Abstract
Cardosins are aspartic proteinases of the flowers of Cynara cardunculus L. These flowers have economical relevance in Portugal since they are traditionally used in the manufacture of highly appreciated ewe cheeses such as Serra, Azeitäo and Serpa. Although the milk-clotting activity of the cardoon has been exploited for centuries, the biochemistry of the process was relatively unknown until some years ago when we and other laboratories started to study both basic and applied aspects of the cardoon preparation [1–7]. In a first stage it was demonstrated that the milk-clotting activity is due to the presence of aspartic proteinases which cleave the peptide bond Phe 105–Met 106 of k-casein [1,3], a bond also cleaved by other milk-clotting enzymes used for cheese making [8]. Cleavage of this bond is known to induce destabilization of the casein micelle and subsequent formation of a clot, [9], and thus it is possible that the milk-clotting process induced by cardoon proteinases occurs in a similar way. However, the organoleptic properties of the products obtained with the flower of cardoon are clearly different from those of cheeses made from the same milk with chymosin or microbial rennets [10], stressing the unique characteristics of the cardoon enzymes.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Similar content being viewed by others
References
Faro, C.J., Alface, J.S. and Pires, E.V. (1987) Purification of a protease from the flowers of Cynara cardunculus L. Ciênc. Biol 12, 5A, 201.
Heimgartner, U., Pietrzak, M., Geertsen, R., Brodelius, P., Figueiredo, A.C. and Pais, M.S.(1990) Purification and partial characterization of milk clotting proteinases from flowers of Cynara cardunculus L. Phytochemistry 29, 1405–1410.
Faro, C.J., Moir, A.G.J, and Pires, E.M.V. (1992) Specificity of a milk clotting enzyme extracted from the thistle Cynara cardunculus L.: action on oxidised insulin and k-casein Biotech. Lett. 14, 841–S47.
Macedo, I.Q., Faro, C.J. and Pires, E.M.(1993) Specificity and kinetics of the milk clotting enzyme from cardoon (Cynara cardunculus L) toward bovine k-casein”. J. Agrie. Food Chem. 41, 1537–1540.
Verissimo, P.C., Esteves, C, Faro, C.J. and Pires, E. (1995) The vegetable rennet from Cynara cardunculus L. contains two proteinases with chymosin-Iike and pepsin-like specificities” Biotech. Lett. 17, 614–645.
Veríssimo, P., Faro, C, Moir, A., Lin, Y., Tang, J. and Pires, E. (1996) Purification, characterization and partial amino acid sequencing of two novel aspartic proteinases from the flowers of Cynara cardunculus L. Eur. J. Biochem. 235, 762–768.
Cordeiro, M., Jakob, E., Puhan, Z., Pais, M.S. and Brodelius, P.E. (1992) Milk clotting and proteolytic activities of purified cynarases from Cynara cardunculus L.-a comparison to chymosin. Milchwissenschaft 47, 683–687.
Drohse, H.B. and Foltman, B. (1989) Specificity of milk-clotting enzymes towards bovine k-casein Biochem. Biophys. Acta 995, 221–224.
Visser, S. (1981) Proteolytic enzymes and their action on milk proteins: a review. Neth. Milk Dairy J. 35, 65–88.
Sá, F.V. and Barbosa, M. (1972) Cheese-making with a vegetable rennet from cardo (Cynara cardunculus). J. Dairy Res. 39, 335–343.
Verissimo, P., Ramalho-Santos, M., Faro, C. and Pires, E. (1998) A comparative study on the aspartic proteinases from different species of Cynara. In structure and function of aspartic proteinases: retroviral and cellular enzymes (M. N. G. James, ed.) New York: Plenum Press.
Faro, C, Verissimo, P., Lin, Y., Tang, J. and Pires, E. (1995) Cardosins A and B, aspartic proteinases from the flowers of cardoon. In Aspartic proteinases: structure, function, biology and biomedical implications (Takahashi, K., ed.) New York: Plenum Press, pp. 374–377.
Ramalho-Santos, M., Verissimo, P., Faro, C.J. and Pires, E.V.(1996) Action on bovine as 1-casein of cardosins A and B, aspartic proteinases from the flowers of the cardoon Cynara cardunculus L. Biochem. Biophys. Acta 1297, 83–89.
Simões, I., Verissimo, P., Faro, C. and Pires, E.V. Action on bovine ß-casein of cardosins A and B, aspartic proteinases from the flowers of the cardoon Cynara cardunculus L. (submitted for publication).
Asakura T, Watanabe H, Abe K, Arai S (1995) Rice aspartic proteinase, oryzasin, expressed during seed ripening and germination, has a gene organization distinct from those of animal amd microbial aspartic proteinases. Eur J Biochem 232: 77–83.
Cordeiro MC, Xue Z-T, Pietrzak M, Pais MS, Brodelius PE (1994) Isolation and characterization of a cDN A from flowers of Cynara cardunculus encoding cyprosin (an aspartic proteinase) and its use to study the organ-specific expression of cyprosin. Plant Mol Biol 24: 733–741.
Runeberg-Roos P, Törmäkangas K, Östman A (1991) Primary structure of a barley-grain aspartic proteinase. Eur J Biochem 202: 1021–1027.
Leahy, D.J., Aukhil, I. and Erickson H.P. (1996) 2.0 A Crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell 84, 155–164.
Guruprasad K, Törmäkangas K, Kervinen J, Blundell TL (1994) Comparative modelling of barley-grain aspartic proteinase: a structural racionale for observed hydrolytic specificity. FEBS Lett 352: 131–136.
Costa, J., Ashford, A., Nimetz, M., Bento, I., Frazão, C, Esteves, C, Faro, C, Kervinen, J, Pires, E., Verissimo, P., Wlodawer, A., Carrondo, MA. (1997) The glycosylation of barley (Hordeum vulgare L.) and cardoon (Cynara cardunculus L) aspartic proteinases Eur. J. Biochem. (in press).
Tang, J. and Wong, R.N.S. (1987) Evolution in the structure and function of aspartic proteinases J. Cell Biochem. 33, 53–63.
Davies, D.R.(1990) The structure and function of the aspartic proteinases Annu. Rev. Biophys. Chem. 19, 189–215.
Ramalho-Santos, M., Pissarra, J., Pires, E. and Faro, C.(1997) Cardosinogen A, a precursor form of the major aspartic proteinase from cardoon. In structure and function of aspartic proteinases: retroviral and cellular enzymes (M.N.G James.ed.) New York: Plenum Press.
Ramalho-Santos, M., Pissarra, J., Verissimo, R, Pereira, S., Salema, R., Pires, E. and Faro, C.(1997) “Car-dosin A accumulates in protein storage vacuoles of the stigmatic pappilae of Cynara cardunculus L.” Planta (accepted for publication).
Kervinen, J., Tormakangas, K., Runeberg-Roos, P., Guruprasad, K., Blundell, T. and Teeri, T.H. (1995) Structure and possible function of aspartic proteinases in barley and other plants In Aspartic proteinases: structure, function, biology and biomedical implications (Takahashi, K., ed.) New York: Plenum Press, pp. 241–254.
Tokes, Z.A., Woon, W.C. and Chambers, S.M. (1974) Digestive enzymes secreted by the carnivorous plant napenthes macferlaine L. Planta 119, 39–46.
Elleman CJ, Dickinson HG (1994) Pollen-stigma interaction during sporophytic self-incompatibility in Brassica oleracea. In EG Williams, AE Clarke, RB Knox, eds, Genetic Control of Self-Incompatibility and Reproductive Development in Flowering Plants. Kluwer Academic Publishers, Dordrecht, pp 67–87.
Nasrallah JB, Stein JC, Kandasamy MK, Nasrallah ME (1994) Signaling the arrest of pollen tube development in self-incompatible plants. Science 266: 1505–1508.
Boiler T (1986) Roles of proteolytic enzymes in interactions of plants with other organisms. In MJ Dalling ed, Plant Proteolytic Enzymes, Vol 1. CRC Press, Boca Raton, pp. 67–96.
Kraulis, P. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallogr. 24, 946–950.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1998 Springer Science+Business Media New York
About this chapter
Cite this chapter
Faro, C. et al. (1998). Structural and Functional Aspects of Cardosins. In: James, M.N.G. (eds) Aspartic Proteinases. Advances in Experimental Medicine and Biology, vol 436. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5373-1_58
Download citation
DOI: https://doi.org/10.1007/978-1-4615-5373-1_58
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-7452-7
Online ISBN: 978-1-4615-5373-1
eBook Packages: Springer Book Archive