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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/195121

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network_name_str 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
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info:eu-repo/semantics/conferenceObject
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Book
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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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