Study of phytoproteases stability in aqueous-organic biphasic systems using linear free energy relationships

Autores
Barberis, Sonia Esther; Quiroga, Evelina; Morcelle del Valle, Susana Raquel; Priolo, Nora Silvia; Luco, Juan Maria
Año de publicación
2006
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In this paper we study the effect of different water-immiscible organic solvents (benzene, toluene, 1-butanol, 1-octanol, dichloroethane, dichloromethane, diethyl ether, hexane, chlorobenzene, acetophenone, n-dodecane, trichloroethylene, ethyl acetate) on the stability (residual caseinolytic activity after 4h) of soluble phytoproteases, such as araujiain, funastrain and papain in aqueous-organic biphasic systems. Besides, the effect of organic solvents on enzymatic catalysis was quantitatively studied by means of linear free energy relationships (LFERs). The organic solvents werecharacterized byseveral physicochemicalproperties, and multiple linear regression analysis (MLRA)togetherwithnon-linearregression were the methods used to search the relationships between the residual caseinolytic activity data and several physicochemical parameters. Those enzymes show much greater activity and stability in some biphasic media than in water. On the other hand, all developed correlations represented highly significant LFERs models and showed that non-specific polar and hydrophobic factors are of prime and approximately equal importance for the biocatalytic activity of araujiain, funastrain and papain in the studied biphasic systems, while the specific polar interactions are of little importance for activity. The results suggested that araujiain, funastrain and papain do not suffer unfolding in the studied biphasic media and they are able to retain their native or native-like configurations, though with altered characteristics or properties. This fact was demonstrated by means of a comparative FTIR spectroscopy study in both, buffer and biphasic media, for each studied enzyme.
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
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: Morcelle del Valle, Susana Raquel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; 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: Luco, Juan Maria. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Química; Argentina
Materia
AQUEOUS-ORGANIC BIPHASIC SYSTEMS
ARAUJIAIN
FUNASTRAIN
LFERS
PAPAIN
PHYTOPROTEASES
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:11336/159729
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/159729
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Study of phytoproteases stability in aqueous-organic biphasic systems using linear free energy relationshipsBarberis, Sonia EstherQuiroga, EvelinaMorcelle del Valle, Susana RaquelPriolo, Nora SilviaLuco, Juan MariaAQUEOUS-ORGANIC BIPHASIC SYSTEMSARAUJIAINFUNASTRAINLFERSPAPAINPHYTOPROTEASEShttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2In this paper we study the effect of different water-immiscible organic solvents (benzene, toluene, 1-butanol, 1-octanol, dichloroethane, dichloromethane, diethyl ether, hexane, chlorobenzene, acetophenone, n-dodecane, trichloroethylene, ethyl acetate) on the stability (residual caseinolytic activity after 4h) of soluble phytoproteases, such as araujiain, funastrain and papain in aqueous-organic biphasic systems. Besides, the effect of organic solvents on enzymatic catalysis was quantitatively studied by means of linear free energy relationships (LFERs). The organic solvents werecharacterized byseveral physicochemicalproperties, and multiple linear regression analysis (MLRA)togetherwithnon-linearregression were the methods used to search the relationships between the residual caseinolytic activity data and several physicochemical parameters. Those enzymes show much greater activity and stability in some biphasic media than in water. On the other hand, all developed correlations represented highly significant LFERs models and showed that non-specific polar and hydrophobic factors are of prime and approximately equal importance for the biocatalytic activity of araujiain, funastrain and papain in the studied biphasic systems, while the specific polar interactions are of little importance for activity. The results suggested that araujiain, funastrain and papain do not suffer unfolding in the studied biphasic media and they are able to retain their native or native-like configurations, though with altered characteristics or properties. This fact was demonstrated by means of a comparative FTIR spectroscopy study in both, buffer and biphasic media, for each studied enzyme.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; ArgentinaFil: 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: Morcelle del Valle, Susana Raquel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; ArgentinaFil: Priolo, Nora Silvia. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; ArgentinaFil: Luco, Juan Maria. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Química; ArgentinaElsevier Science2006-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/159729Barberis, Sonia Esther; Quiroga, Evelina; Morcelle del Valle, Susana Raquel; Priolo, Nora Silvia; Luco, Juan Maria; Study of phytoproteases stability in aqueous-organic biphasic systems using linear free energy relationships; Elsevier Science; Journal of Molecular Catalysis B: Enzymatic; 38; 2; 2-2006; 95-1031381-1177CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S1381117705002018info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2005.11.011info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:22:58Zoai:ri.conicet.gov.ar:11336/159729instacron: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 10:22:58.399CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Study of phytoproteases stability in aqueous-organic biphasic systems using linear free energy relationships
title Study of phytoproteases stability in aqueous-organic biphasic systems using linear free energy relationships
spellingShingle Study of phytoproteases stability in aqueous-organic biphasic systems using linear free energy relationships
Barberis, Sonia Esther
AQUEOUS-ORGANIC BIPHASIC SYSTEMS
ARAUJIAIN
FUNASTRAIN
LFERS
PAPAIN
PHYTOPROTEASES
title_short Study of phytoproteases stability in aqueous-organic biphasic systems using linear free energy relationships
title_full Study of phytoproteases stability in aqueous-organic biphasic systems using linear free energy relationships
title_fullStr Study of phytoproteases stability in aqueous-organic biphasic systems using linear free energy relationships
title_full_unstemmed Study of phytoproteases stability in aqueous-organic biphasic systems using linear free energy relationships
title_sort Study of phytoproteases stability in aqueous-organic biphasic systems using linear free energy relationships
dc.creator.none.fl_str_mv Barberis, Sonia Esther
Quiroga, Evelina
Morcelle del Valle, Susana Raquel
Priolo, Nora Silvia
Luco, Juan Maria
author Barberis, Sonia Esther
author_facet Barberis, Sonia Esther
Quiroga, Evelina
Morcelle del Valle, Susana Raquel
Priolo, Nora Silvia
Luco, Juan Maria
author_role author
author2 Quiroga, Evelina
Morcelle del Valle, Susana Raquel
Priolo, Nora Silvia
Luco, Juan Maria
author2_role author
author
author
author
dc.subject.none.fl_str_mv AQUEOUS-ORGANIC BIPHASIC SYSTEMS
ARAUJIAIN
FUNASTRAIN
LFERS
PAPAIN
PHYTOPROTEASES
topic AQUEOUS-ORGANIC BIPHASIC SYSTEMS
ARAUJIAIN
FUNASTRAIN
LFERS
PAPAIN
PHYTOPROTEASES
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv In this paper we study the effect of different water-immiscible organic solvents (benzene, toluene, 1-butanol, 1-octanol, dichloroethane, dichloromethane, diethyl ether, hexane, chlorobenzene, acetophenone, n-dodecane, trichloroethylene, ethyl acetate) on the stability (residual caseinolytic activity after 4h) of soluble phytoproteases, such as araujiain, funastrain and papain in aqueous-organic biphasic systems. Besides, the effect of organic solvents on enzymatic catalysis was quantitatively studied by means of linear free energy relationships (LFERs). The organic solvents werecharacterized byseveral physicochemicalproperties, and multiple linear regression analysis (MLRA)togetherwithnon-linearregression were the methods used to search the relationships between the residual caseinolytic activity data and several physicochemical parameters. Those enzymes show much greater activity and stability in some biphasic media than in water. On the other hand, all developed correlations represented highly significant LFERs models and showed that non-specific polar and hydrophobic factors are of prime and approximately equal importance for the biocatalytic activity of araujiain, funastrain and papain in the studied biphasic systems, while the specific polar interactions are of little importance for activity. The results suggested that araujiain, funastrain and papain do not suffer unfolding in the studied biphasic media and they are able to retain their native or native-like configurations, though with altered characteristics or properties. This fact was demonstrated by means of a comparative FTIR spectroscopy study in both, buffer and biphasic media, for each studied enzyme.
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
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: Morcelle del Valle, Susana Raquel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Laboratorio de Investigación de Proteínas Vegetales; 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: Luco, Juan Maria. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Química; Argentina
description In this paper we study the effect of different water-immiscible organic solvents (benzene, toluene, 1-butanol, 1-octanol, dichloroethane, dichloromethane, diethyl ether, hexane, chlorobenzene, acetophenone, n-dodecane, trichloroethylene, ethyl acetate) on the stability (residual caseinolytic activity after 4h) of soluble phytoproteases, such as araujiain, funastrain and papain in aqueous-organic biphasic systems. Besides, the effect of organic solvents on enzymatic catalysis was quantitatively studied by means of linear free energy relationships (LFERs). The organic solvents werecharacterized byseveral physicochemicalproperties, and multiple linear regression analysis (MLRA)togetherwithnon-linearregression were the methods used to search the relationships between the residual caseinolytic activity data and several physicochemical parameters. Those enzymes show much greater activity and stability in some biphasic media than in water. On the other hand, all developed correlations represented highly significant LFERs models and showed that non-specific polar and hydrophobic factors are of prime and approximately equal importance for the biocatalytic activity of araujiain, funastrain and papain in the studied biphasic systems, while the specific polar interactions are of little importance for activity. The results suggested that araujiain, funastrain and papain do not suffer unfolding in the studied biphasic media and they are able to retain their native or native-like configurations, though with altered characteristics or properties. This fact was demonstrated by means of a comparative FTIR spectroscopy study in both, buffer and biphasic media, for each studied enzyme.
publishDate 2006
dc.date.none.fl_str_mv 2006-02
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/11336/159729
Barberis, Sonia Esther; Quiroga, Evelina; Morcelle del Valle, Susana Raquel; Priolo, Nora Silvia; Luco, Juan Maria; Study of phytoproteases stability in aqueous-organic biphasic systems using linear free energy relationships; Elsevier Science; Journal of Molecular Catalysis B: Enzymatic; 38; 2; 2-2006; 95-103
1381-1177
CONICET Digital
CONICET
url http://hdl.handle.net/11336/159729
identifier_str_mv Barberis, Sonia Esther; Quiroga, Evelina; Morcelle del Valle, Susana Raquel; Priolo, Nora Silvia; Luco, Juan Maria; Study of phytoproteases stability in aqueous-organic biphasic systems using linear free energy relationships; Elsevier Science; Journal of Molecular Catalysis B: Enzymatic; 38; 2; 2-2006; 95-103
1381-1177
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S1381117705002018
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2005.11.011
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
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
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
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score 13.070432

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