude as those obtained for other milk-clotting \nenzymes, but the k, is significantly lower, which reflects the higher affinity of Cynara protease to \nK-casein
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Extracts of Cynara spp. have been used in making Portuguese Serra and Serpa cheeses, Spanish Los Pedroches, La Serena, Torta del Casar, Los Ibores, and Flor de Guía cheeses.
“The extracts of Cynara spp.have been used in the making of Portuguese Serra and Serpa cheeses (Macedo et al. 1993) and Spanish Los Pedroches, La Serena (Roa et al. 1999) and Torta del Casar cheeses (from ewes' milk) as well as Los Ibores cheese (from goats' milk) and Flor de Guía cheese (from a mixture of ewes' and cows' milk) (Fernández-Salguero et al. 1991;Fernández-Salguero 1999;Sanjuán et al.”
From Plant proteases as milk-clotting enzymes in cheesemaking: a review (2014) · cites this paper as Macedo et al. 1993
The Introduction (page not provided) says cardoon protease is traditionally used in Portugal to make Serra cheese. It does not mention Serpa cheese. The Spanish cheeses in the citing sentence are attributed to other citations, not to Macedo et al. (LLM, conf=0.88)
Experimental — accuracy not yet measuredThe major cleavage site of bovine and ovine κ-casein is Phe105-Met106, whereas caprine κ-casein is preferentially cleaved at Lys116-Thr117.
“The major cleavage site of bovine [31] and ovine κ-casein is Phe 105 -Met 106 , whereas caprine κ-casein is preferentially cleaved at Lys 116 -Thr 117 [55] (Fig. 1a).”
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 [31]
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Self-citation
- Authors
- Macedo, I. Q., Faro, C. J., & Pires, E. M.
- Affiliations
- University of Coimbra (PT)
- Venue
- Journal of Agricultural and Food Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1993-10
- Volume
- 41
- Issue
- 10
- Pages
- 1537-1540
- ISSN
- 0021-8561 (ISSN-L)
- 1520-5118
- OpenAlex
- W2031933211
- Cited by
- 75
- References
- 15
- Citations by year
- 2025: 1 · 2023: 1 · 2022: 2 · 2021: 2 · 2020: 3 · 2019: 2 · 2018: 4 · 2017: 4 · 2016: 1 · 2014: 2 · 2013: 2 · 2012: 1
- FWCI
- 1.96
- Type
- journal article
- Language
- en
- Open access
- green
- hdl.handle.net
- Locations
- Journal of Agricultural and Food Chemistry (publishedVersion)
- Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) (submittedVersion)
- Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) (submittedVersion, other-oa)
- Funders
- Universidade de Aveiro
- Iran Nanotechnology Initiative Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Cynara cardunculus studies
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Keywords
- Cynara cardunculus, milk-clotting enzyme, bovine kappa-casein, casein hydrolysis, caseinomacropeptide, hydrolysis kinetics, substrate specificity, protease specificity
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