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 | Acesso ao texto completo restrito à biblioteca da Embrapa Agroenergia. Para informações adicionais entre em contato com cnpae.biblioteca@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Agroenergia. |
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Data corrente: |
05/11/2020 |
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Data da última atualização: |
06/11/2020 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
LIMA, R. A. T.; OLIVEIRA, G. d.; SOUZA, A. A.; LOPES, F. A. C.; SANTANA, R. H.; ISTVAN, P.; QUIRINO, B. F.; BARBOSA, J.; FREITAS, S. d.; GARAY, A. V.; KRUGER, R. H. |
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Afiliação: |
Raul Alcântara Teixeira Lima, Universidade de Brasília; Gideane de Oliveira, Universidade de Brasília; Amanda Araújo Souza, Universidade de Brasília; Fabyano Alvares Cardoso Lopes, Universidade Federal do Tocantins; Renata Henrique Santana, Instituto Federal de Brasília; Paula Istvan, Universidade de Brasília; BETANIA FERRAZ QUIRINO, CNPAE; João Barbosa, Universidade de Brasília; Sônia de Freitas, Universidade de Brasília; Aisel Valle Garay, Universidade de Brasília; Ricardo Henrique Kruger, Universidade de Brasília. |
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Título: |
Functional and structural characterization of a novel GH3 Beta-glucosidase from the gut metagenome of the Brazilian Cerrado termite Syntermes wheeleri. |
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Ano de publicação: |
2020 |
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Fonte/Imprenta: |
International Journal of Biological Macromolecules, v. 165, Part A, p. 822-834, Dec. 2020. |
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Volume: |
165 |
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DOI: |
https://doi.org/10.1016/j.ijbiomac.2020.09.236 |
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Idioma: |
Inglês |
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Conteúdo: |
In this study, a GH3 family Beta-glucosidase (Bgl7226) from metagenomic sequences of the Syntermes wheeleri gut, a Brazilian Cerrado termite, was expressed, purified and characterized. The enzyme showed two optimum pHs (pH 7 and pH 10), and a maximum optimum temperature of about 40 °C using 4-Nitrophenyl ?-D-glucopyranoside (pNPG) as substrate. Bgl7226 showed higher enzymatic activity at basic pH, but higher affinity (Km) at neutral pH. However, at neutral pH the Bgl7226 enzyme showed higher catalytic efficiency (kcat/Km) for pNPG substrate. Predictive analysis about the enzyme structure-function relationship by sequence alignment suggested the presence of multi-domains and conserved catalytic sites. Circular dichroism results showed that the secondary structure composition of the enzyme is pH-dependent. Small conformational changes occurred close to the optimum temperature of 40 o C, and seem important for the highest activity of Bgl7226 observed at pH 7 and 10. In addition, the small transition in the unfolding curves close to 40 o C is typical of intermediates associated with proteins structured in several domains. Bgl7226 has significant Beta-glucosidase activity which could be attractive for biotechnological applications, such as plant roots detoxification; specifically, our group is interested in cassava roots (Manihot esculenta) detoxification. |
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Palavras-Chave: |
Genômica ambiental. |
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Thesagro: |
Cerrado; Enzima; RNA. |
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Thesaurus NAL: |
Beta-glucosidase; Metagenomics. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 02436naa a2200349 a 4500
001 2126334
005 2020-11-06
008 2020 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.1016/j.ijbiomac.2020.09.236$2DOI
100 1 $aLIMA, R. A. T.
245 $aFunctional and structural characterization of a novel GH3 Beta-glucosidase from the gut metagenome of the Brazilian Cerrado termite Syntermes wheeleri.$h[electronic resource]
260 $c2020
300 $a165
490 $v165
520 $aIn this study, a GH3 family Beta-glucosidase (Bgl7226) from metagenomic sequences of the Syntermes wheeleri gut, a Brazilian Cerrado termite, was expressed, purified and characterized. The enzyme showed two optimum pHs (pH 7 and pH 10), and a maximum optimum temperature of about 40 °C using 4-Nitrophenyl ?-D-glucopyranoside (pNPG) as substrate. Bgl7226 showed higher enzymatic activity at basic pH, but higher affinity (Km) at neutral pH. However, at neutral pH the Bgl7226 enzyme showed higher catalytic efficiency (kcat/Km) for pNPG substrate. Predictive analysis about the enzyme structure-function relationship by sequence alignment suggested the presence of multi-domains and conserved catalytic sites. Circular dichroism results showed that the secondary structure composition of the enzyme is pH-dependent. Small conformational changes occurred close to the optimum temperature of 40 o C, and seem important for the highest activity of Bgl7226 observed at pH 7 and 10. In addition, the small transition in the unfolding curves close to 40 o C is typical of intermediates associated with proteins structured in several domains. Bgl7226 has significant Beta-glucosidase activity which could be attractive for biotechnological applications, such as plant roots detoxification; specifically, our group is interested in cassava roots (Manihot esculenta) detoxification.
650 $aBeta-glucosidase
650 $aMetagenomics
650 $aCerrado
650 $aEnzima
650 $aRNA
653 $aGenômica ambiental
700 1 $aOLIVEIRA, G. d.
700 1 $aSOUZA, A. A.
700 1 $aLOPES, F. A. C.
700 1 $aSANTANA, R. H.
700 1 $aISTVAN, P.
700 1 $aQUIRINO, B. F.
700 1 $aBARBOSA, J.
700 1 $aFREITAS, S. d.
700 1 $aGARAY, A. V.
700 1 $aKRUGER, R. H.
773 $tInternational Journal of Biological Macromolecules$gv. 165, Part A, p. 822-834, Dec. 2020.
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