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| Registros recuperados : 5 | |
| Registros recuperados : 5 | |
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Registro Completo
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Biblioteca(s): |
Embrapa Agroenergia. |
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Data corrente: |
23/09/2019 |
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Data da última atualização: |
23/09/2019 |
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Tipo da produção científica: |
Artigo em Anais de Congresso |
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Autoria: |
GREGORINE, L. F.; MONCLARO, A. V.; SILVA, C. de O. G.; RODRIGUES, K. B.; PEIXOTO, J. S. G.; ABDELNUR, P. V.; FAVARO, L. C. de L. |
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Afiliação: |
Lucas F. Gregorine; Antonielle V. Monclaro; Caio de Oliveira Gorgulho Silva, Consultor da Embrapa Agroenergia; Kelly B. Rodrigues; Jéssica S. G. Peixoto, UnB; PATRICIA VERARDI ABDELNUR, CNPAE; LEIA CECILIA DE LIMA FAVARO, CNPAE. |
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Título: |
Heterologous expression of a new lytic polysaccharide monooxygenase from Hahella ganghwensis and their functional characterization. |
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Ano de publicação: |
2019 |
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Fonte/Imprenta: |
In: SIMPÓSIO NACIONAL DE BIOPROCESSOS, 22.; SIMPÓSIO DE HIDRÓLISE ENZIMÁTICA DE BIOMASSA, 13., 2019, Uberlandia, MG. [Anais ...]. São Paulo: Associação Brasileira de Engenharia Química, 2019. |
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Idioma: |
Inglês |
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Conteúdo: |
The powerful class of oxidative enzymes, lytic polysaccharide monooxygenases (LPMOs) - also named Auxiliary Activity (AA) - are able to oxidize recalcitrant polysaccharides on lignocellulosic biomass. In this work, we successfully expressed three catalytic domains from bacterial LPMOs in the yeast Komagataella phaffii: domain MdAA10.1-SD (from Moritella dasanensis), domain VmAA10.2-SD (from Verrucosispora maris), and domain HgAA10.1-SD (from Hahella ganghwensis). Heterologous expression was analyzed by SDS-PAGE, Western-Blot, and Dot-Blot, while functional activity of these proteins was investigated by a combination of mass spectrometric and chromatographic methods. The recombinant LPMO catalytic domain HgAA10.1-SD from H. ganghwensis, a C1-oxidizer, was able to promote an oxidative cleavage of phosphoric-acid swollen cellulose (PASC) substrate in the presence of ascorbic acid as an electron donor, showing its potential for cellulose depolymerization. |
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Palavras-Chave: |
Chromatographic; Spectrometric. |
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Categoria do assunto: |
-- |
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URL: |
https://www.alice.cnptia.embrapa.br/alice/bitstream/doc/1112393/1/107193786998fieldsubmissionfulltextfile1.pdf
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Marc: |
LEADER 01787nam a2200205 a 4500
001 2112393
005 2019-09-23
008 2019 bl uuuu u00u1 u #d
100 1 $aGREGORINE, L. F.
245 $aHeterologous expression of a new lytic polysaccharide monooxygenase from Hahella ganghwensis and their functional characterization.$h[electronic resource]
260 $aIn: SIMPÓSIO NACIONAL DE BIOPROCESSOS, 22.; SIMPÓSIO DE HIDRÓLISE ENZIMÁTICA DE BIOMASSA, 13., 2019, Uberlandia, MG. [Anais ...]. São Paulo: Associação Brasileira de Engenharia Química$c2019
520 $aThe powerful class of oxidative enzymes, lytic polysaccharide monooxygenases (LPMOs) - also named Auxiliary Activity (AA) - are able to oxidize recalcitrant polysaccharides on lignocellulosic biomass. In this work, we successfully expressed three catalytic domains from bacterial LPMOs in the yeast Komagataella phaffii: domain MdAA10.1-SD (from Moritella dasanensis), domain VmAA10.2-SD (from Verrucosispora maris), and domain HgAA10.1-SD (from Hahella ganghwensis). Heterologous expression was analyzed by SDS-PAGE, Western-Blot, and Dot-Blot, while functional activity of these proteins was investigated by a combination of mass spectrometric and chromatographic methods. The recombinant LPMO catalytic domain HgAA10.1-SD from H. ganghwensis, a C1-oxidizer, was able to promote an oxidative cleavage of phosphoric-acid swollen cellulose (PASC) substrate in the presence of ascorbic acid as an electron donor, showing its potential for cellulose depolymerization.
653 $aChromatographic
653 $aSpectrometric
700 1 $aMONCLARO, A. V.
700 1 $aSILVA, C. de O. G.
700 1 $aRODRIGUES, K. B.
700 1 $aPEIXOTO, J. S. G.
700 1 $aABDELNUR, P. V.
700 1 $aFAVARO, L. C. de L.
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Registro original: |
Embrapa Agroenergia (CNPAE) |
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