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

Autores
Barberis, Sonia; Quiroga, Evelina; Morcelle del Valle, Susana Raquel; Priolo de Lufrano, Nora Silvia; Luco, Juan M.
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 4 h) 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 were characterized by several physicochemical properties, and multiple linear regression analysis (MLRA) together with non-linear regression 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.
Facultad de Ciencias Exactas
Materia
Ciencias Exactas
Phytoproteases; Papain; Funastrain; Araujiain; Aqueous-organic biphasic systems; LFERs
Biología
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/74526
Acceder
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network_name_str SEDICI (UNLP)
spelling Study of phytoproteases stability in aqueous-organic biphasic systems using linear free energy relationshipsBarberis, SoniaQuiroga, EvelinaMorcelle del Valle, Susana RaquelPriolo de Lufrano, Nora SilviaLuco, Juan M.Ciencias ExactasPhytoproteases; Papain; Funastrain; Araujiain; Aqueous-organic biphasic systems; LFERsBiologíaIn 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 4 h) 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 were characterized by several physicochemical properties, and multiple linear regression analysis (MLRA) together with non-linear regression 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.Facultad de Ciencias Exactas2006info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf95-103http://sedici.unlp.edu.ar/handle/10915/74526enginfo:eu-repo/semantics/altIdentifier/issn/1381-1177info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2005.11.011info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:12:47Zoai:sedici.unlp.edu.ar:10915/74526Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:12:47.491SEDICI (UNLP) - Universidad Nacional de La Platafalse
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
Ciencias Exactas
Phytoproteases; Papain; Funastrain; Araujiain; Aqueous-organic biphasic systems; LFERs
Biología
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
Quiroga, Evelina
Morcelle del Valle, Susana Raquel
Priolo de Lufrano, Nora Silvia
Luco, Juan M.
author Barberis, Sonia
author_facet Barberis, Sonia
Quiroga, Evelina
Morcelle del Valle, Susana Raquel
Priolo de Lufrano, Nora Silvia
Luco, Juan M.
author_role author
author2 Quiroga, Evelina
Morcelle del Valle, Susana Raquel
Priolo de Lufrano, Nora Silvia
Luco, Juan M.
author2_role author
author
author
author
dc.subject.none.fl_str_mv Ciencias Exactas
Phytoproteases; Papain; Funastrain; Araujiain; Aqueous-organic biphasic systems; LFERs
Biología
topic Ciencias Exactas
Phytoproteases; Papain; Funastrain; Araujiain; Aqueous-organic biphasic systems; LFERs
Biología
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 4 h) 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 were characterized by several physicochemical properties, and multiple linear regression analysis (MLRA) together with non-linear regression 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.
Facultad de Ciencias Exactas
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 4 h) 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 were characterized by several physicochemical properties, and multiple linear regression analysis (MLRA) together with non-linear regression 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
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/74526
url http://sedici.unlp.edu.ar/handle/10915/74526
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/1381-1177
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.molcatb.2005.11.011
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
95-103
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instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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