Results 111 to 120 of about 537 (137)
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Effect of acetonitrile on Cynara cardunculus L. cardosin A stability

International Journal of Biological Macromolecules, 2006
The kinetics of the structural changes affecting cardosin A, a plant aspartic proteinase (AP) from Cynara cardunculus L., in the presence of a mixture of acetonitrile (AN) in water (W) was studied. Incubation of cardosin A with 10% (v/v) AN resulted in a gradual increase in protein helicity, accompanied by changes in the tertiary structure, seen by ...
Shnyrova, Anna V.   +6 more
openaire   +2 more sources

Structural and Functional Aspects of Cardosins

1998
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, Azeitao and Serpa. Although the milk-clotting activity of the cardoon has been exploited for centuries, the biochemistry of ...
C, Faro   +8 more
openaire   +2 more sources

Caseinolytic Specificity of Cardosin, an Aspartic Protease from the Cardoon Cynara cardunculus L.:  Action on Bovine αs- and β-Casein and Comparison with Chymosin [PDF]

open access: yesJournal of Agricultural and Food Chemistry, 1996
The action of cardosin on bovine αs- and β-casein at 30 °C in 50 mM citrate buffer (pH 6.2) was studied. Peptides were isolated by reversed-phase HPLC on C18 columns and identified from their amino acid composition and N-terminal amino acid sequence. The
Carlos Faro
exaly   +2 more sources

Cardosin A and B, Aspartic Proteases from the Flowers of Cardoon

1995
Plant aspartic proteinases have been detected and purified from several plant monocotyledoneous, dicotyledoneous and gymnosperms. The physiological role of these aspartic proteinases is not as yet well elucidated, although the involvement in the hydrolysis of exogenous and storage proteins have been reported (for review see reference 1)
C, Faro   +4 more
openaire   +2 more sources

Cloning and Characterization of cDNA Encoding Cardosin A, an RGD-containing Plant Aspartic Proteinase* [PDF]

open access: yesJournal of Biological Chemistry, 1999
Cardosin A is an abundant aspartic proteinase from pistils of Cynara cardunculus L. whose milk-clotting activity has been exploited for the manufacture of cheese. Here we report the cloning and characterization of cardosin A cDNA. The deduced amino acid sequence contains the conserved features of plant aspartic proteinases, including the plant-specific
Carlos Faro   +2 more
exaly   +3 more sources

Immobilisation of Cardosin A in Chitosan Sponges as a Novel Implant for Drug Delivery

Current Drug Discovery Technologies, 2005
Cardosin A is extracted from the pistils of the plant Cynara cardunculus L. and chitosan is a polysaccharide derived from chitin with valuable properties as a biomaterial. In this work we report our experiments on the synthesis of chitosan sponges and immobilisation of cardosin A, by entrapment.
Pereira, Anabela O.   +6 more
openaire   +3 more sources

Crystallisation, Structure Solution, and Initial Refinement of Plant Cardosin-A

1998
In the cheese industry, calf chymosin is universally used as one of the main milk-clotting enzymes. However, in traditional cheese manufacturing, several other coagulating agents have also been used for a long time. A special case in Portugal, involves the use of an enzyme preparation obtained by aqueous extraction of cardoon flowers (Cynara ...
I, Bento   +10 more
openaire   +2 more sources

Engineering a cardosin B-derived rennet for sheep and goat cheese manufacture

Applied Microbiology and Biotechnology, 2014
Different sheep and goat cheeses with world-renowned excellence are produced using aqueous extracts of Cynara cardunculus flowers as coagulants. However, the use of this vegetable rennet is mostly limited to artisanal scale production, and no effective solutions to large-scale industrial applications have been reported so far.
Carla Malaquias, Almeida   +3 more
openaire   +2 more sources

Evaluation of cardosin A as a probe for limited proteolysis in non-aqueous environments—complex substrates hydrolysis

Enzyme and Microbial Technology, 2006
Cardosin A is an aspartic proteinase, like pepsin, purified from the cardoon, Cynara cardunculus L. and has been traditionally used in Portugal in the manufacture of traditional cheeses, due to its milk clotting activity. This enzyme is a fine example of a small number of plant aspartic proteinases that have been isolated, purified and characterised ...
Ana S. Duarte   +2 more
exaly   +3 more sources

Activity of cardosins A and B in the presence of organic solvents

1998
Cardosin A and cardosin B are two aspartic proteinases extracted from Cynara cardunculus L. stigma [1]. These enzymes show different specificities, although they prefer bonds between hydrophobic residues. In a previous work [2] we have shown that cardosins are stable and active in a biphasic (aqueous/organic) system.
Ana Cristina Sarmento   +2 more
openaire   +1 more source

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