Comparative catalytic activity of two plant proteinases upon caprine caseins in solution
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Proteolysis by cardosin A is faster than by cardosin B.
“proteolysis by cardosin A was reported to be faster than by cardosin B [47].”
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 [47]
The primary and most susceptible sites for attack by both cardosins in caprine β-casein are Leu190-Tyr191 and Leu127-Thr128.
“one concludes that the primary (and most susceptible) sites with regard to attack by both cardosins in caprine β-casein are Leu 190 -Tyr 191 and Leu 127 -Thr 128 (Fig. 1b), whereas in caprine α s1 -casein they are Phe 23 -Val 24 and Phe 153 -Tyr 154 (Fig. 1c).”
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 [47]
Regarding specificity of cardosins A and B upon β-casein, either in caseinate or in pure forms, the major cleavage sites are Leu127-Thr128 and Leu190-Tyr191.
“Regarding the specificity of cardosins A and B upon β-casein, either in caseinate or in pure forms, the major cleavage sites were found to be Leu 127 -Thr 128 and Leu 190 -Tyr 191 ; conversely, in α s -casein, either in caseinate or in pure forms, both cardosins were reported to cleave the peptide bond Phe 153 -Tyr 154 [47].”
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 [47]
The primary and most susceptible sites for attack by both cardosins in caprine αs1-casein are Phe23-Val24 and Phe153-Tyr154.
“one concludes that the primary (and most susceptible) sites with regard to attack by both cardosins in caprine β-casein are Leu 190 -Tyr 191 and Leu 127 -Thr 128 (Fig. 1b), whereas in caprine α s1 -casein they are Phe 23 -Val 24 and Phe 153 -Tyr 154 (Fig. 1c).”
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 [47]
In αs-casein, either in caseinate or in pure forms, both cardosins cleave the peptide bond Phe153-Tyr154.
“Regarding the specificity of cardosins A and B upon β-casein, either in caseinate or in pure forms, the major cleavage sites were found to be Leu 127 -Thr 128 and Leu 190 -Tyr 191 ; conversely, in α s -casein, either in caseinate or in pure forms, both cardosins were reported to cleave the peptide bond Phe 153 -Tyr 154 [47].”
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 [47]
In caprine caseinate, β-caseins are hydrolysed to a higher degree than αs-caseins.
“In caprine caseinate, β-caseins were hydrolysed to a higher degree than α s -caseins, and proteolysis by cardosin A was reported to be faster than by cardosin B [47].”
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 [47]
Cites
Proteolytic Enzymes and Their Relation to Cheese Ripening and Flavor: An Overview
Visser, S. (1993) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(93)77354-3 · Cited by 305 · see citing works
Ver�ssimo, P., Esteves, C., Faro, C., & Pires, E. (1995) · Biotechnology Letters · doi:10.1007/bf00129389 · Cited by 148 · see citing works
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Chazarra, S., Sidrach, L., López-Molina, D., & Rodríguez-López, J. N. (2007) · International Dairy Journal · doi:10.1016/j.idairyj.2007.04.010 · Cited by 110 · see citing works
Sousa, M. J., & Malcata, F. X. (2002) · Le Lait · doi:10.1051/lait:2002001 · Cited by 84 · see citing works
Self-citationSilva, S. V., Allmere, T., Xavier Malcata, F., & Andrén, A. (2003) · International Dairy Journal · doi:10.1016/s0958-6946(03)00075-x · Cited by 48 · see citing works
Self-citation
- Authors
- Silva, S. V., & Malcata, F. X.
- Affiliations
- Universidade Católica Portuguesa (PT)
- ORCID
- Malcata, F.Xavier
- Venue
- Food Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-11
- Volume
- 71
- Issue
- 2
- Pages
- 207-214
- ISSN
- 0308-8146 (ISSN-L)
- OpenAlex
- W2009915581
- Cited by
- 15
- References
- 2
- Citations by year
- 2024: 1 · 2015: 1 · 2013: 1
- FWCI
- 1.12
- Type
- journal article
- Language
- en
- Open access
- green
- hdl.handle.net
- Licence
- Locations
- Food Chemistry (publishedVersion)
- Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) (submittedVersion, other-oa)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Cynara cardunculus studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Pineapple and bromelain studies
- Keywords
- Cynara cardunculus, αs1-casein, β-casein, proteolytic specificity, cleavage site
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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