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Registro Completo |
Biblioteca(s): |
Embrapa Pecuária Sul. |
Data corrente: |
10/11/2014 |
Data da última atualização: |
10/11/2014 |
Tipo da produção científica: |
Resumo em Anais de Congresso |
Autoria: |
MARTIN, M. de S.; GENRO, T. C. M.; FARIA, B. M. de; ROSSETTO, J.; SILVA, M. A. P. da; SAVIAN, J. V.; BAYER, C.; CARVALHO, P. C. de F. |
Afiliação: |
Maiara de Sousa Martin, ACADÊMICA URCAMP; TERESA CRISTINA MORAES GENRO, CPPSUL; Bruna Moscat de Faria, POSGRADUANDA UFRGS; Jusiane Rossetto, POSGRADUANDA UFRGS; MARCO ANTONIO PADILHA DA SILVA, CPPSUL; Jean Victor Savian, DOUTORANDO UFRGS; Cimélio Bayer, UFRGS; Paulo César de Faccio Carvalho, UFRGS. |
Título: |
O metano na pecuária: serão os bovinos de corte mantidos em pastagem natural os vilões? |
Ano de publicação: |
2014 |
Fonte/Imprenta: |
In: SIMPÓSIO DE INICIAÇÃO CIENTÍFICA DA EMBRAPA PECUÁRIA SUL, 4., 2014, Bagé. Resumos... Bagé: Embrapa Pecuária Sul, 2014. |
Páginas: |
p. 24. |
Idioma: |
Português |
Thesagro: |
Efeito Estufa. |
Categoria do assunto: |
-- |
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/111209/1/Martin-et-al.pdf
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Marc: |
LEADER 00706nam a2200205 a 4500 001 1999499 005 2014-11-10 008 2014 bl uuuu u00u1 u #d 100 1 $aMARTIN, M. de S. 245 $aO metano na pecuária$bserão os bovinos de corte mantidos em pastagem natural os vilões?$h[electronic resource] 260 $aIn: SIMPÓSIO DE INICIAÇÃO CIENTÍFICA DA EMBRAPA PECUÁRIA SUL, 4., 2014, Bagé. Resumos... Bagé: Embrapa Pecuária Sul$c2014 300 $ap. 24. 650 $aEfeito Estufa 700 1 $aGENRO, T. C. M. 700 1 $aFARIA, B. M. de 700 1 $aROSSETTO, J. 700 1 $aSILVA, M. A. P. da 700 1 $aSAVIAN, J. V. 700 1 $aBAYER, C. 700 1 $aCARVALHO, P. C. de F.
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Registro original: |
Embrapa Pecuária Sul (CPPSUL) |
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Registro Completo
Biblioteca(s): |
Embrapa Agroenergia. |
Data corrente: |
27/01/2021 |
Data da última atualização: |
27/01/2021 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
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. |
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. |
Título: |
Functional screening of a Caatinga goat (Capra hircus) rumen metagenomic library reveals a novel GH3 beta-xylosidase. |
Ano de publicação: |
2021 |
Fonte/Imprenta: |
PLoS ONE, v. 16, n. 1, e024511, 2021. |
DOI: |
https://doi.org/10.1371/journal.pone.0245118 |
Idioma: |
Inglês |
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 |
Thesagro: |
Clonagem; Enzima; Peptídeo; Programa de Computador. |
Thesaurus NAL: |
Cloning (animals); Computer software; Enzymes; Metagenomics; Prevotella; Screening; Signal peptide. |
Categoria do assunto: |
-- |
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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