Cited by 56Cynara cardunculus studiesEnzyme Production and CharacterizationPineapple and bromelain studies

Action on bovine αs1-casein of cardosins A and B, aspartic proteinases from the flowers of the cardoon Cynara cardunculus L.

Ramalho-Santos, Miguel, Veríssimo, Paula, Faro, Carlos, Pires, Euclides·1996·Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Abstract

The cleavage of purified bovine alpha s1-casein separately by cardosin A and cardosin B, two distinct milk-clotting aspartic proteinases (APs) present in the stigmas of the plant Cynara cardunculus L., was studied. Casein digestion peptides were separated either by SDS-PAGE or by reverse-phase HPLC, and their N-terminal amino acid sequences were subsequently determined by automated Edman degradation, thus identifying the cleavage sites. Results showed that both enzymes exert a similar but distinct action on bovine alpha s1-casein. In common they have the preference for the bond Phe23-Phe24, and the cleavage of Trp164-Tyr165 and Phe153-Tyr154. Cardosin A also cleaves the bond Tyr165-Tyr166, whereas Cardosin B cleaves an extra type of bond, Phe150-Arg151, revealing a slightly broader specificity. A model for the action of both enzymes on bovine alpha s1-casein is proposed and discussed. In comparison with the reported action of chymosin on bovine alpha s1-casein, both cardosins proved to have a broader specificity towards this particular substrate due to a higher ability to cleave bonds between residues with large hydrophobic side-chains.

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Crossref · 10.1016/0167-4838(96)00103-3

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  • Comparison of results suggests that the bonds in pure caseins (or in sodium caseinate) most susceptible to cardosins A and B are Leu190-Tyr191 and Leu127-Thr128 in β-casein, and Phe23-Val24 and Trp164-Tyr165 in αs1-casein.

    “However, comparison of the results reported by Ramalho-Santos et al. [38,39], by Sousa and Malcata [55], and by Silva and Malcata [46] suggests that the bonds in pure caseins (or in sodium caseinate, for that matter) most susceptible to cardosins A and B are Leu 190 -Tyr 191 and Leu 127 -Thr 128 in β-casein (Fig. 1b), and Phe 23 -Val 24 and Trp 164 -Tyr 165 in α s1 -casein (Fig. 1c).”

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Authors
Ramalho-Santos, M., Veríssimo, P., Faro, C., & Pires, E.
Affiliations
University of Coimbra (PT)
Corresponding author
Faro, Carlos
Venue
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
Publisher
Elsevier BV
Published
1996-09
Volume
1297
Issue
1
Pages
83-89
ISSN
0167-4838 (ISSN-L)
OpenAlex
W2045977252
Cited by
56
References
2
Citations by year
2026: 2 · 2025: 1 · 2023: 1 · 2021: 1 · 2020: 3 · 2019: 1 · 2018: 3 · 2017: 1 · 2016: 1 · 2014: 4 · 2013: 2
FWCI
6.55
Type
journal article
Language
en
Open access
closed
Locations
  • Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology (publishedVersion)
  • PubMed (publishedVersion)
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
aspartic protease, Cynara cardunculus, cleavage site, substrate specificity, milk-clotting enzyme, chymosin, protein digestion
MeSH terms
Animals, Arginine, Caseins, Cattle, Molecular Weight, Peptide Fragments, Phenylalanine, Plant Proteins, Plants, Substrate Specificity, Tryptophan, Tyrosine, Aspartic Acid Endopeptidases, Sequence Analysis

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