Stability of antiacanthain in aqueous - organic biphasic systems

Autores
Bersi, Grisel; Vallés, Diego; Cantera, Ana; Barberis, Sonia Esther
Año de publicación
2014
Idioma
español castellano
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
The use of organic solvents as reaction media for enzymatic reactions provides numerous industrially attractive advantages compared to traditional aqueous reaction systems. In organic media, the proteases synthesize peptide bonds due to the shift of the thermodynamic equilibria in favor of synthesis. The aim of this work was to study the stability of proteolytic enzyme of fruit of Bromelia antiacantha Bertol, (a plant that growns in Argentina) in biphasic organic media, for its application to the bioactive peptide synthesis. An experimental statistical design allowed to cluster different organic solvents, by its physical chemistry characteristics and to select one of each group. Antiacanthain stability in biphasic system (Tris-HCl (0.1M) pH 8- organic solvent) was assayed by means of incubation of pre-purified crude extract in the reaction mixture (30:70; 50:50 and 70:30) during 24h. Enzyme specific activity was determined using N-alpha-benzoyl-DL-arginine-p-nitroanilide (BApNA) as substrate. Antiacanthain in biphasic systems (aqueous-organic) at 50% showed increased stability than in buffer Tris-HCl (pH 8) (t1/2 = 8 h). In addition, initial activity and the profile stabilities of antiacanthain were activated for (50%) ethyl acetate and hexane; maintained for benzene, ethyl ether and dichloromethane (50%) and diminished for octane and chlorobenzene (50%), when they was compared whit buffer. Profiles stabilities of antiacanthain in biphasic aqueous-organic systems (30 and 70%) were maintained, except for chlorobenzene (70%).
Fil: Bersi, Grisel. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia. Laboratorio de Bromatología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina
Fil: Vallés, Diego. Universidad de la República. Facultad de Ciencias; Uruguay
Fil: Cantera, Ana. Universidad del Uruguay. Facultad de Ciencias; Uruguay
Fil: Barberis, Sonia Esther. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia. Laboratorio de Bromatología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina
XXXII Reunión Científica Anual de la Sociedad de Biología de Cuyo
Estancia Grande
Argentina
Sociedad de Biología de Cuyo
Materia
ENZYME STABILITY
AQUEOUS ORGANIC MEDIA
ANTIACANTHAIN
BYPHASIC SYSTEMS
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:11336/287728
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/287728
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Stability of antiacanthain in aqueous - organic biphasic systemsBersi, GriselVallés, DiegoCantera, AnaBarberis, Sonia EstherENZYME STABILITYAQUEOUS ORGANIC MEDIAANTIACANTHAINBYPHASIC SYSTEMShttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2The use of organic solvents as reaction media for enzymatic reactions provides numerous industrially attractive advantages compared to traditional aqueous reaction systems. In organic media, the proteases synthesize peptide bonds due to the shift of the thermodynamic equilibria in favor of synthesis. The aim of this work was to study the stability of proteolytic enzyme of fruit of Bromelia antiacantha Bertol, (a plant that growns in Argentina) in biphasic organic media, for its application to the bioactive peptide synthesis. An experimental statistical design allowed to cluster different organic solvents, by its physical chemistry characteristics and to select one of each group. Antiacanthain stability in biphasic system (Tris-HCl (0.1M) pH 8- organic solvent) was assayed by means of incubation of pre-purified crude extract in the reaction mixture (30:70; 50:50 and 70:30) during 24h. Enzyme specific activity was determined using N-alpha-benzoyl-DL-arginine-p-nitroanilide (BApNA) as substrate. Antiacanthain in biphasic systems (aqueous-organic) at 50% showed increased stability than in buffer Tris-HCl (pH 8) (t1/2 = 8 h). In addition, initial activity and the profile stabilities of antiacanthain were activated for (50%) ethyl acetate and hexane; maintained for benzene, ethyl ether and dichloromethane (50%) and diminished for octane and chlorobenzene (50%), when they was compared whit buffer. Profiles stabilities of antiacanthain in biphasic aqueous-organic systems (30 and 70%) were maintained, except for chlorobenzene (70%).Fil: Bersi, Grisel. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia. Laboratorio de Bromatología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; ArgentinaFil: Vallés, Diego. Universidad de la República. Facultad de Ciencias; UruguayFil: Cantera, Ana. Universidad del Uruguay. Facultad de Ciencias; UruguayFil: Barberis, Sonia Esther. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia. Laboratorio de Bromatología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; ArgentinaXXXII Reunión Científica Anual de la Sociedad de Biología de CuyoEstancia GrandeArgentinaSociedad de Biología de CuyoSociedad de Biología de Cuyo2014info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectCongresoBookhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/287728Stability of antiacanthain in aqueous - organic biphasic systems; XXXII Reunión Científica Anual de la Sociedad de Biología de Cuyo; Estancia Grande; Argentina; 2014; 1-7CONICET DigitalCONICETspainfo:eu-repo/semantics/altIdentifier/url/https://sbcuyo.org.ar/wp-content/uploads/2017/05/SBdeCuyo-2014.pdfNacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2026-06-17T09:42:10Zoai:ri.conicet.gov.ar:11336/287728instacron: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:34982026-06-17 09:42:11.199CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Stability of antiacanthain in aqueous - organic biphasic systems
title Stability of antiacanthain in aqueous - organic biphasic systems
spellingShingle Stability of antiacanthain in aqueous - organic biphasic systems
Bersi, Grisel
ENZYME STABILITY
AQUEOUS ORGANIC MEDIA
ANTIACANTHAIN
BYPHASIC SYSTEMS
title_short Stability of antiacanthain in aqueous - organic biphasic systems
title_full Stability of antiacanthain in aqueous - organic biphasic systems
title_fullStr Stability of antiacanthain in aqueous - organic biphasic systems
title_full_unstemmed Stability of antiacanthain in aqueous - organic biphasic systems
title_sort Stability of antiacanthain in aqueous - organic biphasic systems
dc.creator.none.fl_str_mv Bersi, Grisel
Vallés, Diego
Cantera, Ana
Barberis, Sonia Esther
author Bersi, Grisel
author_facet Bersi, Grisel
Vallés, Diego
Cantera, Ana
Barberis, Sonia Esther
author_role author
author2 Vallés, Diego
Cantera, Ana
Barberis, Sonia Esther
author2_role author
author
author
dc.subject.none.fl_str_mv ENZYME STABILITY
AQUEOUS ORGANIC MEDIA
ANTIACANTHAIN
BYPHASIC SYSTEMS
topic ENZYME STABILITY
AQUEOUS ORGANIC MEDIA
ANTIACANTHAIN
BYPHASIC SYSTEMS
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv The use of organic solvents as reaction media for enzymatic reactions provides numerous industrially attractive advantages compared to traditional aqueous reaction systems. In organic media, the proteases synthesize peptide bonds due to the shift of the thermodynamic equilibria in favor of synthesis. The aim of this work was to study the stability of proteolytic enzyme of fruit of Bromelia antiacantha Bertol, (a plant that growns in Argentina) in biphasic organic media, for its application to the bioactive peptide synthesis. An experimental statistical design allowed to cluster different organic solvents, by its physical chemistry characteristics and to select one of each group. Antiacanthain stability in biphasic system (Tris-HCl (0.1M) pH 8- organic solvent) was assayed by means of incubation of pre-purified crude extract in the reaction mixture (30:70; 50:50 and 70:30) during 24h. Enzyme specific activity was determined using N-alpha-benzoyl-DL-arginine-p-nitroanilide (BApNA) as substrate. Antiacanthain in biphasic systems (aqueous-organic) at 50% showed increased stability than in buffer Tris-HCl (pH 8) (t1/2 = 8 h). In addition, initial activity and the profile stabilities of antiacanthain were activated for (50%) ethyl acetate and hexane; maintained for benzene, ethyl ether and dichloromethane (50%) and diminished for octane and chlorobenzene (50%), when they was compared whit buffer. Profiles stabilities of antiacanthain in biphasic aqueous-organic systems (30 and 70%) were maintained, except for chlorobenzene (70%).
Fil: Bersi, Grisel. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia. Laboratorio de Bromatología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina
Fil: Vallés, Diego. Universidad de la República. Facultad de Ciencias; Uruguay
Fil: Cantera, Ana. Universidad del Uruguay. Facultad de Ciencias; Uruguay
Fil: Barberis, Sonia Esther. Universidad Nacional de San Luis. Facultad de Química, Bioquímica y Farmacia. Departamento de Farmacia. Laboratorio de Bromatología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis; Argentina
XXXII Reunión Científica Anual de la Sociedad de Biología de Cuyo
Estancia Grande
Argentina
Sociedad de Biología de Cuyo
description The use of organic solvents as reaction media for enzymatic reactions provides numerous industrially attractive advantages compared to traditional aqueous reaction systems. In organic media, the proteases synthesize peptide bonds due to the shift of the thermodynamic equilibria in favor of synthesis. The aim of this work was to study the stability of proteolytic enzyme of fruit of Bromelia antiacantha Bertol, (a plant that growns in Argentina) in biphasic organic media, for its application to the bioactive peptide synthesis. An experimental statistical design allowed to cluster different organic solvents, by its physical chemistry characteristics and to select one of each group. Antiacanthain stability in biphasic system (Tris-HCl (0.1M) pH 8- organic solvent) was assayed by means of incubation of pre-purified crude extract in the reaction mixture (30:70; 50:50 and 70:30) during 24h. Enzyme specific activity was determined using N-alpha-benzoyl-DL-arginine-p-nitroanilide (BApNA) as substrate. Antiacanthain in biphasic systems (aqueous-organic) at 50% showed increased stability than in buffer Tris-HCl (pH 8) (t1/2 = 8 h). In addition, initial activity and the profile stabilities of antiacanthain were activated for (50%) ethyl acetate and hexane; maintained for benzene, ethyl ether and dichloromethane (50%) and diminished for octane and chlorobenzene (50%), when they was compared whit buffer. Profiles stabilities of antiacanthain in biphasic aqueous-organic systems (30 and 70%) were maintained, except for chlorobenzene (70%).
publishDate 2014
dc.date.none.fl_str_mv 2014
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/conferenceObject
Congreso
Book
http://purl.org/coar/resource_type/c_5794
info:ar-repo/semantics/documentoDeConferencia
status_str publishedVersion
format conferenceObject
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/287728
Stability of antiacanthain in aqueous - organic biphasic systems; XXXII Reunión Científica Anual de la Sociedad de Biología de Cuyo; Estancia Grande; Argentina; 2014; 1-7
CONICET Digital
CONICET
url http://hdl.handle.net/11336/287728
identifier_str_mv Stability of antiacanthain in aqueous - organic biphasic systems; XXXII Reunión Científica Anual de la Sociedad de Biología de Cuyo; Estancia Grande; Argentina; 2014; 1-7
CONICET Digital
CONICET
dc.language.none.fl_str_mv spa
language spa
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://sbcuyo.org.ar/wp-content/uploads/2017/05/SBdeCuyo-2014.pdf
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
dc.coverage.none.fl_str_mv Nacional
dc.publisher.none.fl_str_mv Sociedad de Biología de Cuyo
publisher.none.fl_str_mv Sociedad de Biología de Cuyo
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 13.040872

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