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Registro Completo |
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Biblioteca(s): |
Embrapa Florestas. |
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Data corrente: |
17/08/2015 |
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Data da última atualização: |
10/06/2016 |
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Autoria: |
SILVA S. A.; ZAPATA, B.; ESPINOZA T. C.; ÁVILA, G.; MURILLO GARCÍA, R.; LIENDO BUSTO, R.; ROJAS, W.; CADIMA, X.; VALOIS, A. C. C.; GOEDERT, C. de O.; VALLS, J. F. M.; FERREIRA, M. A. J. da F.; WETZEL, M. M. V. da S.; LOBO ARIAS, M.; VALENCIA R. R. A.; TAPIA, C.; ZAMBRANO, E.; PAREDES, N.; CARRILLO CASTILLO, F.; GARCÍA COCHAGNE, J.; RÍOS LOBO, L.; SIGUENAS SAAVEDRA, M.; POWER, I.; KANTEN, R. van; PÉREZ, D.; SÁNCHEZ, I.; GUITIÉRREZ, M.; MORROS, M. H.; CAMACARO, N. |
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Título: |
Recursos fitogenéticos en los trópicos suramericanos: Bolívia, Brasil, Colombia, Ecuador, Perú, Surinam, Venezuela. |
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Ano de publicação: |
2010 |
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Fonte/Imprenta: |
Brasília, DF: PROCITROPICOS: IICA, 2010. |
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Páginas: |
367 p. |
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Descrição Física: |
il., color. |
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Idioma: |
Espanhol |
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Notas: |
Programa Cooperativo de Investigación, Desarrollo e Innovación Agrícola para los Trópicos Suramericanos - PROCITROPICOS/IICA. |
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Conteúdo: |
Recursos fitogenéticos en Bolivia; Recursos fitogenéticos en Brasil; Recursos fitogenéticos en Colombia; Recursos fitogenéticos en Ecuador; Recursos fitogenéticos en Perú; Recursos fitogenéticos en Surinam; Recursos fitogenéticos en Venezuela. |
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Palavras-Chave: |
Agrobiodiversidade; América do Sul; Recurso genético vegetal; Recursos genéticos vegetais. |
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Thesagro: |
Germoplasma. |
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Thesaurus Nal: |
Amazonia. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 01882nam a2200541 a 4500
001 2022100
005 2016-06-10
008 2010 bl uuuu u00u1 u #d
100 1 $aSILVA S. A.
245 $aRecursos fitogenéticos en los trópicos suramericanos$bBolívia, Brasil, Colombia, Ecuador, Perú, Surinam, Venezuela.
260 $aBrasília, DF: PROCITROPICOS: IICA$c2010
300 $a367 p.$cil., color.
500 $aPrograma Cooperativo de Investigación, Desarrollo e Innovación Agrícola para los Trópicos Suramericanos - PROCITROPICOS/IICA.
520 $aRecursos fitogenéticos en Bolivia; Recursos fitogenéticos en Brasil; Recursos fitogenéticos en Colombia; Recursos fitogenéticos en Ecuador; Recursos fitogenéticos en Perú; Recursos fitogenéticos en Surinam; Recursos fitogenéticos en Venezuela.
650 $aAmazonia
650 $aGermoplasma
653 $aAgrobiodiversidade
653 $aAmérica do Sul
653 $aRecurso genético vegetal
653 $aRecursos genéticos vegetais
700 1 $aZAPATA, B.
700 1 $aESPINOZA T. C.
700 1 $aÁVILA, G.
700 1 $aMURILLO GARCÍA, R.
700 1 $aLIENDO BUSTO, R.
700 1 $aROJAS, W.
700 1 $aCADIMA, X.
700 1 $aVALOIS, A. C. C.
700 1 $aGOEDERT, C. de O.
700 1 $aVALLS, J. F. M.
700 1 $aFERREIRA, M. A. J. da F.
700 1 $aWETZEL, M. M. V. da S.
700 1 $aLOBO ARIAS, M.
700 1 $aVALENCIA R. R. A.
700 1 $aTAPIA, C.
700 1 $aZAMBRANO, E.
700 1 $aPAREDES, N.
700 1 $aCARRILLO CASTILLO, F.
700 1 $aGARCÍA COCHAGNE, J.
700 1 $aRÍOS LOBO, L.
700 1 $aSIGUENAS SAAVEDRA, M.
700 1 $aPOWER, I.
700 1 $aKANTEN, R. van
700 1 $aPÉREZ, D.
700 1 $aSÁNCHEZ, I.
700 1 $aGUITIÉRREZ, M.
700 1 $aMORROS, M. H.
700 1 $aCAMACARO, N.
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Registro original: |
Embrapa Florestas (CNPF) |
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 | Acesso ao texto completo restrito à biblioteca da Embrapa Instrumentação. Para informações adicionais entre em contato com cnpdia.biblioteca@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Instrumentação. |
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Data corrente: |
23/03/2022 |
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Data da última atualização: |
24/06/2022 |
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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: |
PINOTTI, L. M.; TARDIOLI, P. W.; FARINAS, C. S.; FERNÁNDEZ-LORENTE, G.; ORREGO, A. H.; GUISAN, J. M.; PESSELA, B. C. |
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Afiliação: |
CRISTIANE SANCHEZ FARINAS, CNPDIA. |
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Título: |
Stabilization of glycosylated ?-glucosidase by intramolecular crosslinking between oxidized glycosidic chains and lysine residues. |
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Ano de publicação: |
2022 |
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Fonte/Imprenta: |
Applied Biochemistry and Biotechnology, v. 192, 2020. |
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Páginas: |
325?337 |
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DOI: |
https://doi.org/10.1007/s12010-020-03321-x |
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Idioma: |
Inglês |
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Conteúdo: |
Many industrial enzymes can be highly glycosylated, including the β-glucosidase enzymes. Although glycosylation plays an important role in many biological processes, such chains can cause problems in the multipoint immobilization techniques of the enzymes, since the glycosylated chains can cover the reactive groups of the protein (e.g., Lys) and do not allow those groups to react with reactive groups of the support (e.g., aldehyde and epoxy groups). Nevertheless, the activated glycosylated chains can be used as excellent crosslinking agents. The glycosylated chains when oxidized with periodate can generate aldehyde groups capable of reacting with the amino groups of the protein itself. Such intramolecular crosslinks may have significant stabilizing effects. In this study, we investigated if the intramolecular crosslinking occurs in the oxidized βglucosidase and its effect on the stability of the enzyme. For this, the oxidation of glycosidic chains of β-glucosidase was carried out, allowing to demonstrate the formation of aldehyde groups and subsequent interaction with the amine groups and to verify the stability of the different forms of free enzyme (glycosylated and oxidized). Furthermore, we verified the influence of the glycosidic chains on the immobilization of β-glucosidase from Aspergillus niger and on the consequent stabilization. The results suggest that intramolecular crosslinking occurred and consequently the oxidized enzyme showed a much greater stabilization than the native enzyme (glycosylated). When the multipoint immobilization was performed in amino-epoxy-agarose supports, the stabilization of the oxidized enzyme increases by a 6-fold factor. The overall stabilization strategy was capable to promote an enzyme stabilization of 120-fold regarding to the soluble unmodified enzyme. MenosMany industrial enzymes can be highly glycosylated, including the β-glucosidase enzymes. Although glycosylation plays an important role in many biological processes, such chains can cause problems in the multipoint immobilization techniques of the enzymes, since the glycosylated chains can cover the reactive groups of the protein (e.g., Lys) and do not allow those groups to react with reactive groups of the support (e.g., aldehyde and epoxy groups). Nevertheless, the activated glycosylated chains can be used as excellent crosslinking agents. The glycosylated chains when oxidized with periodate can generate aldehyde groups capable of reacting with the amino groups of the protein itself. Such intramolecular crosslinks may have significant stabilizing effects. In this study, we investigated if the intramolecular crosslinking occurs in the oxidized βglucosidase and its effect on the stability of the enzyme. For this, the oxidation of glycosidic chains of β-glucosidase was carried out, allowing to demonstrate the formation of aldehyde groups and subsequent interaction with the amine groups and to verify the stability of the different forms of free enzyme (glycosylated and oxidized). Furthermore, we verified the influence of the glycosidic chains on the immobilization of β-glucosidase from Aspergillus niger and on the consequent stabilization. The results suggest that intramolecular crosslinking occurred and consequently the oxidized enzyme showed a much greater stabilization than... Mostrar Tudo |
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Palavras-Chave: |
Immobilization; Stabilization enzymes. |
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Categoria do assunto: |
-- |
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Marc: |
LEADER 02609naa a2200241 a 4500
001 2141186
005 2022-06-24
008 2022 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.1007/s12010-020-03321-x$2DOI
100 1 $aPINOTTI, L. M.
245 $aStabilization of glycosylated ?-glucosidase by intramolecular crosslinking between oxidized glycosidic chains and lysine residues.$h[electronic resource]
260 $c2022
300 $a325?337
520 $aMany industrial enzymes can be highly glycosylated, including the β-glucosidase enzymes. Although glycosylation plays an important role in many biological processes, such chains can cause problems in the multipoint immobilization techniques of the enzymes, since the glycosylated chains can cover the reactive groups of the protein (e.g., Lys) and do not allow those groups to react with reactive groups of the support (e.g., aldehyde and epoxy groups). Nevertheless, the activated glycosylated chains can be used as excellent crosslinking agents. The glycosylated chains when oxidized with periodate can generate aldehyde groups capable of reacting with the amino groups of the protein itself. Such intramolecular crosslinks may have significant stabilizing effects. In this study, we investigated if the intramolecular crosslinking occurs in the oxidized βglucosidase and its effect on the stability of the enzyme. For this, the oxidation of glycosidic chains of β-glucosidase was carried out, allowing to demonstrate the formation of aldehyde groups and subsequent interaction with the amine groups and to verify the stability of the different forms of free enzyme (glycosylated and oxidized). Furthermore, we verified the influence of the glycosidic chains on the immobilization of β-glucosidase from Aspergillus niger and on the consequent stabilization. The results suggest that intramolecular crosslinking occurred and consequently the oxidized enzyme showed a much greater stabilization than the native enzyme (glycosylated). When the multipoint immobilization was performed in amino-epoxy-agarose supports, the stabilization of the oxidized enzyme increases by a 6-fold factor. The overall stabilization strategy was capable to promote an enzyme stabilization of 120-fold regarding to the soluble unmodified enzyme.
653 $aImmobilization
653 $aStabilization enzymes
700 1 $aTARDIOLI, P. W.
700 1 $aFARINAS, C. S.
700 1 $aFERNÁNDEZ-LORENTE, G.
700 1 $aORREGO, A. H.
700 1 $aGUISAN, J. M.
700 1 $aPESSELA, B. C.
773 $tApplied Biochemistry and Biotechnology$gv. 192, 2020.
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