Artículo
Study of phytoproteases stability in aqueous-organic biphasic systems using linear free energy relationships
Barberis, Sonia Esther
; Quiroga, Evelina
; Morcelle del Valle, Susana Raquel
; Priolo, Nora Silvia; Luco, Juan Maria
Fecha de publicación:
02/2006
Editorial:
Elsevier Science
Revista:
Journal of Molecular Catalysis B: Enzymatic
ISSN:
1381-1177
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
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.
Archivos asociados
Licencia
Identificadores
Colecciones
Articulos(CCT - LA PLATA)
Articulos de CTRO.CIENTIFICO TECNOL.CONICET - LA PLATA
Articulos de CTRO.CIENTIFICO TECNOL.CONICET - LA PLATA
Articulos(CCT - SAN LUIS)
Articulos de CTRO.CIENTIFICO TECNOL.CONICET - SAN LUIS
Articulos de CTRO.CIENTIFICO TECNOL.CONICET - SAN LUIS
Articulos(INFAP)
Articulos de INST. DE FISICA APLICADA "DR. JORGE ANDRES ZGRABLICH"
Articulos de INST. DE FISICA APLICADA "DR. JORGE ANDRES ZGRABLICH"
Citación
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
Compartir
Altmétricas