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
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/108593
Ver los metadatos del registro completo
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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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http://sedici.unlp.edu.ar/handle/10915/108593 |
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