Aqueous micellar two phase systems as novel tools to recover pepsin like surubí proteases: effect of surfactants on enzyme activity

Autores
Acevedo Gomez, Antonella Valeria; Escobar, Guilermo; Gomez, Gabriela Noemi; Leiva, Laura Cristina Ana; Bustillo, Soledad; Nerli, Bibiana Beatriz
Año de publicación
2019
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
Surubí is farmed in the northeast of Argentina. It is of interest to valorize the current disposal of fish processing through the use of viscera waste, source of enzymes such as Pepsin. These enzymes have been recovered mainly using conventional methods (e.g.salting out, chromatography), however the use of liquid-liquid extraction using surfactants have not been fully explored. Aqueous micellar two-phase systems (AMTPS) are an extractive method based on the ability of some surfactants to form two immiscible aqueous phases, a rich and a poor micelle phases to recover the product of interest. Thus, the objective of this work was to firstly evaluate the stability of surubí crude extracts under different concentrations of Genapol (GX080) and Tergitol (Tg7) to estimate the feasibility of their use as potential micellar extractants of surubí pepsin. Enzymatic extracts (ERPi) were recovered from stomachs homogenates using salting-out procedure and pepsin activity was estimated by acid hemoglobin method. ERPi were first incubated with various concentrations of surfactants (1, 3 and 5% GX080/Tg7) in 100mM NaCit pH 5 for different times (0, 1, 2 and 3h) and then enzymatic activity was measured. Data represent the mean ± standard deviation (SD) of at least three replications. Statistical significance was tested by one-way ANOVA and Tukey (HSD) (p<0.05) Results showed that any surfactant concentration tested affected ERPi enzymatic activity moderately and this effect was dose dependent. ERPi retained 92, 65 and 60% of its initial activity when were incubated with 1, 3 and 5% of Tg7. After incubating with GX080 (1, 3 and 5%), the ERPi exhibited 80, 70 and 60% of its initial activity, respectively. The time variable in these assays had not significant influence on enzymatic activity decrease. Pepsin, a hydrophilic protein, is expected to be preferentially distributed into the aqueous phase of AMTPS.Considering that the surfactant concentration at this phase is always below 1%, the obtained results suggest that AMTPS formed with either GX080 or Tg7 could be viable tools in the primary recovery of pepsin-like proteases from fishing waste.
Fil: Acevedo Gomez, Antonella Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; Argentina
Fil: Escobar, Guilermo. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Departamento de Bioquímica. Laboratorio de Investigación en Proteínas; Argentina
Fil: Gomez, Gabriela Noemi. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; Argentina
Fil: Leiva, Laura Cristina Ana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; Argentina
Fil: Bustillo, Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; Argentina
Fil: Nerli, Bibiana Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Procesos Biotecnológicos y Químicos Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Procesos Biotecnológicos y Químicos Rosario; Argentina
Reunión Anual de Sociedades de Biociencia
Mar del Plata
Argentina
Sociedad Argentina de Farmacologia Experimental
Sociedad Argentina de Investigación Clínica
Sociedad Argentina de Biología
Sociedad Argentina de Protozoología
Asociación Argentina de Nanomedicinas
Asociación Argentina de Ciencia y Tecnología de Animales de Laboratorio
Materia
AQUEOUS MICELLAR
TWO-PHASE SYSTEMS
PEPSIN-LIKE
PROTEASE
SURUBI
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:11336/154121
Acceder
id CONICETDig_4d166dca76b7b0607041322ba46d0ff3
oai_identifier_str oai:ri.conicet.gov.ar:11336/154121
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Aqueous micellar two phase systems as novel tools to recover pepsin like surubí proteases: effect of surfactants on enzyme activityAcevedo Gomez, Antonella ValeriaEscobar, GuilermoGomez, Gabriela NoemiLeiva, Laura Cristina AnaBustillo, SoledadNerli, Bibiana BeatrizAQUEOUS MICELLARTWO-PHASE SYSTEMSPEPSIN-LIKEPROTEASESURUBIhttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2Surubí is farmed in the northeast of Argentina. It is of interest to valorize the current disposal of fish processing through the use of viscera waste, source of enzymes such as Pepsin. These enzymes have been recovered mainly using conventional methods (e.g.salting out, chromatography), however the use of liquid-liquid extraction using surfactants have not been fully explored. Aqueous micellar two-phase systems (AMTPS) are an extractive method based on the ability of some surfactants to form two immiscible aqueous phases, a rich and a poor micelle phases to recover the product of interest. Thus, the objective of this work was to firstly evaluate the stability of surubí crude extracts under different concentrations of Genapol (GX080) and Tergitol (Tg7) to estimate the feasibility of their use as potential micellar extractants of surubí pepsin. Enzymatic extracts (ERPi) were recovered from stomachs homogenates using salting-out procedure and pepsin activity was estimated by acid hemoglobin method. ERPi were first incubated with various concentrations of surfactants (1, 3 and 5% GX080/Tg7) in 100mM NaCit pH 5 for different times (0, 1, 2 and 3h) and then enzymatic activity was measured. Data represent the mean ± standard deviation (SD) of at least three replications. Statistical significance was tested by one-way ANOVA and Tukey (HSD) (p<0.05) Results showed that any surfactant concentration tested affected ERPi enzymatic activity moderately and this effect was dose dependent. ERPi retained 92, 65 and 60% of its initial activity when were incubated with 1, 3 and 5% of Tg7. After incubating with GX080 (1, 3 and 5%), the ERPi exhibited 80, 70 and 60% of its initial activity, respectively. The time variable in these assays had not significant influence on enzymatic activity decrease. Pepsin, a hydrophilic protein, is expected to be preferentially distributed into the aqueous phase of AMTPS.Considering that the surfactant concentration at this phase is always below 1%, the obtained results suggest that AMTPS formed with either GX080 or Tg7 could be viable tools in the primary recovery of pepsin-like proteases from fishing waste.Fil: Acevedo Gomez, Antonella Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; ArgentinaFil: Escobar, Guilermo. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Departamento de Bioquímica. Laboratorio de Investigación en Proteínas; ArgentinaFil: Gomez, Gabriela Noemi. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; ArgentinaFil: Leiva, Laura Cristina Ana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; ArgentinaFil: Bustillo, Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; ArgentinaFil: Nerli, Bibiana Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Procesos Biotecnológicos y Químicos Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Procesos Biotecnológicos y Químicos Rosario; ArgentinaReunión Anual de Sociedades de BiocienciaMar del PlataArgentinaSociedad Argentina de Farmacologia ExperimentalSociedad Argentina de Investigación ClínicaSociedad Argentina de BiologíaSociedad Argentina de ProtozoologíaAsociación Argentina de NanomedicinasAsociación Argentina de Ciencia y Tecnología de Animales de LaboratorioFundación Revista Medicina2019info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectReuniónJournalhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/vnd.openxmlformats-officedocument.wordprocessingml.documentapplication/vnd.openxmlformats-officedocument.wordprocessingml.documentapplication/pdfhttp://hdl.handle.net/11336/154121Aqueous micellar two phase systems as novel tools to recover pepsin like surubí proteases: effect of surfactants on enzyme activity; Reunión Anual de Sociedades de Biociencia; Mar del Plata; Argentina; 2019; 80-800025-76801669-9106CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.medicinabuenosaires.com/indices-de-2010-a-2019/Nacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:29:47Zoai:ri.conicet.gov.ar:11336/154121instacron: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:34982025-10-15 15:29:47.31CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Aqueous micellar two phase systems as novel tools to recover pepsin like surubí proteases: effect of surfactants on enzyme activity
title Aqueous micellar two phase systems as novel tools to recover pepsin like surubí proteases: effect of surfactants on enzyme activity
spellingShingle Aqueous micellar two phase systems as novel tools to recover pepsin like surubí proteases: effect of surfactants on enzyme activity
Acevedo Gomez, Antonella Valeria
AQUEOUS MICELLAR
TWO-PHASE SYSTEMS
PEPSIN-LIKE
PROTEASE
SURUBI
title_short Aqueous micellar two phase systems as novel tools to recover pepsin like surubí proteases: effect of surfactants on enzyme activity
title_full Aqueous micellar two phase systems as novel tools to recover pepsin like surubí proteases: effect of surfactants on enzyme activity
title_fullStr Aqueous micellar two phase systems as novel tools to recover pepsin like surubí proteases: effect of surfactants on enzyme activity
title_full_unstemmed Aqueous micellar two phase systems as novel tools to recover pepsin like surubí proteases: effect of surfactants on enzyme activity
title_sort Aqueous micellar two phase systems as novel tools to recover pepsin like surubí proteases: effect of surfactants on enzyme activity
dc.creator.none.fl_str_mv Acevedo Gomez, Antonella Valeria
Escobar, Guilermo
Gomez, Gabriela Noemi
Leiva, Laura Cristina Ana
Bustillo, Soledad
Nerli, Bibiana Beatriz
author Acevedo Gomez, Antonella Valeria
author_facet Acevedo Gomez, Antonella Valeria
Escobar, Guilermo
Gomez, Gabriela Noemi
Leiva, Laura Cristina Ana
Bustillo, Soledad
Nerli, Bibiana Beatriz
author_role author
author2 Escobar, Guilermo
Gomez, Gabriela Noemi
Leiva, Laura Cristina Ana
Bustillo, Soledad
Nerli, Bibiana Beatriz
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv AQUEOUS MICELLAR
TWO-PHASE SYSTEMS
PEPSIN-LIKE
PROTEASE
SURUBI
topic AQUEOUS MICELLAR
TWO-PHASE SYSTEMS
PEPSIN-LIKE
PROTEASE
SURUBI
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.9
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Surubí is farmed in the northeast of Argentina. It is of interest to valorize the current disposal of fish processing through the use of viscera waste, source of enzymes such as Pepsin. These enzymes have been recovered mainly using conventional methods (e.g.salting out, chromatography), however the use of liquid-liquid extraction using surfactants have not been fully explored. Aqueous micellar two-phase systems (AMTPS) are an extractive method based on the ability of some surfactants to form two immiscible aqueous phases, a rich and a poor micelle phases to recover the product of interest. Thus, the objective of this work was to firstly evaluate the stability of surubí crude extracts under different concentrations of Genapol (GX080) and Tergitol (Tg7) to estimate the feasibility of their use as potential micellar extractants of surubí pepsin. Enzymatic extracts (ERPi) were recovered from stomachs homogenates using salting-out procedure and pepsin activity was estimated by acid hemoglobin method. ERPi were first incubated with various concentrations of surfactants (1, 3 and 5% GX080/Tg7) in 100mM NaCit pH 5 for different times (0, 1, 2 and 3h) and then enzymatic activity was measured. Data represent the mean ± standard deviation (SD) of at least three replications. Statistical significance was tested by one-way ANOVA and Tukey (HSD) (p<0.05) Results showed that any surfactant concentration tested affected ERPi enzymatic activity moderately and this effect was dose dependent. ERPi retained 92, 65 and 60% of its initial activity when were incubated with 1, 3 and 5% of Tg7. After incubating with GX080 (1, 3 and 5%), the ERPi exhibited 80, 70 and 60% of its initial activity, respectively. The time variable in these assays had not significant influence on enzymatic activity decrease. Pepsin, a hydrophilic protein, is expected to be preferentially distributed into the aqueous phase of AMTPS.Considering that the surfactant concentration at this phase is always below 1%, the obtained results suggest that AMTPS formed with either GX080 or Tg7 could be viable tools in the primary recovery of pepsin-like proteases from fishing waste.
Fil: Acevedo Gomez, Antonella Valeria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; Argentina
Fil: Escobar, Guilermo. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Departamento de Bioquímica. Laboratorio de Investigación en Proteínas; Argentina
Fil: Gomez, Gabriela Noemi. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; Argentina
Fil: Leiva, Laura Cristina Ana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; Argentina
Fil: Bustillo, Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Nordeste. Instituto de Química Básica y Aplicada del Nordeste Argentino. Universidad Nacional del Nordeste. Facultad de Ciencias Exactas Naturales y Agrimensura. Instituto de Química Básica y Aplicada del Nordeste Argentino; Argentina
Fil: Nerli, Bibiana Beatriz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Procesos Biotecnológicos y Químicos Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Procesos Biotecnológicos y Químicos Rosario; Argentina
Reunión Anual de Sociedades de Biociencia
Mar del Plata
Argentina
Sociedad Argentina de Farmacologia Experimental
Sociedad Argentina de Investigación Clínica
Sociedad Argentina de Biología
Sociedad Argentina de Protozoología
Asociación Argentina de Nanomedicinas
Asociación Argentina de Ciencia y Tecnología de Animales de Laboratorio
description Surubí is farmed in the northeast of Argentina. It is of interest to valorize the current disposal of fish processing through the use of viscera waste, source of enzymes such as Pepsin. These enzymes have been recovered mainly using conventional methods (e.g.salting out, chromatography), however the use of liquid-liquid extraction using surfactants have not been fully explored. Aqueous micellar two-phase systems (AMTPS) are an extractive method based on the ability of some surfactants to form two immiscible aqueous phases, a rich and a poor micelle phases to recover the product of interest. Thus, the objective of this work was to firstly evaluate the stability of surubí crude extracts under different concentrations of Genapol (GX080) and Tergitol (Tg7) to estimate the feasibility of their use as potential micellar extractants of surubí pepsin. Enzymatic extracts (ERPi) were recovered from stomachs homogenates using salting-out procedure and pepsin activity was estimated by acid hemoglobin method. ERPi were first incubated with various concentrations of surfactants (1, 3 and 5% GX080/Tg7) in 100mM NaCit pH 5 for different times (0, 1, 2 and 3h) and then enzymatic activity was measured. Data represent the mean ± standard deviation (SD) of at least three replications. Statistical significance was tested by one-way ANOVA and Tukey (HSD) (p<0.05) Results showed that any surfactant concentration tested affected ERPi enzymatic activity moderately and this effect was dose dependent. ERPi retained 92, 65 and 60% of its initial activity when were incubated with 1, 3 and 5% of Tg7. After incubating with GX080 (1, 3 and 5%), the ERPi exhibited 80, 70 and 60% of its initial activity, respectively. The time variable in these assays had not significant influence on enzymatic activity decrease. Pepsin, a hydrophilic protein, is expected to be preferentially distributed into the aqueous phase of AMTPS.Considering that the surfactant concentration at this phase is always below 1%, the obtained results suggest that AMTPS formed with either GX080 or Tg7 could be viable tools in the primary recovery of pepsin-like proteases from fishing waste.
publishDate 2019
dc.date.none.fl_str_mv 2019
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/conferenceObject
Reunión
Journal
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/11336/154121
Aqueous micellar two phase systems as novel tools to recover pepsin like surubí proteases: effect of surfactants on enzyme activity; Reunión Anual de Sociedades de Biociencia; Mar del Plata; Argentina; 2019; 80-80
0025-7680
1669-9106
CONICET Digital
CONICET
url http://hdl.handle.net/11336/154121
identifier_str_mv Aqueous micellar two phase systems as novel tools to recover pepsin like surubí proteases: effect of surfactants on enzyme activity; Reunión Anual de Sociedades de Biociencia; Mar del Plata; Argentina; 2019; 80-80
0025-7680
1669-9106
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.medicinabuenosaires.com/indices-de-2010-a-2019/
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
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eu_rights_str_mv openAccess
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dc.coverage.none.fl_str_mv Nacional
dc.publisher.none.fl_str_mv Fundación Revista Medicina
publisher.none.fl_str_mv Fundación Revista Medicina
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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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