Please use this identifier to cite or link to this item: http://hdl.handle.net/10316/3904
Title: Cardosins A and B, two new enzymes available for peptide synthesis
Authors: Sarmento, Ana Cristina 
Silvestre, Liliana 
Barros, Marlene 
Pires, Euclides 
Keywords: Aspartic proteases; Specificity; Organic solvents
Issue Date: 1998
Citation: Journal of Molecular Catalysis B: Enzymatic. 5:1-4 (1998) 327-330
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. Veríssimo, C. Faro, A.J.G. Moir, Y. Lin, J. Tang, E. Pires, Eur. J. Biochem., 235 (1996) 762.]. Cardosins were shown to be stable in aqueous-organic biphasic systems [M. Barros, M.G.V. Carvalho, F.A. Garcia, E. Pires, Biotech. Lett. 14 (1992) 174.]. In this work, we have investigated peptide bond specificity of Cardosin A and Cardosin B in what concerns the amino acids in P'1 position. The results were compared with pepsin under the same conditions. Information about secondary specificity of Cardosin A and B was also investigated by tripeptide synthesis. The condensation reactions were carried out in aqueous-organic biphasic systems of n-hexane/ethyl acetate and sodium phosphate buffer. The reaction products were isolated by RP-HPLC and identified by amino acid analysis and eventually by M.S. The results in the synthesis of dipeptides showed that Cardosin A and B have similar P'1 position preference. The production of tripeptides by condensation of CBZ·Val·Phe with Phe·OMe, Met·OMe and Val·OMe reveals that the addition of Val in the P2 position modifies the Cardosins' preferences concerning the amino acid in P'1 position.
URI: http://hdl.handle.net/10316/3904
DOI: 10.1016/S1381-1177(98)00066-6
Rights: openAccess
Appears in Collections:FCTUC Ciências da Vida - Artigos em Revistas Internacionais

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