Behavior of Araujiain, a new cysteine phytoprotease, in organic media with low water content

Autores
Quiroga, Evelina; Priolo, Nora Silvia; Marchese, Jose; Barberis, Sonia Esther
Año de publicación
2006
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In this paper we studied the effect of different organic solvents (1-octanol, trichloroethylene, ethanol, ethyl acetate, tetrahydrofuran, cyclohexane, propanone, acetonitrile, dichloromethane, chlorobenzene, N,N-dimethylformamide, acetophenone, diethyl ether, methanol, ethylene glycol and toluene) with low and constant water content on substrate preferences, thermostability and stability (caseinolytic activity retention after 4 h) of proteases of Araujia hortorum Fourn. (Asclepiadaceae). The stability of araujiain was high in N,N-dimethylformamide and ethanol at 40ºC, but decreased at higher temperature. Araujiain substrates preferences in buffer Tris-HCl (pH 8), ethylene glycol and N,N-dimethylformamide exhibited different patterns, but the enzyme showed a high preference by glutamine derivative in all cases. According to FTIR spectroscopy studies, araujiain changed its secondary structure and as a consequence, it also changed its substrate preferences. This enzyme showed lower α-helical character and greater β-sheet folding in buffer than in organic media. A larger amount of antiparallel β-sheet residues indicates the formation of tighter intermolecular hydrogen bonds and enzymatic aggregates. These facts could explain the higher esterolytic activities, the greater stability and good hydrolytic potential of araujiain in some organic media such as N,N-dimethylformamide.
Fil: Quiroga, Evelina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia. Laboratorio de Bromatología; Argentina
Fil: Priolo, Nora Silvia. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Marchese, Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Ciencias Fisico Matematicas y Naturales. Departamento de Fisica. Laboratorio de Ciencias de Superficies y Medios Porosos; Argentina
Fil: Barberis, Sonia Esther. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia. Laboratorio de Bromatología; Argentina
Materia
Araujia hortorum Fourn
Organic solvents
Plant protease
Substrate preferences
Thermostability
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/158831
Acceder
id CONICETDig_b2c3d1f5ee810457fde516a995753dd1
oai_identifier_str oai:ri.conicet.gov.ar:11336/158831
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Behavior of Araujiain, a new cysteine phytoprotease, in organic media with low water contentQuiroga, EvelinaPriolo, Nora SilviaMarchese, JoseBarberis, Sonia EstherAraujia hortorum FournOrganic solventsPlant proteaseSubstrate preferencesThermostabilityhttps://purl.org/becyt/ford/2.4https://purl.org/becyt/ford/2In this paper we studied the effect of different organic solvents (1-octanol, trichloroethylene, ethanol, ethyl acetate, tetrahydrofuran, cyclohexane, propanone, acetonitrile, dichloromethane, chlorobenzene, N,N-dimethylformamide, acetophenone, diethyl ether, methanol, ethylene glycol and toluene) with low and constant water content on substrate preferences, thermostability and stability (caseinolytic activity retention after 4 h) of proteases of Araujia hortorum Fourn. (Asclepiadaceae). The stability of araujiain was high in N,N-dimethylformamide and ethanol at 40ºC, but decreased at higher temperature. Araujiain substrates preferences in buffer Tris-HCl (pH 8), ethylene glycol and N,N-dimethylformamide exhibited different patterns, but the enzyme showed a high preference by glutamine derivative in all cases. According to FTIR spectroscopy studies, araujiain changed its secondary structure and as a consequence, it also changed its substrate preferences. This enzyme showed lower α-helical character and greater β-sheet folding in buffer than in organic media. A larger amount of antiparallel β-sheet residues indicates the formation of tighter intermolecular hydrogen bonds and enzymatic aggregates. These facts could explain the higher esterolytic activities, the greater stability and good hydrolytic potential of araujiain in some organic media such as N,N-dimethylformamide.Fil: Quiroga, Evelina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia. Laboratorio de Bromatología; ArgentinaFil: Priolo, Nora Silvia. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; ArgentinaFil: Marchese, Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Ciencias Fisico Matematicas y Naturales. Departamento de Fisica. Laboratorio de Ciencias de Superficies y Medios Porosos; ArgentinaFil: Barberis, Sonia Esther. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia. Laboratorio de Bromatología; ArgentinaPontificia Universidad Católica de Valparaíso2006-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/158831Quiroga, Evelina; Priolo, Nora Silvia; Marchese, Jose; Barberis, Sonia Esther; Behavior of Araujiain, a new cysteine phytoprotease, in organic media with low water content; Pontificia Universidad Católica de Valparaíso; Electronic Journal of Biotechnology; 9; 1; 1-2006; 18-250717-3458CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.ejbiotechnology.info/content/vol9/issue1/full/6/index.htmlinfo:eu-repo/semantics/altIdentifier/doi/10.2225/vol9-issue1-fulltext-6info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:44:57Zoai:ri.conicet.gov.ar:11336/158831instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:44:58.057CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Behavior of Araujiain, a new cysteine phytoprotease, in organic media with low water content
title Behavior of Araujiain, a new cysteine phytoprotease, in organic media with low water content
spellingShingle Behavior of Araujiain, a new cysteine phytoprotease, in organic media with low water content
Quiroga, Evelina
Araujia hortorum Fourn
Organic solvents
Plant protease
Substrate preferences
Thermostability
title_short Behavior of Araujiain, a new cysteine phytoprotease, in organic media with low water content
title_full Behavior of Araujiain, a new cysteine phytoprotease, in organic media with low water content
title_fullStr Behavior of Araujiain, a new cysteine phytoprotease, in organic media with low water content
title_full_unstemmed Behavior of Araujiain, a new cysteine phytoprotease, in organic media with low water content
title_sort Behavior of Araujiain, a new cysteine phytoprotease, in organic media with low water content
dc.creator.none.fl_str_mv Quiroga, Evelina
Priolo, Nora Silvia
Marchese, Jose
Barberis, Sonia Esther
author Quiroga, Evelina
author_facet Quiroga, Evelina
Priolo, Nora Silvia
Marchese, Jose
Barberis, Sonia Esther
author_role author
author2 Priolo, Nora Silvia
Marchese, Jose
Barberis, Sonia Esther
author2_role author
author
author
dc.subject.none.fl_str_mv Araujia hortorum Fourn
Organic solvents
Plant protease
Substrate preferences
Thermostability
topic Araujia hortorum Fourn
Organic solvents
Plant protease
Substrate preferences
Thermostability
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.4
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv In this paper we studied the effect of different organic solvents (1-octanol, trichloroethylene, ethanol, ethyl acetate, tetrahydrofuran, cyclohexane, propanone, acetonitrile, dichloromethane, chlorobenzene, N,N-dimethylformamide, acetophenone, diethyl ether, methanol, ethylene glycol and toluene) with low and constant water content on substrate preferences, thermostability and stability (caseinolytic activity retention after 4 h) of proteases of Araujia hortorum Fourn. (Asclepiadaceae). The stability of araujiain was high in N,N-dimethylformamide and ethanol at 40ºC, but decreased at higher temperature. Araujiain substrates preferences in buffer Tris-HCl (pH 8), ethylene glycol and N,N-dimethylformamide exhibited different patterns, but the enzyme showed a high preference by glutamine derivative in all cases. According to FTIR spectroscopy studies, araujiain changed its secondary structure and as a consequence, it also changed its substrate preferences. This enzyme showed lower α-helical character and greater β-sheet folding in buffer than in organic media. A larger amount of antiparallel β-sheet residues indicates the formation of tighter intermolecular hydrogen bonds and enzymatic aggregates. These facts could explain the higher esterolytic activities, the greater stability and good hydrolytic potential of araujiain in some organic media such as N,N-dimethylformamide.
Fil: Quiroga, Evelina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia. Laboratorio de Bromatología; Argentina
Fil: Priolo, Nora Silvia. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; Argentina
Fil: Marchese, Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Ciencias Fisico Matematicas y Naturales. Departamento de Fisica. Laboratorio de Ciencias de Superficies y Medios Porosos; Argentina
Fil: Barberis, Sonia Esther. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia. Laboratorio de Bromatología; Argentina
description In this paper we studied the effect of different organic solvents (1-octanol, trichloroethylene, ethanol, ethyl acetate, tetrahydrofuran, cyclohexane, propanone, acetonitrile, dichloromethane, chlorobenzene, N,N-dimethylformamide, acetophenone, diethyl ether, methanol, ethylene glycol and toluene) with low and constant water content on substrate preferences, thermostability and stability (caseinolytic activity retention after 4 h) of proteases of Araujia hortorum Fourn. (Asclepiadaceae). The stability of araujiain was high in N,N-dimethylformamide and ethanol at 40ºC, but decreased at higher temperature. Araujiain substrates preferences in buffer Tris-HCl (pH 8), ethylene glycol and N,N-dimethylformamide exhibited different patterns, but the enzyme showed a high preference by glutamine derivative in all cases. According to FTIR spectroscopy studies, araujiain changed its secondary structure and as a consequence, it also changed its substrate preferences. This enzyme showed lower α-helical character and greater β-sheet folding in buffer than in organic media. A larger amount of antiparallel β-sheet residues indicates the formation of tighter intermolecular hydrogen bonds and enzymatic aggregates. These facts could explain the higher esterolytic activities, the greater stability and good hydrolytic potential of araujiain in some organic media such as N,N-dimethylformamide.
publishDate 2006
dc.date.none.fl_str_mv 2006-01
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/158831
Quiroga, Evelina; Priolo, Nora Silvia; Marchese, Jose; Barberis, Sonia Esther; Behavior of Araujiain, a new cysteine phytoprotease, in organic media with low water content; Pontificia Universidad Católica de Valparaíso; Electronic Journal of Biotechnology; 9; 1; 1-2006; 18-25
0717-3458
CONICET Digital
CONICET
url http://hdl.handle.net/11336/158831
identifier_str_mv Quiroga, Evelina; Priolo, Nora Silvia; Marchese, Jose; Barberis, Sonia Esther; Behavior of Araujiain, a new cysteine phytoprotease, in organic media with low water content; Pontificia Universidad Católica de Valparaíso; Electronic Journal of Biotechnology; 9; 1; 1-2006; 18-25
0717-3458
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.ejbiotechnology.info/content/vol9/issue1/full/6/index.html
info:eu-repo/semantics/altIdentifier/doi/10.2225/vol9-issue1-fulltext-6
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Pontificia Universidad Católica de Valparaíso
publisher.none.fl_str_mv Pontificia Universidad Católica de Valparaíso
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1844613415048314880
score 13.070432

Publicaciones similares