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Biotechnology Letters

, Volume 17, Issue 6, pp 621–626 | Cite as

The vegetable rennet of Cynara cardunculus L. contains two proteinases with chymosin and pepsin-like specificities

  • Paula Veríssimo
  • Cristina Esteves
  • Carlos Faro
  • Euclides Pires
Article

Abstract

The flowers of cardoon (genus Cynara) are traditionally used in Portugal for cheese making. In this work the vegetable rennet of the species Cynara cardunculus L. was characterized in terms of enzymic composition and proteolytic specificity of its proteinases (cardosin A and cardosin B). Cardosin A was found to cleave insulin B chain at the bonds Leu15-Tyr16, Leu17-Val18 and Phe25-Tyr26. In addition to the bonds mentioned cardosin B cleaves also Glu13-Ala14, Ala14-Leu15 and Phe24-Phe25 indicating that it has a broader specificity. The kinetic parameters for the hydrolysis of the synthetic peptide Leu-Ser-Phe(NO2)-Nle-Ala-Leu-oMe were also determined and compared to those of chymosin and pepsin. The results obtained indicate that in terms of specificity and kinetic parameters cardosin A is similar to chymosin whereas cardosin B is similar to pepsin. It appears therefore that the enzyme composition of cardoon rennet closely resembles that of calf rennet.

Keywords

Enzyme Peptide Hydrolysis Organic Chemistry Kinetic Parameter 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Chapman & Hall 1995

Authors and Affiliations

  • Paula Veríssimo
    • 1
  • Cristina Esteves
    • 1
  • Carlos Faro
    • 1
  • Euclides Pires
    • 1
  1. 1.Departamento Bioquímica, Faculdade de Ciências e TecnologiaUniversidade de CoimbraCoimbraPortugal

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