cynara scolymus/protease

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Hydrolysis of whey proteins by proteases extracted from Cynara cardunculus and immobilized onto highly activated supports.

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Blends of cardosins A and B, enzymes present in aqueous extracts of the flowers of the thistle (Cynara cardunculus L.), have for long been used as rennets by the cheesemaking industry in the Iberian Peninsula. These dimeric proteases are present in the stigmae and stylets of said flowers, and are

Use of artichoke (Cynara scolymus) flower extract as a substitute for bovine rennet in the manufacture of Gouda-type cheese: characterization of aspartic proteases.

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Artichoke (Cynara scolymus L.) flower extract was assayed with the aim of replacing animal rennet in the manufacture of Gouda-type cheeses from bovine milk. Floral extract coagulated milk within a suitable time for use on an industrial scale, while the yield of cheese obtained was equal to that

Comparative structure-function characterization of the saposin-like domains from potato, barley, cardoon and Arabidopsis aspartic proteases.

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The present study characterized the aspartic protease saposin-like domains of four plant species, Solanum tuberosum (potato), Hordeum vulgare L. (barley), Cynara cardunculus L. (cardoon; artichoke thistle) and Arabidopsis thaliana, in terms of bilayer disruption and fusion, and structure

Enzymatic milk clotting activity in artichoke (Cynara scolymus) leaves and alpine thistle (Carduus defloratus) flowers. Immobilization of alpine thistle aspartic protease.

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Two different milk clotting enzymes, belonging to the aspartic protease family, were extracted from both artichoke leaves and alpine thistle flowers, and the latter was covalently immobilized by using a polyacrylic support containing polar epoxy groups. Our findings showed that the alpine thistle

Plant Aspartic Proteases for Industrial Applications: Thistle Get Better.

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Plant proteases have a number of applications in industrial processes including cheese manufacturing. The flower of the cardoon plant (Cynara cardunculus L.) is traditionally used as a milk-clotting agent in protected designation of origin cheeses made from goat and sheep milk. Plant-derived

Protease and hemicellulase assisted extraction of dietary fiber from wastes of Cynara cardunculus.

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The action of protease and hemicellulase for the extraction of fractions enriched in soluble fiber from bracts and stems of Cynara cardunculus was evaluated. Using a two-factor simplex design comprising protease amounts of 0-200 μL and hemicellulase amounts of 0-200 mg for 5 g of material, we

Toward alternative sources of milk coagulants for cheese manufacturing: establishment of hairy roots culture and protease characterization from Cynara cardunculus L.

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Extracts from hairy root cultures of Cynara cardunculus L. contain proteases and show milk-clotting activity. Cynara cardunculus L. or cardoon is often used as rennet in traditional cheese manufacturing, due to the presence of specific proteases in the flower. However, the flower extracts are

Characterization and expression analysis of the aspartic protease gene family of Cynara cardunculus L.

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Cardosin A and cardosin B are two aspartic proteases mainly found in the pistils of cardoon Cynara cardunculus L., whose flowers are traditionally used in several Mediterranean countries in the manufacture of ewe's cheese. We have been characterizing cardosins at the biochemical, structural and

Isolation and partial characterization of rennet-like proteases from Australian cardoon (Cynara cardunculus L.).

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The yield, protein content, proteolytic activity, and substrate specificity of crude and partially purified extracts from dried and fresh Australian cardoon (Cynara cardunculus L.) flowers were determined. Crude water extracts had high yield but low protein content and proteolytic activity, whereas

Bioactive peptides in ovine and caprine cheeselike systems prepared with proteases from Cynara cardunculus.

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The potential angiotensin-converting enzyme (ACE)-inhibitory and antioxidant activities of peptides in water-soluble extracts, obtained from raw and sterilized ovine and caprine cheeselike systems coagulated with enzymes from the plant Cynara cardunculus, were assessed. Prior to the assay, the

Bioactivity of hydrolysates obtained from bovine casein using artichoke (Cynara scolymus L.) proteases.

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The objective of this work was to obtain casein hydrolysates with aspartic proteinases present in extracts from the artichoke flower (Cynara scolymus L.) and evaluate their antioxidant, antimicrobial, and angiotensin-I converting enzyme (ACE) inhibitory activity in vitro. The casein hydrolysates

Cardosin A and B, aspartic proteases from the flowers of cardoon.

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Influence of the ripening stage and the lyophilization of wild cardoon flowers on their chemical composition, enzymatic activities of extracts and technological properties of cheese curds.

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The selection of an appropriate Cynara cardunculus flowers batch is a preliminary step to produce rennet with better clotting properties. For this reason, we proposed to study the influence of the ripening stage and the lyophilization of cardoon flowers on their chemical composition, enzymatic

Modeling the kinetics of whey protein hydrolysis brought about by enzymes from Cynara cardunculus.

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The purpose of this research work was to study the proteolytic activity of aqueous crude extracts of flowers of the plant Cynara cardunculus on the major whey proteins, namely, beta-lactoglobulin (beta-Lg) and alpha-lactalbumin (alpha-La). These extracts, containing a mixture of cardosins A and B

Purification and characterization of a milk-clotting aspartic proteinase from globe artichoke (Cynara scolymus L.).

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The study of proteinase expression in crude extracts from different organs of the globe artichoke (Cynara scolymus L.) disclosed that enzymes with proteolytic and milk-clotting activity are mainly located in mature flowers. Maximum proteolytic activity was recorded at pH 5.0, and inhibition studies

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