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Registro Completo |
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Biblioteca(s): |
Embrapa Recursos Genéticos e Biotecnologia. |
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Data corrente: |
05/01/2007 |
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Data da última atualização: |
01/07/2022 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
PEREIRA, R. de A.; BATISTA, J. A. N.; SILVA, M. C. M. da; OLIVEIRA NETO, O. B. de; FIGUEIRA, E. L. Z.; VALENCIA JIMÉNEZ, A.; GROSSI-DE-SÁ, M. F. |
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Título: |
An alfa-amylase inhibitor gene from Phaseolus coccineus encodes a protein with potential for control of coffee berry borer (Hypothenemus hampei). |
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Ano de publicação: |
2006 |
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Fonte/Imprenta: |
Phytochemistry, v. 67, p. 2009-2016, 2006. |
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Idioma: |
Inglês |
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Palavras-Chave: |
Coffee berry borer; Enzimas digestivas. |
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Thesagro: |
Hypothenemus Hampei; Inseto; Phaseolus Coccineus; Praga de Planta. |
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Categoria do assunto: |
-- |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/178071/1/ID-27799-1.PDF
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Marc: |
LEADER 00837naa a2200253 a 4500
001 1188256
005 2022-07-01
008 2006 bl uuuu u00u1 u #d
100 1 $aPEREIRA, R. de A.
245 $aAn alfa-amylase inhibitor gene from Phaseolus coccineus encodes a protein with potential for control of coffee berry borer (Hypothenemus hampei).$h[electronic resource]
260 $c2006
650 $aHypothenemus Hampei
650 $aInseto
650 $aPhaseolus Coccineus
650 $aPraga de Planta
653 $aCoffee berry borer
653 $aEnzimas digestivas
700 1 $aBATISTA, J. A. N.
700 1 $aSILVA, M. C. M. da
700 1 $aOLIVEIRA NETO, O. B. de
700 1 $aFIGUEIRA, E. L. Z.
700 1 $aVALENCIA JIMÉNEZ, A.
700 1 $aGROSSI-DE-SÁ, M. F.
773 $tPhytochemistry$gv. 67, p. 2009-2016, 2006.
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Registro original: |
Embrapa Recursos Genéticos e Biotecnologia (CENARGEN) |
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Registro |
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URL |
Voltar
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 | Acesso ao texto completo restrito à biblioteca da Embrapa Agroindústria de Alimentos. Para informações adicionais entre em contato com ctaa.biblioteca@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Agroindústria de Alimentos. |
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Data corrente: |
09/01/2012 |
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Data da última atualização: |
30/11/2012 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
A - 1 |
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Autoria: |
FARINAS, C. S.; LOYO, M. M.; BARALDO JUNIOR, A.; TARDIOLI, P. W.; BERTUCCI NETO, V.; COURI, S. |
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Afiliação: |
CRISTIANE SANCHEZ FARINAS, CNPDIA; MARCEL MOITAS LOYO, CNPDIA; ANDERSON BARALDO JUNIOR, CNPDIA; PAULO W. TARDIOLI, UFSCAR; VICTOR BERTUCCI NETO, CNPDIA; SONIA COURI, CTAA. |
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Título: |
Finding stable cellulase and xylanase: evaluation of the synergistic effect of pH and temperature. |
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Ano de publicação: |
2010 |
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Fonte/Imprenta: |
New biotechnology, v. 27, n. 6, p. 810-815, Dec. 2010. |
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DOI: |
10.1016/j.nbt.2010.10.001 |
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Idioma: |
Inglês |
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Conteúdo: |
Ethanol fromlignocellulosic biomasshasbeenrecognizedasone of themost promising alternatives for the production of renewable and sustainable energy. However, one of the major bottlenecks holding back its commercialization is the high costs of the enzymes needed for biomass conversion. In this work, we studiedthe enzymesproducedfroma selectedstrainofAspergillusnigerunder solidstate fermentation.The cellulase and xylanase enzymatic cocktail was characterized in terms of pH and temperature by using response surface methodology. Thermostability and kinetic parameters were also determined. The statistical analysis ofpHand temperature effects on enzymatic activity showed a synergistic interaction of these two variables, thus enabling to find a pHand temperature range inwhich the enzymes have a higher activity. The results obtained allowed the construction of mathematical models used to predict endoglucanase, b-glucosidase and xylanase activities under different pH and temperature conditions. Optimumtemperature values for all three enzymes were found to be in the range between 358C and 608C, and the optimum pH range was found between 4 and 5.5. The methodology employed here was very effective in estimating enzyme behavior under different process conditions. |
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Palavras-Chave: |
Cellulase; Xylanase. |
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Thesagro: |
Enzima. |
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Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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Marc: |
LEADER 01922naa a2200229 a 4500
001 1912017
005 2012-11-30
008 2010 bl uuuu u00u1 u #d
024 7 $a10.1016/j.nbt.2010.10.001$2DOI
100 1 $aFARINAS, C. S.
245 $aFinding stable cellulase and xylanase$bevaluation of the synergistic effect of pH and temperature.
260 $c2010
520 $aEthanol fromlignocellulosic biomasshasbeenrecognizedasone of themost promising alternatives for the production of renewable and sustainable energy. However, one of the major bottlenecks holding back its commercialization is the high costs of the enzymes needed for biomass conversion. In this work, we studiedthe enzymesproducedfroma selectedstrainofAspergillusnigerunder solidstate fermentation.The cellulase and xylanase enzymatic cocktail was characterized in terms of pH and temperature by using response surface methodology. Thermostability and kinetic parameters were also determined. The statistical analysis ofpHand temperature effects on enzymatic activity showed a synergistic interaction of these two variables, thus enabling to find a pHand temperature range inwhich the enzymes have a higher activity. The results obtained allowed the construction of mathematical models used to predict endoglucanase, b-glucosidase and xylanase activities under different pH and temperature conditions. Optimumtemperature values for all three enzymes were found to be in the range between 358C and 608C, and the optimum pH range was found between 4 and 5.5. The methodology employed here was very effective in estimating enzyme behavior under different process conditions.
650 $aEnzima
653 $aCellulase
653 $aXylanase
700 1 $aLOYO, M. M.
700 1 $aBARALDO JUNIOR, A.
700 1 $aTARDIOLI, P. W.
700 1 $aBERTUCCI NETO, V.
700 1 $aCOURI, S.
773 $tNew biotechnology$gv. 27, n. 6, p. 810-815, Dec. 2010.
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Embrapa Agroindústria de Alimentos (CTAA) |
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