A Peptidase Enzyme from Bacillus cereus with Antimicrobial Properties: Optimizing the Immobilization in Chitosan Beads Using Box-Behnken Design

Autores
Kotlar, Catalina Elena; Roura, Sara Ines; Ponce, Alejandra Graciela
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Enzymes are exploited as catalysts in many industrial, biomedical, and analytical processes. There has been considerable interest in the development of carrier systems for enzyme immobilization because immobilized enzymes have enhanced stability compared to soluble enzymes, and can easily be separated from the reaction. In the current study, microbial peptidases liberated by B. cereus were immobilized in cross-linked chitosan beads and characterized using azocasein as a substrate. The Box-Behnken design was applied to determine the optimal conditions to maximize proteolytic activity. An empirical second-order model was determined by multiple regression analysis of the experimental data to describe the relationship between tested variables and the response. The determination coefficients (R2) were above 90%. Under optimal conditions (2.2 mm bead diameter, 1.06 enzyme/ bead ratio, 5.82% v/v glutaraldehyde and 18°C) the proteolytic activity was 0.938 U/ml. The retained immobilized enzyme can be reused up to five times. The storage stability of immobilized peptidases at 4°C was up to 10 days, while at 32°C the enzyme lost its activity within three days. Finally, novel antimicrobial properties of the immobilized peptidases were found. These results could have important benefit for the food industry.
Fil: Kotlar, Catalina Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ingeniería. Departamento de Ingeniería Química; Argentina
Fil: Roura, Sara Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ingeniería. Departamento de Ingeniería Química; Argentina
Fil: Ponce, Alejandra Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ingeniería. Departamento de Ingeniería Química; Argentina
Materia
BACILLUS CEREUS
INMOBILIZATION ENZYMES
RESPONSE SURFACE METHODOLOGY
PROTEOLYTIC ENZYMES
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:11336/71543
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/71543
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A Peptidase Enzyme from Bacillus cereus with Antimicrobial Properties: Optimizing the Immobilization in Chitosan Beads Using Box-Behnken DesignKotlar, Catalina ElenaRoura, Sara InesPonce, Alejandra GracielaBACILLUS CEREUSINMOBILIZATION ENZYMESRESPONSE SURFACE METHODOLOGYPROTEOLYTIC ENZYMEShttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2Enzymes are exploited as catalysts in many industrial, biomedical, and analytical processes. There has been considerable interest in the development of carrier systems for enzyme immobilization because immobilized enzymes have enhanced stability compared to soluble enzymes, and can easily be separated from the reaction. In the current study, microbial peptidases liberated by B. cereus were immobilized in cross-linked chitosan beads and characterized using azocasein as a substrate. The Box-Behnken design was applied to determine the optimal conditions to maximize proteolytic activity. An empirical second-order model was determined by multiple regression analysis of the experimental data to describe the relationship between tested variables and the response. The determination coefficients (R2) were above 90%. Under optimal conditions (2.2 mm bead diameter, 1.06 enzyme/ bead ratio, 5.82% v/v glutaraldehyde and 18°C) the proteolytic activity was 0.938 U/ml. The retained immobilized enzyme can be reused up to five times. The storage stability of immobilized peptidases at 4°C was up to 10 days, while at 32°C the enzyme lost its activity within three days. Finally, novel antimicrobial properties of the immobilized peptidases were found. These results could have important benefit for the food industry.Fil: Kotlar, Catalina Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ingeniería. Departamento de Ingeniería Química; ArgentinaFil: Roura, Sara Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ingeniería. Departamento de Ingeniería Química; ArgentinaFil: Ponce, Alejandra Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ingeniería. Departamento de Ingeniería Química; ArgentinaSciepub2016-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/71543Kotlar, Catalina Elena; Roura, Sara Ines; Ponce, Alejandra Graciela; A Peptidase Enzyme from Bacillus cereus with Antimicrobial Properties: Optimizing the Immobilization in Chitosan Beads Using Box-Behnken Design; Sciepub; Journal of Polymer and Biopolymer Physics Chemistry; 4; 5-2016; 28-392373-3403CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.sciepub.com/JPBPC/abstract/6935info:eu-repo/semantics/altIdentifier/doi/10.12691/jpbpc-4-1-4info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:16:17Zoai:ri.conicet.gov.ar:11336/71543instacron: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 15:16:17.298CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A Peptidase Enzyme from Bacillus cereus with Antimicrobial Properties: Optimizing the Immobilization in Chitosan Beads Using Box-Behnken Design
title A Peptidase Enzyme from Bacillus cereus with Antimicrobial Properties: Optimizing the Immobilization in Chitosan Beads Using Box-Behnken Design
spellingShingle A Peptidase Enzyme from Bacillus cereus with Antimicrobial Properties: Optimizing the Immobilization in Chitosan Beads Using Box-Behnken Design
Kotlar, Catalina Elena
BACILLUS CEREUS
INMOBILIZATION ENZYMES
RESPONSE SURFACE METHODOLOGY
PROTEOLYTIC ENZYMES
title_short A Peptidase Enzyme from Bacillus cereus with Antimicrobial Properties: Optimizing the Immobilization in Chitosan Beads Using Box-Behnken Design
title_full A Peptidase Enzyme from Bacillus cereus with Antimicrobial Properties: Optimizing the Immobilization in Chitosan Beads Using Box-Behnken Design
title_fullStr A Peptidase Enzyme from Bacillus cereus with Antimicrobial Properties: Optimizing the Immobilization in Chitosan Beads Using Box-Behnken Design
title_full_unstemmed A Peptidase Enzyme from Bacillus cereus with Antimicrobial Properties: Optimizing the Immobilization in Chitosan Beads Using Box-Behnken Design
title_sort A Peptidase Enzyme from Bacillus cereus with Antimicrobial Properties: Optimizing the Immobilization in Chitosan Beads Using Box-Behnken Design
dc.creator.none.fl_str_mv Kotlar, Catalina Elena
Roura, Sara Ines
Ponce, Alejandra Graciela
author Kotlar, Catalina Elena
author_facet Kotlar, Catalina Elena
Roura, Sara Ines
Ponce, Alejandra Graciela
author_role author
author2 Roura, Sara Ines
Ponce, Alejandra Graciela
author2_role author
author
dc.subject.none.fl_str_mv BACILLUS CEREUS
INMOBILIZATION ENZYMES
RESPONSE SURFACE METHODOLOGY
PROTEOLYTIC ENZYMES
topic BACILLUS CEREUS
INMOBILIZATION ENZYMES
RESPONSE SURFACE METHODOLOGY
PROTEOLYTIC ENZYMES
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Enzymes are exploited as catalysts in many industrial, biomedical, and analytical processes. There has been considerable interest in the development of carrier systems for enzyme immobilization because immobilized enzymes have enhanced stability compared to soluble enzymes, and can easily be separated from the reaction. In the current study, microbial peptidases liberated by B. cereus were immobilized in cross-linked chitosan beads and characterized using azocasein as a substrate. The Box-Behnken design was applied to determine the optimal conditions to maximize proteolytic activity. An empirical second-order model was determined by multiple regression analysis of the experimental data to describe the relationship between tested variables and the response. The determination coefficients (R2) were above 90%. Under optimal conditions (2.2 mm bead diameter, 1.06 enzyme/ bead ratio, 5.82% v/v glutaraldehyde and 18°C) the proteolytic activity was 0.938 U/ml. The retained immobilized enzyme can be reused up to five times. The storage stability of immobilized peptidases at 4°C was up to 10 days, while at 32°C the enzyme lost its activity within three days. Finally, novel antimicrobial properties of the immobilized peptidases were found. These results could have important benefit for the food industry.
Fil: Kotlar, Catalina Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ingeniería. Departamento de Ingeniería Química; Argentina
Fil: Roura, Sara Ines. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ingeniería. Departamento de Ingeniería Química; Argentina
Fil: Ponce, Alejandra Graciela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ingeniería. Departamento de Ingeniería Química; Argentina
description Enzymes are exploited as catalysts in many industrial, biomedical, and analytical processes. There has been considerable interest in the development of carrier systems for enzyme immobilization because immobilized enzymes have enhanced stability compared to soluble enzymes, and can easily be separated from the reaction. In the current study, microbial peptidases liberated by B. cereus were immobilized in cross-linked chitosan beads and characterized using azocasein as a substrate. The Box-Behnken design was applied to determine the optimal conditions to maximize proteolytic activity. An empirical second-order model was determined by multiple regression analysis of the experimental data to describe the relationship between tested variables and the response. The determination coefficients (R2) were above 90%. Under optimal conditions (2.2 mm bead diameter, 1.06 enzyme/ bead ratio, 5.82% v/v glutaraldehyde and 18°C) the proteolytic activity was 0.938 U/ml. The retained immobilized enzyme can be reused up to five times. The storage stability of immobilized peptidases at 4°C was up to 10 days, while at 32°C the enzyme lost its activity within three days. Finally, novel antimicrobial properties of the immobilized peptidases were found. These results could have important benefit for the food industry.
publishDate 2016
dc.date.none.fl_str_mv 2016-05
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/71543
Kotlar, Catalina Elena; Roura, Sara Ines; Ponce, Alejandra Graciela; A Peptidase Enzyme from Bacillus cereus with Antimicrobial Properties: Optimizing the Immobilization in Chitosan Beads Using Box-Behnken Design; Sciepub; Journal of Polymer and Biopolymer Physics Chemistry; 4; 5-2016; 28-39
2373-3403
CONICET Digital
CONICET
url http://hdl.handle.net/11336/71543
identifier_str_mv Kotlar, Catalina Elena; Roura, Sara Ines; Ponce, Alejandra Graciela; A Peptidase Enzyme from Bacillus cereus with Antimicrobial Properties: Optimizing the Immobilization in Chitosan Beads Using Box-Behnken Design; Sciepub; Journal of Polymer and Biopolymer Physics Chemistry; 4; 5-2016; 28-39
2373-3403
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciepub.com/JPBPC/abstract/6935
info:eu-repo/semantics/altIdentifier/doi/10.12691/jpbpc-4-1-4
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
dc.publisher.none.fl_str_mv Sciepub
publisher.none.fl_str_mv Sciepub
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 13.22299

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