Comparative behaviour of proteinases from the latex of Carica papaya and Funastrum clausum as catalysts for the synthesis of Z-Ala-Phe-OMe

The proteolytic extract obtained from the latex of Funastrum clausum (Jacq.) Schlechter (Asclepiadaceae), a South American climbing plant, was assayed as a novel catalyst for peptide synthesis and compared with commercial papain under the same conditions. After immobilization on polyamide, the synth...

Descripción completa

Detalles Bibliográficos
Autores principales: Morcelle del Valle, Susana Raquel, Barberis, Sonia, Priolo de Lufrano, Nora Silvia, Caffini, Néstor Oscar, Clapés, Pere
Formato: Articulo
Lenguaje:Inglés
Publicado: 2006
Materias:
Biología
Protease catalysis
Funastrain
Papain
Peptide synthesis
Oligopeptides
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/153057
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-153057
record_format dspace
spelling I19-R120-10915-1530572023-05-17T04:05:59Z http://sedici.unlp.edu.ar/handle/10915/153057 issn:1381-1177 Comparative behaviour of proteinases from the latex of Carica papaya and Funastrum clausum as catalysts for the synthesis of Z-Ala-Phe-OMe Morcelle del Valle, Susana Raquel Barberis, Sonia Priolo de Lufrano, Nora Silvia Caffini, Néstor Oscar Clapés, Pere 2006 2023-05-16T13:57:50Z en Biología Protease catalysis Funastrain Papain Peptide synthesis Oligopeptides The proteolytic extract obtained from the latex of Funastrum clausum (Jacq.) Schlechter (Asclepiadaceae), a South American climbing plant, was assayed as a novel catalyst for peptide synthesis and compared with commercial papain under the same conditions. After immobilization on polyamide, the synthesis of the bitter peptide precursor Z-Ala-Phe-OMe was performed and different conditions were tried. Acetonitrile and ethyl acetate with low water content were tested as organic solvents. Equilibrium- and kinetically-controlled synthesis were tried by using either Z-Ala-OH or Z-Ala-OMe as acyl donors, respectively. The best conditions for the synthesis of the desired product varied according to the catalyst used. For papain, thermodynamic control in acetonitrile (aw ∼= 0.12) in the presence of triethylamine (TEA) or boric acid–borate buffer (40 mM), and equilibrium- and kinetic-controlled synthesis in ethyl acetate (aw ∼= 0.75) proved to be the best conditions. The thermodynamic control in either acetonitrile with aw ∼= 0.12 (40mM TEA or Na₂CO₃) or ethyl acetate (aw ∼= 0.75) were the best conditions found for funastrain. In all cases, the formation of oligopeptides up to three Phe was observed. The proteolytic extract of F. clausum latex showed more selectivity than papain towards the conversion to Z-Ala-Phe-OMe leading to less proportion of oligopeptides. Centro de Investigación de Proteínas Vegetales Articulo Articulo http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) application/pdf 117-124
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Biología
Protease catalysis
Funastrain
Papain
Peptide synthesis
Oligopeptides
spellingShingle Biología
Protease catalysis
Funastrain
Papain
Peptide synthesis
Oligopeptides
Morcelle del Valle, Susana Raquel
Barberis, Sonia
Priolo de Lufrano, Nora Silvia
Caffini, Néstor Oscar
Clapés, Pere
Comparative behaviour of proteinases from the latex of Carica papaya and Funastrum clausum as catalysts for the synthesis of Z-Ala-Phe-OMe
topic_facet Biología
Protease catalysis
Funastrain
Papain
Peptide synthesis
Oligopeptides
description The proteolytic extract obtained from the latex of Funastrum clausum (Jacq.) Schlechter (Asclepiadaceae), a South American climbing plant, was assayed as a novel catalyst for peptide synthesis and compared with commercial papain under the same conditions. After immobilization on polyamide, the synthesis of the bitter peptide precursor Z-Ala-Phe-OMe was performed and different conditions were tried. Acetonitrile and ethyl acetate with low water content were tested as organic solvents. Equilibrium- and kinetically-controlled synthesis were tried by using either Z-Ala-OH or Z-Ala-OMe as acyl donors, respectively. The best conditions for the synthesis of the desired product varied according to the catalyst used. For papain, thermodynamic control in acetonitrile (aw ∼= 0.12) in the presence of triethylamine (TEA) or boric acid–borate buffer (40 mM), and equilibrium- and kinetic-controlled synthesis in ethyl acetate (aw ∼= 0.75) proved to be the best conditions. The thermodynamic control in either acetonitrile with aw ∼= 0.12 (40mM TEA or Na₂CO₃) or ethyl acetate (aw ∼= 0.75) were the best conditions found for funastrain. In all cases, the formation of oligopeptides up to three Phe was observed. The proteolytic extract of F. clausum latex showed more selectivity than papain towards the conversion to Z-Ala-Phe-OMe leading to less proportion of oligopeptides.
format Articulo
Articulo
author Morcelle del Valle, Susana Raquel
Barberis, Sonia
Priolo de Lufrano, Nora Silvia
Caffini, Néstor Oscar
Clapés, Pere
author_facet Morcelle del Valle, Susana Raquel
Barberis, Sonia
Priolo de Lufrano, Nora Silvia
Caffini, Néstor Oscar
Clapés, Pere
author_sort Morcelle del Valle, Susana Raquel
title Comparative behaviour of proteinases from the latex of Carica papaya and Funastrum clausum as catalysts for the synthesis of Z-Ala-Phe-OMe
title_short Comparative behaviour of proteinases from the latex of Carica papaya and Funastrum clausum as catalysts for the synthesis of Z-Ala-Phe-OMe
title_full Comparative behaviour of proteinases from the latex of Carica papaya and Funastrum clausum as catalysts for the synthesis of Z-Ala-Phe-OMe
title_fullStr Comparative behaviour of proteinases from the latex of Carica papaya and Funastrum clausum as catalysts for the synthesis of Z-Ala-Phe-OMe
title_full_unstemmed Comparative behaviour of proteinases from the latex of Carica papaya and Funastrum clausum as catalysts for the synthesis of Z-Ala-Phe-OMe
title_sort comparative behaviour of proteinases from the latex of carica papaya and funastrum clausum as catalysts for the synthesis of z-ala-phe-ome
publishDate 2006
url http://sedici.unlp.edu.ar/handle/10915/153057
work_keys_str_mv AT morcelledelvallesusanaraquel comparativebehaviourofproteinasesfromthelatexofcaricapapayaandfunastrumclausumascatalystsforthesynthesisofzalapheome
AT barberissonia comparativebehaviourofproteinasesfromthelatexofcaricapapayaandfunastrumclausumascatalystsforthesynthesisofzalapheome
AT priolodelufranonorasilvia comparativebehaviourofproteinasesfromthelatexofcaricapapayaandfunastrumclausumascatalystsforthesynthesisofzalapheome
AT caffininestoroscar comparativebehaviourofproteinasesfromthelatexofcaricapapayaandfunastrumclausumascatalystsforthesynthesisofzalapheome
AT clapespere comparativebehaviourofproteinasesfromthelatexofcaricapapayaandfunastrumclausumascatalystsforthesynthesisofzalapheome
_version_ 1766370239774195712

Ejemplares similares