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Structural and Functional Aspects of Cardosins

1998; Springer Nature; Linguagem: Inglês

10.1007/978-1-4615-5373-1_58

2214-8019

Carlos Faro, Miguel Ramalho‐Santos, Paula Verı́ssimo, José Pissarra, Carlos Frazão, Júlia Costa, Xinli Lin, Jordan Tang, Euclides Pires,

Coagulation, Bradykinin, Polyphosphates, and Angioedema

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.