Results 11 to 20 of about 537 (137)
Thermostability of cardosin A from Cynara cardunculus L. [PDF]
Thermochimica Acta, 2003 The structural stability of cardosin A, a plant aspartic proteinase (AP) from Cynara cardunculus L., has been investigated by high-sensitivity differential scanning calorimetry, intrinsic fluorescence and circular dichroism spectroscopy, and enzymatic activity assays.
Pina, David G. +8 more
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Action of cardosin A from Cynara humilis on ovine and caprine caseinates [PDF]
Journal of Dairy Research, 2000 In the Iberian Peninsula, the proteinases present in the flowers of members of the Cynara genus, C. cardunculus, C. humilis and C. scolymus, have for many years been successfully used in the manufacture of traditional cheeses from ovine and/or caprine milk on individual farms (Vieira de Sá & Barbosa, 1972; Trujillo et al. 1994). In Portugal, C.
Silva, Sofia V., Malcata, F. Xavier
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A kinetic model for hydrolysis of whey proteins by cardosin A extracted from Cynara cardunculus [PDF]
Food Chemistry, 2004 The enzymatic hydrolysis of the major whey proteins, namely β-lactoglobulin (β-Lg) and α-lactalbumin (α-La), was experimentally studied using whey as substrate; an aspartic protease (cardosin A), previously extracted from the flowers of Cynara cardunculus and purified by gel filtration and ion exchange chromatographies, was used for this purpose. Sweet
Barros, Rui M., Malcata, F. Xavier
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Evaluation of cardosin A as a proteolytic probe in the presence of organic solvents
Journal of Molecular Catalysis B: Enzymatic, 2004 This investigation showed that cardosin A not only is active in media with organic solvents, cleaving the β-chain of oxidised insulin at three susceptible peptide bonds, but also maintains its specificity in all media tested. Additionally, the presence of organic solvents in the reaction media led to modifications of enzyme selectivity, which enabled ...
Sarmento, A.C. +4 more
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Planta, 2008 Cardosin A is the major vacuolar aspartic proteinase (APs) (E.C.3.4.23) in pistils of Cynara cardunculus L. (cardoon). Plant APs carry a unique domain, the plant-specific-insert (PSI), and a pro-segment which are separated from the catalytic domains during maturation but the sequence and location of processing steps for cardosins have not been ...
Duarte, P, Pissarra, J, Moore, I
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Unfolding of cardosin A in organic solvents and detection of intermediaries
Journal of Molecular Catalysis B: Enzymatic, 2009 In the present study the relationship between conformational stability and enzymatic activity in the presence of organic solvents (OS) was investigated. We have found that cardosin A, the model protease investigated in this work, inactivates through a biphasic mechanism, which is incipient in aqueous buffer and becomes visible in the presence of ...
Sarmento, Ana Cristina +7 more
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Proteolysis of ovine caseins by cardosin A, an aspartic acid proteinase from Cynara cardunculus L. [PDF]
Le Lait, 1998 The breakdown of αs-caseins and β-caseins (in the form of αs-caseins, the form of β-caseins, and the form of a mixture of αs- and β-caseins in Na-caseinate) by cardosin A, one of the major two proteinases present in the flowers of Cynara cardunculus L., was experimentally studied via urea polyacrylamide gel electrophoresis.
Silva, Sofia V., Malcata, F. Xavier
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Cardosin A is an aspartic protease present in large amount in the pistils of cardoon flowers. This protease is known to contain an -Arg-Gly-Asp- (RGD) motif located on the molecular surface. In this study, we found that isolated recombinant cardosin A attached to human epithelial cells A549, mediated by the binding of its RGD motif to cell surface ...
Wu, Hao +3 more
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Cardosins A and B, two new enzymes available for peptide synthesis [PDF]
Journal of Molecular Catalysis B: Enzymatic, 1998 Abstract Two new aspartic proteases, Cardosins A and B, with a high specificity toward bonds between hydrophobic amino acids were isolated from the flowers of the cardoon, Cynara cardunculus L., and recently characterised [C.J. Faro, A.G.J. Moir, E. Pires, Biotech. Lett., 14 (1992) 841.]; [P. Verissimo, C. Faro, A.J.G. Moir, Y. Lin, J.
Sarmento, Ana Cristina +3 more
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Cynara cardunculus as a potential source of milk coagulating protease: Effects on physical properties of cow's milk. [PDF]
Food Sci Nutr, 2022 ‐Cynara cardunculus flowers were extracted using different types of buffers for different maceration times ‐Formation of milk gels prepared in the presence of CE with different types of milk was evaluated using dynamic rheology and Turbiscan ‐ Textural properties and the curd‐firming rate of coagulum were determined Abstract In the present research ...
Ghribi AM +5 more
europepmc +2 more sources