title: Purification of cynarases from artichoke (Cynara scolymus L.): enzymatic properties of cynarase A.
abstract: Aspartic proteinases from flowers of Cynara cardunculus have been extensively studied and long used as coagulants in the manufacture of several traditional Spanish and Portuguese cheeses. These endopeptidases are called cardosins or cynarases, depending on the authors. However, the proteinases of another plant of the genus Cynara, the artichoke (Cynara scolymus), are less known, probably because the flower of this plant is usually consumed as a vegetable. In the study described here, three proteinases (cynarases A, B and C) with milk-clotting properties were purified from the stigma of artichoke. All three proteinases are glycoproteins and composed of a one large and one small subunit. The enzymatic properties of cynarase A, a glycoprotein containing N-linked high mannose type glycans, which express maximum activity at pH 5.0 and 70 degrees C, were studied in detail. Catalytic and inhibition studies indicated that this cynarase is of the aspartic acid type. The results indicate artichoke extract could also be used in the milk industry in the same way as the extract obtained from the flower of C. cardunculus.
authors.affiliation: Grupo de Investigación de Enzimología (GENZ)., Departamento de Bioquímica y Biología Molecular A, Facultad de Biología, Universidad de Murcia, E-30100 Espinardo, Murcia, Spain.
authors.forename: Lara
authors.initials: L
authors.lastname: Sidrach
authors.forename: Francisco
authors.initials: F
authors.lastname: García-Cánovas
authors.forename: José
authors.initials: J
authors.lastname: Tudela
authors.forename: José Neptuno
authors.initials: JN
authors.lastname: Rodríguez-López
mesh_terms: D000818:Animals; D002384:Catalysis; D031943:Cynara scolymus / Q000201:enzymology*; D035264:Flowers / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008892:Milk / Q000737:chemistry; D010436:Pepstatins / Q000494:pharmacology; D010447:Peptide Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D010940:Plant Proteins / Q000302:isolation & purification; D011480:Protease Inhibitors / Q000494:pharmacology; D013696:Temperature
chemical_list: D010436:Pepstatins; D010940:Plant Proteins; D011480:Protease Inhibitors; D010447:Peptide Hydrolases; C031375:pepstatin