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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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Registro original: |
Embrapa Agroenergia (CNPAE) |
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Registro Completo
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Biblioteca(s): |
Embrapa Uva e Vinho. |
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Data corrente: |
19/07/2016 |
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Data da última atualização: |
19/07/2019 |
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Tipo da produção científica: |
Resumo em Anais de Congresso |
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Autoria: |
IWAMOTO, H.; VIEIRA, J. L.; MORAIS NETO, J. A. de; FIORELLI, L. E.; SCANAGATTA, V.; ZALAMENA, J.; MELO, G. W. B. de. |
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Afiliação: |
Hissashi Iwamoto, Graduandos do Curso de Engenharia de Bioprocessos e Biotecnologia, UERGS, Bento Gonçalves, RS. E-mails: hissashi.mobile@gmail.com; Jaqueline Leite Vieira, Graduandos do Curso de Engenharia de Bioprocessos e Biotecnologia, UERGS, Bento Gonçalves, RS; José Antônio de Morais Neto, Graduandos do Curso de Engenharia de Bioprocessos e Biotecnologia, UERGS, Bento Gonçalves, RS; Luís Eduardo Fiorelli, Graduando do Curso de Tecnologia em Viticultura e Enologia, IFRGS, Bento Gonçalves, RS. E-mail: luisefiorelli@gmail.com; VOLMIR SCANAGATTA, CNPUV; Jovani Zalamena, Pós doutorando da UFSM. E-mail: jovanizalamena@yahoo.com.br; GEORGE WELLINGTON BASTOS DE MELO, CNPUV. |
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Título: |
Efeito do gesso agrícola sobre a fitotoxicidade de cobre em aveia. |
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Ano de publicação: |
2016 |
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Fonte/Imprenta: |
In: ENCONTRO DE INICIAÇÃO CIENTÍFICA, 14. ENCONTRO DE PÓS-GRADUANDOS DA EMBRAPA UVA E VINHO, 10., 2016, Bento Gonçalves. Resumos...Bento Gonçalves, RS: Embrapa uva e Vinho, 2016. p. 42. |
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Idioma: |
Português |
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Notas: |
(Embrapa Uva e Vinho. Documentos, 99) |
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Conteúdo: |
A viticultura no Rio Grande do Sul faz uso de grande quantidade de fungicidas cúpricos, que ao se acumular no solo pode atingir níveis tóxicos às plantas. O gesso agrícola, subproduto das indústrias na produção de ácido fosfórico, é um resíduo abundante e alvo de estudo para reaproveitamento e descarte apropriado. O objetivo deste trabalho foi verificar o efeito do gesso na mitigação do cobre (Cu) na cultura da aveia e efeitos no solo. |
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Palavras-Chave: |
Anais; CNPUV; Cultura da aveia; Fitotoxicidade de cobre; Fitotoxicidade de cobre em aveia; Fungicidas cúpricos; Gesso agrícola; IC; Iniciação cientifica; Mitigação do cobre (Cu); Mitigação do cobre (Cu) na cultura da aveia; Viticultura no Rio Grande do Sul. |
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Thesagro: |
Ácido Fosfórico; Aveia; Fitotoxicidade; Fruticultura; Fungo; Solo; Uva; Viticultura. |
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Categoria do assunto: |
A Sistemas de Cultivo |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/145592/1/Doc99-iwamoto-p42.pdf
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Marc: |
LEADER 01842nam a2200433 a 4500
001 2049165
005 2019-07-19
008 2016 bl uuuu u00u1 u #d
100 1 $aIWAMOTO, H.
245 $aEfeito do gesso agrícola sobre a fitotoxicidade de cobre em aveia.$h[electronic resource]
260 $aIn: ENCONTRO DE INICIAÇÃO CIENTÍFICA, 14. ENCONTRO DE PÓS-GRADUANDOS DA EMBRAPA UVA E VINHO, 10., 2016, Bento Gonçalves. Resumos...Bento Gonçalves, RS: Embrapa uva e Vinho, 2016. p. 42.$c2016
500 $a(Embrapa Uva e Vinho. Documentos, 99)
520 $aA viticultura no Rio Grande do Sul faz uso de grande quantidade de fungicidas cúpricos, que ao se acumular no solo pode atingir níveis tóxicos às plantas. O gesso agrícola, subproduto das indústrias na produção de ácido fosfórico, é um resíduo abundante e alvo de estudo para reaproveitamento e descarte apropriado. O objetivo deste trabalho foi verificar o efeito do gesso na mitigação do cobre (Cu) na cultura da aveia e efeitos no solo.
650 $aÁcido Fosfórico
650 $aAveia
650 $aFitotoxicidade
650 $aFruticultura
650 $aFungo
650 $aSolo
650 $aUva
650 $aViticultura
653 $aAnais
653 $aCNPUV
653 $aCultura da aveia
653 $aFitotoxicidade de cobre
653 $aFitotoxicidade de cobre em aveia
653 $aFungicidas cúpricos
653 $aGesso agrícola
653 $aIC
653 $aIniciação cientifica
653 $aMitigação do cobre (Cu)
653 $aMitigação do cobre (Cu) na cultura da aveia
653 $aViticultura no Rio Grande do Sul
700 1 $aVIEIRA, J. L.
700 1 $aMORAIS NETO, J. A. de
700 1 $aFIORELLI, L. E.
700 1 $aSCANAGATTA, V.
700 1 $aZALAMENA, J.
700 1 $aMELO, G. W. B. de
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