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

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 activit...

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Detalles Bibliográficos
Autores principales: Barberis, Sonia, Quiroga, Evelina, Morcelle del Valle, Susana Raquel, Priolo de Lufrano, Nora Silvia, Luco, Juan M.
Formato: Articulo
Lenguaje:Inglés
Publicado: 2006
Materias:
Ciencias Exactas
Phytoproteases; Papain; Funastrain; Araujiain; Aqueous-organic biphasic systems; LFERs
Biología
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/74526
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-74526
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Exactas
Phytoproteases; Papain; Funastrain; Araujiain; Aqueous-organic biphasic systems; LFERs
Biología
spellingShingle Ciencias Exactas
Phytoproteases; Papain; Funastrain; Araujiain; Aqueous-organic biphasic systems; LFERs
Biología
Barberis, Sonia
Quiroga, Evelina
Morcelle del Valle, Susana Raquel
Priolo de Lufrano, Nora Silvia
Luco, Juan M.
Study of phytoproteases stability in aqueous-organic biphasic systems using linear free energy relationships
topic_facet Ciencias Exactas
Phytoproteases; Papain; Funastrain; Araujiain; Aqueous-organic biphasic systems; LFERs
Biología
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.
format Articulo
Articulo
author Barberis, Sonia
Quiroga, Evelina
Morcelle del Valle, Susana Raquel
Priolo de Lufrano, Nora Silvia
Luco, Juan M.
author_facet Barberis, Sonia
Quiroga, Evelina
Morcelle del Valle, Susana Raquel
Priolo de Lufrano, Nora Silvia
Luco, Juan M.
author_sort Barberis, Sonia
title Study of phytoproteases stability in aqueous-organic biphasic systems using linear free energy relationships
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
publishDate 2006
url http://sedici.unlp.edu.ar/handle/10915/74526
work_keys_str_mv AT barberissonia studyofphytoproteasesstabilityinaqueousorganicbiphasicsystemsusinglinearfreeenergyrelationships
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AT priolodelufranonorasilvia studyofphytoproteasesstabilityinaqueousorganicbiphasicsystemsusinglinearfreeenergyrelationships
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bdutipo_str Repositorios
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