Artículo
Peptide synthesis in aqueous-organic biphasic systems catalyzed by a protease isolated from Morrenia brachysthephana (Asclepiadaceae)
Fecha de publicación:
07/03/2002
Editorial:
Elsevier Science
Revista:
Journal of Molecular Catalysis B: Enzymatic
ISSN:
1381-1177
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
A new cysteine protease, morrenain b II, isolated from the latex of a South American climbing plant, Morrenia brachystephana Griseb. (Asclepiadaceae), was found to be stable in aqueous–organic biphasic systems. In this work, we have investigated the ability of morrenain b II to perform peptide synthesis using Phe.OMe and Asp as substrates; Cys as activator; 0.1 M Tris–HCl buffer pH 8.5 and chloroform as reaction media. The reaction products were separated by RP-HPLC and identified by TLC, H-NMR and EI-MS. Morrenain b II showed high specificity towards bonds between Cys and Phe.OMe amino acids. A significant amount of the cystine–Phe.OMe peptide was produced within 1 h. These preliminary results were compared with papain under the same conditions.
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Articulos(CCT - SAN LUIS)
Articulos de CTRO.CIENTIFICO TECNOL.CONICET - SAN LUIS
Articulos de CTRO.CIENTIFICO TECNOL.CONICET - SAN LUIS
Citación
Barberis, Sonia Esther; Quiroga, Evelina; Arribére, María Cecilia; Priolo, Nora Silvia; Peptide synthesis in aqueous-organic biphasic systems catalyzed by a protease isolated from Morrenia brachysthephana (Asclepiadaceae); Elsevier Science; Journal of Molecular Catalysis B: Enzymatic; 17; 1; 7-3-2002; 39-47
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