Chemical characterization of proteases extracted from wild thistle (Cynara cardunculus)

Campos, Rolando; Guerra, Ricardo; Aguilar, Marlene; Ventura, Oro; Camacho, L.

doi:10.1016/0308-8146(90)90023-w

Cited by 43 publications

(37 citation statements)

References 9 publications

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“…The ratios of milk-clotting activity/proteolytic activity were, therefore, 0.14 and 0.6 for CECF and commercial rennet, respectively. Similarly, Campos et al (1990) reported a higher proteolytic activity of cardoon crude extract and a less milk-clotting activity than calf rennet. According to Roseiro et al (2003), clotting activity relates to the enzyme's ability to cut the peptide bond Phe (105)-Met (106) of k-casein, which is considered as specific for cheesemaking, and the excessive proteolytic activity of extracts from Cynara species is due to their broader specificity for caseins.…”

Section: Resultsmentioning

confidence: 88%

“…Similarly, Campos et al . () reported a higher proteolytic activity of cardoon crude extract and a less milk‐clotting activity than calf rennet. According to Roseiro et al .…”

Section: Resultsmentioning

confidence: 96%

“…Similarly, previous studies have reported an optimum activity of enzymatic extracts from C. cardunculus between 60 and 70 °C (Campos et al . ).…”

Section: Resultsmentioning

confidence: 97%

See 2 more Smart Citations

Enzymatic extract from flowers of Algerian spontaneous Cynara cardunculus: Milk‐clotting properties and use in the manufacture of a Camembert‐type cheese

Zikiou

Zidoune

2018

Int J of Dairy Tech

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The aim of this study was to assess the coagulant properties of crude extract from cardoon flowers (CECF) as a replacement for the imported coagulants used in the local Algerian cheese factories. Optimal coagulation activity of the extract was observed at pH 5 and 60 °C with a CaCl2 concentration of 0.02 M. The electrophoretic pattern revealed that the crude extract contains mainly cardosins A and B. The study of interactions involved in the formation of milk gel coagulated by CECF showed that hydrogen forces, hydrophobic interactions and calcium bridges contributed highly to the formation of milk gel. Camembert‐type cheese obtained by CECF was judged by trained panellists and was found to be in agreement with standard specifications. The present study highlights the possibility of using Algerian CECF as a promising plant coagulant in cheesemaking for the dairy industry.

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Section: Resultsmentioning

confidence: 88%

“…Similarly, Campos et al . () reported a higher proteolytic activity of cardoon crude extract and a less milk‐clotting activity than calf rennet. According to Roseiro et al .…”

Section: Resultsmentioning

confidence: 96%

See 1 more Smart Citation

Enzymatic extract from flowers of Algerian spontaneous Cynara cardunculus: Milk‐clotting properties and use in the manufacture of a Camembert‐type cheese

Zikiou

Zidoune

2018

Int J of Dairy Tech

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“…mol -1 ; that enzyme was found to induce milk coagulation through cleavage of the Phe 105 -Met 106 bond in bovine κ-casein [20]. This enzyme preparation was further shown to be heterogeneous in that three active proteinases (initially referred to as cynarases or cyprosins 1, 2 and 3) could be isolated, purified and partly characterised in terms of activity [6,13,19,27]. Those proteinases were reported to have a pH optimum of 5.1 and they were classified as aspartic proteinases [27].…”

Section: Purification Of Proteinasesmentioning

confidence: 99%

Advances in the role of a plant coagulant (Cynara cardunculus) in vitro and during ripening of cheeses from several milk species

Sousa

Malcata

2002

Lait

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-Extracts from dried flowers of Cynara cardunculus have been employed successfully for many centuries in Portugal and some regions of Spain for the manufacture of traditional cheeses. Several studies have been performed in vitro and in actual cheeses focusing on the activity and specificity of proteinases from C. cardunculus, in attempts to further characterise this plant coagulant as a proteolytic agent in cheese ripening. In vitro studies encompassed extraction conditions, storage of extracts, proteolysis and specificity on caseins using experimental conditions that parallel milk and cheese during ripening. In vivo studies encompassed the effect of the type of milk (bovine, ovine and caprine) in terms of proteolysis, specificity of those plant proteinases during ripening, comparison of microbiological, chemical, proteolytic and lipolytic characteristics in ovine milk cheeses relative to animal rennet counterparts, and effect of native microflora, thermal processing and addition of starter cultures in ovine cheeses. milk clotting enzyme / plant coagulant / cheese / ewe's milk / cow's milk / goat's milk / ripeningResumé -Rôle de l'extrait coagulant de chardon (Cynara cardunculus) in vitro et au cours de l'affinage de fromages fabriqués à partir de laits de plusieurs espèces. L'extrait de fleurs séchées de Cynara cardunculus a été employé avec succès depuis plusieurs siècles au Portugal et dans quelques régions d'Espagne pour la fabrication de fromages traditionnels. De nombreuses études ont été réalisées in vitro et en fabrication fromagère sur l'activité et la spécificité des protéases de C. cardunculus, dans le but de mieux caractériser ce coagulant végétal comme agent protéolytique dans l'affinage du fromage. Les études in vitro ont concerné les conditions d'extraction, la conservation des extraits, la protéolyse et la spécificité sur les caséines en utilisant des conditions expérimentales qui 151

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“…the violet part of the flower and have molecular masses about 49-50 kDa (Heimgartner et al 1990;Campos et al 1990). Cardosin A (Veríssimo et al 1995(Veríssimo et al , 1996, the most abundant of the cardosins, accumulates in the protein storage vacuoles of the stigmatic epidermal papillae and in the vacuoles of the epidermal cells in the stylus (Ramalho-Santos et al 1997).…”

Section: Enzymes From Extracts Of C Cardunculusmentioning

confidence: 99%

Native and Biotechnologically Engineered Plant Proteases with Industrial Applications

Feijoo-Siota

Villa

2010

Food Bioprocess Technol

128

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Proteases occupy the most relevant position among industrial enzymes. Plant proteases have been used in medicine, detergent manufacturing, and food science for many years, but their production is diminishing in favor of those of microbial origin because lower production costs. Papain, bromelain, and ficin are the most frequently employed plant proteases, although new proteases with new and more appealing physicochemical properties for industry are still emerging. DNA technology and genetic engineering shall play, without a doubt, an important role for the production of these proteases at the industrial level. The present review focuses on the applications of traditional plant proteases as well as new proteases discovered during the last 20 years, some of which have already been genetically engineered either to increase production or to strengthen some of their physicochemical properties. The review also refers to the protease classification, action pattern, and main characteristics.

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Chemical characterization of proteases extracted from wild thistle (Cynara cardunculus)

Cited by 43 publications

References 9 publications

Enzymatic extract from flowers of Algerian spontaneous Cynara cardunculus: Milk‐clotting properties and use in the manufacture of a Camembert‐type cheese

Enzymatic extract from flowers of Algerian spontaneous Cynara cardunculus: Milk‐clotting properties and use in the manufacture of a Camembert‐type cheese

Advances in the role of a plant coagulant (Cynara cardunculus) in vitro and during ripening of cheeses from several milk species

Native and Biotechnologically Engineered Plant Proteases with Industrial Applications

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