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Registro Completo |
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Biblioteca(s): |
Embrapa Gado de Leite. |
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Data corrente: |
19/03/2009 |
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Data da última atualização: |
19/03/2009 |
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Tipo da produção científica: |
Resumo em Anais de Congresso |
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Autoria: |
BOITÉ, M. C.; CAMARGO, L. S. A.; GUIMARÃES, M. F. M.; SERAPIÃO, R. V.; WOHLRES-VIANA, S.; VIANA, J. H. M.; SÁ, W. F.; NOGUEIRA, L. A. G. |
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Afiliação: |
Mariana Cortes Boité, UFF; Luis Sérgio de Almeida Camargo, Embrapa Gado de Leite; Marta Fonseca Martins Guimarães, Embrapa Gado de Leite; Raquel Varella Serapião, UFRRJ; Sabine Wohlres Viana, UFJF; João Henrique Moreira Viana, Embrapa Gado de Leite; Wanderlei Ferreira de Sá, Embrapa Gado de Leite; Luiz Altamiro Garcia Nogueira, UFF. |
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Título: |
Analysis of gene expression of in vitro produced bovine blastocyst cultured for 72 hours post-vitrification. |
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Ano de publicação: |
2008 |
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Fonte/Imprenta: |
In: INTERNATIONAL CONGRESS ON ANIMAL REPRODUCTION, 16., 2008, Budapest. Abstracts... Budapest, 2008. |
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Páginas: |
p. 186 |
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Idioma: |
Inglês |
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Palavras-Chave: |
Expressão genética. |
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Thesagro: |
Bovino. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 00730naa a2200229 a 4500
001 1596311
005 2009-03-19
008 2008 bl --- 0-- u #d
100 1 $aBOITÉ, M. C.
245 $aAnalysis of gene expression of in vitro produced bovine blastocyst cultured for 72 hours post-vitrification.
260 $c2008
300 $ap. 186
650 $aBovino
653 $aExpressão genética
700 1 $aCAMARGO, L. S. A.
700 1 $aGUIMARÃES, M. F. M.
700 1 $aSERAPIÃO, R. V.
700 1 $aWOHLRES-VIANA, S.
700 1 $aVIANA, J. H. M.
700 1 $aSÁ, W. F.
700 1 $aNOGUEIRA, L. A. G.
773 $tIn: INTERNATIONAL CONGRESS ON ANIMAL REPRODUCTION, 16., 2008, Budapest. Abstracts... Budapest, 2008.
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Registro original: |
Embrapa Gado de Leite (CNPGL) |
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Registro Completo
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Biblioteca(s): |
Embrapa Agroenergia. |
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Data corrente: |
27/01/2021 |
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Data da última atualização: |
27/01/2021 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
SOUTO, B. de M.; ARAÚJO, A. C. B. de; HAMANN, P. R. V.; BASTOS, A. de R.; CUNHA, I. de S.; PEIXOTO, J.; KRUGER, R. H.; NORONHA, E. F.; QUIRINO, B. F. |
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Afiliação: |
BETULIA DE MORAIS SOUTO, CNPAE; Ana Carolina Bitencourt de Araújo; Pedro Ricardo Vieira Hamann, Universidade de Brasília; Andrêssa de Rezende Bastos; Isabel de Souza Cunha, Universidade Católica de Brasília; Julianna Peixoto, Universidade de Brasília; Ricardo Henrique Kruger, Universidade de Brasília; Eliane Ferreira Noronha, Universidade de Brasília; BETANIA FERRAZ QUIRINO, CNPAE. |
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Título: |
Functional screening of a Caatinga goat (Capra hircus) rumen metagenomic library reveals a novel GH3 beta-xylosidase. |
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Ano de publicação: |
2021 |
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Fonte/Imprenta: |
PLoS ONE, v. 16, n. 1, e024511, 2021. |
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DOI: |
https://doi.org/10.1371/journal.pone.0245118 |
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Idioma: |
Inglês |
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Conteúdo: |
Functional screening of metagenomic libraries is an effective approach for identification of novel enzymes. A Caatinga biome goat rumen metagenomic library was screened using esculin as a substrate, and a gene from an unknown bacterium encoding a novel GH3 enzyme, BGL11, was identified. None of the BGL11 closely related genes have been previously characterized. Recombinant BGL11 was obtained and kinetically characterized. Substrate specificity of the purified protein was assessed using seven synthetic aryl substrates. Activity towards nitrophenyl-beta-D-glucopyranoside (pNPG), 4-nitrophenyl- beta -D-xylopyranoside (pNPX) and 4-nitrophenyl- beta -D-cellobioside (pNPC) suggested that BGL11 is a multifunctional enzyme with beta-glucosidase, beta-xylosidase, and cellobiohydrolase activities. However, further testing with five natural substrates revealed that, although BGL11 has multiple substrate specificity, it is most active towards xylobiose. Thus, in its native goat rumen environment, BGL11 most likely functions as an extracellular beta-xylosidase acting on hemicellulose. Biochemical characterization of BGL11 showed an optimal pH of 5.6, and an optimal temperature of 50°C. Enzyme stability, an important parameter for industrial application, was also investigated. At 40°C purified BGL11 remained active for more than 15 hours without reduction in activity, and at 50°C, after 7 hours of incubation, BGL11 remained 60% active. In contrast to BLG11, most beta-xylosidases kinetically studied belong to the GH43 family and have been characterized only using synthetic substrates. In industry, beta-xylosidases can be used for plant biomass deconstruction, and the released sugars can be fermented into valuable bio-products, ranging from the biofuel ethanol to the sugar substitute xylitol. MenosFunctional screening of metagenomic libraries is an effective approach for identification of novel enzymes. A Caatinga biome goat rumen metagenomic library was screened using esculin as a substrate, and a gene from an unknown bacterium encoding a novel GH3 enzyme, BGL11, was identified. None of the BGL11 closely related genes have been previously characterized. Recombinant BGL11 was obtained and kinetically characterized. Substrate specificity of the purified protein was assessed using seven synthetic aryl substrates. Activity towards nitrophenyl-beta-D-glucopyranoside (pNPG), 4-nitrophenyl- beta -D-xylopyranoside (pNPX) and 4-nitrophenyl- beta -D-cellobioside (pNPC) suggested that BGL11 is a multifunctional enzyme with beta-glucosidase, beta-xylosidase, and cellobiohydrolase activities. However, further testing with five natural substrates revealed that, although BGL11 has multiple substrate specificity, it is most active towards xylobiose. Thus, in its native goat rumen environment, BGL11 most likely functions as an extracellular beta-xylosidase acting on hemicellulose. Biochemical characterization of BGL11 showed an optimal pH of 5.6, and an optimal temperature of 50°C. Enzyme stability, an important parameter for industrial application, was also investigated. At 40°C purified BGL11 remained active for more than 15 hours without reduction in activity, and at 50°C, after 7 hours of incubation, BGL11 remained 60% active. In contrast to BLG11, most beta-xylosidases kinetical... Mostrar Tudo |
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Thesagro: |
Clonagem; Enzima; Peptídeo; Programa de Computador. |
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Thesaurus NAL: |
Cloning (animals); Computer software; Enzymes; Metagenomics; Prevotella; Screening; Signal peptide. |
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Categoria do assunto: |
-- |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/220708/1/Functional-screening-of-a-Caatinga-goat-2021.pdf
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Marc: |
LEADER 02852naa a2200361 a 4500
001 2129624
005 2021-01-27
008 2021 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.1371/journal.pone.0245118$2DOI
100 1 $aSOUTO, B. de M.
245 $aFunctional screening of a Caatinga goat (Capra hircus) rumen metagenomic library reveals a novel GH3 beta-xylosidase.$h[electronic resource]
260 $c2021
520 $aFunctional screening of metagenomic libraries is an effective approach for identification of novel enzymes. A Caatinga biome goat rumen metagenomic library was screened using esculin as a substrate, and a gene from an unknown bacterium encoding a novel GH3 enzyme, BGL11, was identified. None of the BGL11 closely related genes have been previously characterized. Recombinant BGL11 was obtained and kinetically characterized. Substrate specificity of the purified protein was assessed using seven synthetic aryl substrates. Activity towards nitrophenyl-beta-D-glucopyranoside (pNPG), 4-nitrophenyl- beta -D-xylopyranoside (pNPX) and 4-nitrophenyl- beta -D-cellobioside (pNPC) suggested that BGL11 is a multifunctional enzyme with beta-glucosidase, beta-xylosidase, and cellobiohydrolase activities. However, further testing with five natural substrates revealed that, although BGL11 has multiple substrate specificity, it is most active towards xylobiose. Thus, in its native goat rumen environment, BGL11 most likely functions as an extracellular beta-xylosidase acting on hemicellulose. Biochemical characterization of BGL11 showed an optimal pH of 5.6, and an optimal temperature of 50°C. Enzyme stability, an important parameter for industrial application, was also investigated. At 40°C purified BGL11 remained active for more than 15 hours without reduction in activity, and at 50°C, after 7 hours of incubation, BGL11 remained 60% active. In contrast to BLG11, most beta-xylosidases kinetically studied belong to the GH43 family and have been characterized only using synthetic substrates. In industry, beta-xylosidases can be used for plant biomass deconstruction, and the released sugars can be fermented into valuable bio-products, ranging from the biofuel ethanol to the sugar substitute xylitol.
650 $aCloning (animals)
650 $aComputer software
650 $aEnzymes
650 $aMetagenomics
650 $aPrevotella
650 $aScreening
650 $aSignal peptide
650 $aClonagem
650 $aEnzima
650 $aPeptídeo
650 $aPrograma de Computador
700 1 $aARAÚJO, A. C. B. de
700 1 $aHAMANN, P. R. V.
700 1 $aBASTOS, A. de R.
700 1 $aCUNHA, I. de S.
700 1 $aPEIXOTO, J.
700 1 $aKRUGER, R. H.
700 1 $aNORONHA, E. F.
700 1 $aQUIRINO, B. F.
773 $tPLoS ONE$gv. 16, n. 1, e024511, 2021.
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Embrapa Agroenergia (CNPAE) |
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