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

Autores
Quiroga, Evelina; Priolo de Lufrano, Nora Silvia; Marchese, José; Barberis, Sonia
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,Ndimethylformamide, 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.
Centro de Investigación de Proteínas Vegetales
Materia
Química
Araujia hortorum Fourn
Organic solvents
Plant protease
Substrate preferences
Thermostability
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-nd/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/108593

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oai_identifier_str oai:sedici.unlp.edu.ar:10915/108593
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network_name_str SEDICI (UNLP)
spelling Behavior of Araujiain, a new cysteine phytoprotease, in organic media with low water contentQuiroga, EvelinaPriolo de Lufrano, Nora SilviaMarchese, JoséBarberis, SoniaQuímicaAraujia hortorum FournOrganic solventsPlant proteaseSubstrate preferencesThermostabilityIn this paper we studied the effect of different organic solvents (1-octanol, trichloroethylene, ethanol, ethyl acetate, tetrahydrofuran, cyclohexane, propanone, acetonitrile, dichloromethane, chlorobenzene, N,Ndimethylformamide, 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.Centro de Investigación de Proteínas Vegetales2006info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf18-25http://sedici.unlp.edu.ar/handle/10915/108593enginfo:eu-repo/semantics/altIdentifier/issn/0717-3458info:eu-repo/semantics/altIdentifier/doi/10.2225/vol9-issue1-fulltext-6info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-nd/4.0/Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:24:36Zoai:sedici.unlp.edu.ar:10915/108593Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:24:37.289SEDICI (UNLP) - Universidad Nacional de La Platafalse
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
Química
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 de Lufrano, Nora Silvia
Marchese, José
Barberis, Sonia
author Quiroga, Evelina
author_facet Quiroga, Evelina
Priolo de Lufrano, Nora Silvia
Marchese, José
Barberis, Sonia
author_role author
author2 Priolo de Lufrano, Nora Silvia
Marchese, José
Barberis, Sonia
author2_role author
author
author
dc.subject.none.fl_str_mv Química
Araujia hortorum Fourn
Organic solvents
Plant protease
Substrate preferences
Thermostability
topic Química
Araujia hortorum Fourn
Organic solvents
Plant protease
Substrate preferences
Thermostability
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,Ndimethylformamide, 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.
Centro de Investigación de Proteínas Vegetales
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,Ndimethylformamide, 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
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info:eu-repo/semantics/publishedVersion
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dc.language.none.fl_str_mv eng
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info:eu-repo/semantics/altIdentifier/doi/10.2225/vol9-issue1-fulltext-6
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-nd/4.0/
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-nd/4.0/
Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)
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