Behavior of Araujiain, a new cysteine phytoprotease, in organic media with low water content

In this paper we studied the effect of different organic solvents (1-octanol, trichloroethylene, ethanol, ethyl acetate, tetrahydrofuran, cyclohexane, propanone, acetonitrile, dichloromethane, chlorobenzene, N,N-dimethylformamide, acetophenone, diethyl ether, methanol, ethylene glycol and toluene) w...

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Autores principales: Quiroga,Evelina, Priolo,Nora, Marchese,José, Barberis,Sonia
Lenguaje:English
Publicado: Pontificia Universidad Católica de Valparaíso 2006
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Acceso en línea:http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582006000100004
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spelling oai:scielo:S0717-345820060001000042006-05-11Behavior of Araujiain, a new cysteine phytoprotease, in organic media with low water contentQuiroga,EvelinaPriolo,NoraMarchese,JoséBarberis,Sonia Araujia hortorum Fourn organic solvents plant protease substrate preferences thermostability In this paper we studied the effect of different organic solvents (1-octanol, trichloroethylene, ethanol, ethyl acetate, tetrahydrofuran, cyclohexane, propanone, acetonitrile, dichloromethane, chlorobenzene, N,N-dimethylformamide, 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.info:eu-repo/semantics/openAccessPontificia Universidad Católica de ValparaísoElectronic Journal of Biotechnology v.9 n.1 20062006-01-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582006000100004en
institution Scielo Chile
collection Scielo Chile
language English
topic Araujia hortorum Fourn
organic solvents
plant protease
substrate preferences
thermostability
spellingShingle Araujia hortorum Fourn
organic solvents
plant protease
substrate preferences
thermostability
Quiroga,Evelina
Priolo,Nora
Marchese,José
Barberis,Sonia
Behavior of Araujiain, a new cysteine phytoprotease, in organic media with low water content
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,N-dimethylformamide, 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.
author Quiroga,Evelina
Priolo,Nora
Marchese,José
Barberis,Sonia
author_facet Quiroga,Evelina
Priolo,Nora
Marchese,José
Barberis,Sonia
author_sort Quiroga,Evelina
title Behavior of Araujiain, a new cysteine phytoprotease, in organic media with low water content
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
publisher Pontificia Universidad Católica de Valparaíso
publishDate 2006
url http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582006000100004
work_keys_str_mv AT quirogaevelina behaviorofaraujiainanewcysteinephytoproteaseinorganicmediawithlowwatercontent
AT priolonora behaviorofaraujiainanewcysteinephytoproteaseinorganicmediawithlowwatercontent
AT marchesejose behaviorofaraujiainanewcysteinephytoproteaseinorganicmediawithlowwatercontent
AT barberissonia behaviorofaraujiainanewcysteinephytoproteaseinorganicmediawithlowwatercontent
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