Impact of manganese on the production of a biomass associated β-D-glucosidase activity using a thermophilic Bacillus licheniformis strain
- Autores
- Abdulhamid, María Belén; Baigori, Mario Domingo; Pera, Licia Maria
- Año de publicación
- 2015
- Idioma
- español castellano
- Tipo de recurso
- documento de conferencia
- Estado
- versión publicada
- Descripción
- The b-Glucosidase (EC 3.2.1.21) constitutes a group of well-studied hydrolases. This enzyme catalyzes the hydrolysis of arylglucosides, alkylglucosides, cellobiose, and cellooligosaccharides. The interest in this biocatalyst centers on its roles in the enzymatic hydrolysis of cellulose. The rate of cellulose hydrolysis can be improved by supplementing commercial cellulases with immobilized b-D-glucosidase, which usually has high stability and can be recovered and reused. In addition, for industrial saccharification of cellulosic materials, b-glucosidases from thermophilic bacteria are also of particular interest due to their increased stability. In this work, we study the influence of manganese on the production of a biomass associate b-D-glucosidase activity using a thermophilic Bacillus licheniformis strain. Assays were performed at 45 °C in 500 ml Erlenmeyer containing 200 ml of LB medium supplemented with 0 - 1.0 mM MnCl2 . The b-D-glucosidase activity was also determined at 45 °C using 3.6 mM p-nitrophenyl-b -D-glucopyranoside (Sigma) as substrate. Cells were harvested by centrifugation and washed twice with 100 mM Tris-HCl buffer (pH 7). The pellet was resuspended in the same buffer, and it was directly used as the b-D-glucosidase source. The mixture was shaken at 1000 rpm. Then, the absorbance of the supernatant was measured at 405 nm and the enzyme activity calculated and related to the biomass dry weight. One unit of the enzyme was defined as the amount needed to release 1 µmol p-nitrophenol per min. Thus, dose-response experiments showed that in the presence of 0.3 mM MnCl2 the enzyme production was increased by about 20%. Under this culture condition, a specific activity value of 19.99 U per mg of dry weight was obtaining after 4 h of cultivation. Finally, these results could be of relevance to the bioethanol industry where lignocellulosic material is used as feedstock for fermentation and, which should be treated enzymatically. The use of naturally bound enzymes is an important immobilization technique. This type of biocatalyst system is potentially cost-effective because the biomass can be directly utilized in the treatment.
Fil: Abdulhamid, María Belén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
Fil: Baigori, Mario Domingo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
Fil: Pera, Licia Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
XI Congreso Argentino de Microbiología General
Cordoba
Argentina
Sociedad Argentina de Microbiología General - Materia
-
Production
β-D-glucosidase associated to the biomass
Bacillus - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/195121
Ver los metadatos del registro completo
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CONICET Digital (CONICET) |
spelling |
Impact of manganese on the production of a biomass associated β-D-glucosidase activity using a thermophilic Bacillus licheniformis strainAbdulhamid, María BelénBaigori, Mario DomingoPera, Licia MariaProductionβ-D-glucosidase associated to the biomassBacillushttps://purl.org/becyt/ford/2.9https://purl.org/becyt/ford/2The b-Glucosidase (EC 3.2.1.21) constitutes a group of well-studied hydrolases. This enzyme catalyzes the hydrolysis of arylglucosides, alkylglucosides, cellobiose, and cellooligosaccharides. The interest in this biocatalyst centers on its roles in the enzymatic hydrolysis of cellulose. The rate of cellulose hydrolysis can be improved by supplementing commercial cellulases with immobilized b-D-glucosidase, which usually has high stability and can be recovered and reused. In addition, for industrial saccharification of cellulosic materials, b-glucosidases from thermophilic bacteria are also of particular interest due to their increased stability. In this work, we study the influence of manganese on the production of a biomass associate b-D-glucosidase activity using a thermophilic Bacillus licheniformis strain. Assays were performed at 45 °C in 500 ml Erlenmeyer containing 200 ml of LB medium supplemented with 0 - 1.0 mM MnCl2 . The b-D-glucosidase activity was also determined at 45 °C using 3.6 mM p-nitrophenyl-b -D-glucopyranoside (Sigma) as substrate. Cells were harvested by centrifugation and washed twice with 100 mM Tris-HCl buffer (pH 7). The pellet was resuspended in the same buffer, and it was directly used as the b-D-glucosidase source. The mixture was shaken at 1000 rpm. Then, the absorbance of the supernatant was measured at 405 nm and the enzyme activity calculated and related to the biomass dry weight. One unit of the enzyme was defined as the amount needed to release 1 µmol p-nitrophenol per min. Thus, dose-response experiments showed that in the presence of 0.3 mM MnCl2 the enzyme production was increased by about 20%. Under this culture condition, a specific activity value of 19.99 U per mg of dry weight was obtaining after 4 h of cultivation. Finally, these results could be of relevance to the bioethanol industry where lignocellulosic material is used as feedstock for fermentation and, which should be treated enzymatically. The use of naturally bound enzymes is an important immobilization technique. This type of biocatalyst system is potentially cost-effective because the biomass can be directly utilized in the treatment.Fil: Abdulhamid, María Belén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Baigori, Mario Domingo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Pera, Licia Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaXI Congreso Argentino de Microbiología GeneralCordobaArgentinaSociedad Argentina de Microbiología GeneralSociedad Argentina de Microbiología General2015info: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/11336/195121Impact of manganese on the production of a biomass associated β-D-glucosidase activity using a thermophilic Bacillus licheniformis strain; XI Congreso Argentino de Microbiología General; Cordoba; Argentina; 2015; 69-69CONICET DigitalCONICETspainfo:eu-repo/semantics/altIdentifier/url/https://samige.org.ar/wp-content/uploads/2022/10/Libro-SAMIGE-2015.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 Técnicas2025-09-29T09:56:20Zoai:ri.conicet.gov.ar:11336/195121instacron: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:34982025-09-29 09:56:20.616CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Impact of manganese on the production of a biomass associated β-D-glucosidase activity using a thermophilic Bacillus licheniformis strain |
title |
Impact of manganese on the production of a biomass associated β-D-glucosidase activity using a thermophilic Bacillus licheniformis strain |
spellingShingle |
Impact of manganese on the production of a biomass associated β-D-glucosidase activity using a thermophilic Bacillus licheniformis strain Abdulhamid, María Belén Production β-D-glucosidase associated to the biomass Bacillus |
title_short |
Impact of manganese on the production of a biomass associated β-D-glucosidase activity using a thermophilic Bacillus licheniformis strain |
title_full |
Impact of manganese on the production of a biomass associated β-D-glucosidase activity using a thermophilic Bacillus licheniformis strain |
title_fullStr |
Impact of manganese on the production of a biomass associated β-D-glucosidase activity using a thermophilic Bacillus licheniformis strain |
title_full_unstemmed |
Impact of manganese on the production of a biomass associated β-D-glucosidase activity using a thermophilic Bacillus licheniformis strain |
title_sort |
Impact of manganese on the production of a biomass associated β-D-glucosidase activity using a thermophilic Bacillus licheniformis strain |
dc.creator.none.fl_str_mv |
Abdulhamid, María Belén Baigori, Mario Domingo Pera, Licia Maria |
author |
Abdulhamid, María Belén |
author_facet |
Abdulhamid, María Belén Baigori, Mario Domingo Pera, Licia Maria |
author_role |
author |
author2 |
Baigori, Mario Domingo Pera, Licia Maria |
author2_role |
author author |
dc.subject.none.fl_str_mv |
Production β-D-glucosidase associated to the biomass Bacillus |
topic |
Production β-D-glucosidase associated to the biomass Bacillus |
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 b-Glucosidase (EC 3.2.1.21) constitutes a group of well-studied hydrolases. This enzyme catalyzes the hydrolysis of arylglucosides, alkylglucosides, cellobiose, and cellooligosaccharides. The interest in this biocatalyst centers on its roles in the enzymatic hydrolysis of cellulose. The rate of cellulose hydrolysis can be improved by supplementing commercial cellulases with immobilized b-D-glucosidase, which usually has high stability and can be recovered and reused. In addition, for industrial saccharification of cellulosic materials, b-glucosidases from thermophilic bacteria are also of particular interest due to their increased stability. In this work, we study the influence of manganese on the production of a biomass associate b-D-glucosidase activity using a thermophilic Bacillus licheniformis strain. Assays were performed at 45 °C in 500 ml Erlenmeyer containing 200 ml of LB medium supplemented with 0 - 1.0 mM MnCl2 . The b-D-glucosidase activity was also determined at 45 °C using 3.6 mM p-nitrophenyl-b -D-glucopyranoside (Sigma) as substrate. Cells were harvested by centrifugation and washed twice with 100 mM Tris-HCl buffer (pH 7). The pellet was resuspended in the same buffer, and it was directly used as the b-D-glucosidase source. The mixture was shaken at 1000 rpm. Then, the absorbance of the supernatant was measured at 405 nm and the enzyme activity calculated and related to the biomass dry weight. One unit of the enzyme was defined as the amount needed to release 1 µmol p-nitrophenol per min. Thus, dose-response experiments showed that in the presence of 0.3 mM MnCl2 the enzyme production was increased by about 20%. Under this culture condition, a specific activity value of 19.99 U per mg of dry weight was obtaining after 4 h of cultivation. Finally, these results could be of relevance to the bioethanol industry where lignocellulosic material is used as feedstock for fermentation and, which should be treated enzymatically. The use of naturally bound enzymes is an important immobilization technique. This type of biocatalyst system is potentially cost-effective because the biomass can be directly utilized in the treatment. Fil: Abdulhamid, María Belén. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina Fil: Baigori, Mario Domingo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina Fil: Pera, Licia Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina XI Congreso Argentino de Microbiología General Cordoba Argentina Sociedad Argentina de Microbiología General |
description |
The b-Glucosidase (EC 3.2.1.21) constitutes a group of well-studied hydrolases. This enzyme catalyzes the hydrolysis of arylglucosides, alkylglucosides, cellobiose, and cellooligosaccharides. The interest in this biocatalyst centers on its roles in the enzymatic hydrolysis of cellulose. The rate of cellulose hydrolysis can be improved by supplementing commercial cellulases with immobilized b-D-glucosidase, which usually has high stability and can be recovered and reused. In addition, for industrial saccharification of cellulosic materials, b-glucosidases from thermophilic bacteria are also of particular interest due to their increased stability. In this work, we study the influence of manganese on the production of a biomass associate b-D-glucosidase activity using a thermophilic Bacillus licheniformis strain. Assays were performed at 45 °C in 500 ml Erlenmeyer containing 200 ml of LB medium supplemented with 0 - 1.0 mM MnCl2 . The b-D-glucosidase activity was also determined at 45 °C using 3.6 mM p-nitrophenyl-b -D-glucopyranoside (Sigma) as substrate. Cells were harvested by centrifugation and washed twice with 100 mM Tris-HCl buffer (pH 7). The pellet was resuspended in the same buffer, and it was directly used as the b-D-glucosidase source. The mixture was shaken at 1000 rpm. Then, the absorbance of the supernatant was measured at 405 nm and the enzyme activity calculated and related to the biomass dry weight. One unit of the enzyme was defined as the amount needed to release 1 µmol p-nitrophenol per min. Thus, dose-response experiments showed that in the presence of 0.3 mM MnCl2 the enzyme production was increased by about 20%. Under this culture condition, a specific activity value of 19.99 U per mg of dry weight was obtaining after 4 h of cultivation. Finally, these results could be of relevance to the bioethanol industry where lignocellulosic material is used as feedstock for fermentation and, which should be treated enzymatically. The use of naturally bound enzymes is an important immobilization technique. This type of biocatalyst system is potentially cost-effective because the biomass can be directly utilized in the treatment. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015 |
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/11336/195121 Impact of manganese on the production of a biomass associated β-D-glucosidase activity using a thermophilic Bacillus licheniformis strain; XI Congreso Argentino de Microbiología General; Cordoba; Argentina; 2015; 69-69 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/195121 |
identifier_str_mv |
Impact of manganese on the production of a biomass associated β-D-glucosidase activity using a thermophilic Bacillus licheniformis strain; XI Congreso Argentino de Microbiología General; Cordoba; Argentina; 2015; 69-69 CONICET Digital CONICET |
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spa |
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info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
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Sociedad Argentina de Microbiología General |
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Sociedad Argentina de Microbiología General |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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