|
|
![](/consulta/web/img/deny.png) | Acesso ao texto completo restrito à biblioteca da Embrapa Instrumentação. Para informações adicionais entre em contato com cnpdia.biblioteca@embrapa.br. |
Registro Completo |
Biblioteca(s): |
Embrapa Instrumentação. |
Data corrente: |
23/03/2022 |
Data da última atualização: |
24/06/2022 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Autoria: |
PINOTTI, L. M.; TARDIOLI, P. W.; FARINAS, C. S.; FERNÁNDEZ-LORENTE, G.; ORREGO, A. H.; GUISAN, J. M.; PESSELA, B. C. |
Afiliação: |
CRISTIANE SANCHEZ FARINAS, CNPDIA. |
Título: |
Stabilization of glycosylated ß-glucosidase by intramolecular crosslinking between oxidized glycosidic chains and lysine residues. |
Ano de publicação: |
2022 |
Fonte/Imprenta: |
Applied Biochemistry and Biotechnology, v. 192, 2020. |
Páginas: |
325?337 |
DOI: |
https://doi.org/10.1007/s12010-020-03321-x |
Idioma: |
Inglês |
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 |
Palavras-Chave: |
Immobilization; Stabilization enzymes. |
Categoria do assunto: |
-- |
Marc: |
LEADER 02610naa 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 $aStabilization of glycosylated ß-glucosidase by intramolecular crosslinking between oxidized glycosidic chains and lysine residues.$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.
Download
Esconder MarcMostrar Marc Completo |
Registro original: |
Embrapa Instrumentação (CNPDIA) |
|
Biblioteca |
ID |
Origem |
Tipo/Formato |
Classificação |
Cutter |
Registro |
Volume |
Status |
URL |
Voltar
|
|
Registros recuperados : 9 | |
1. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | CARVALHO, G. M. C.; BEFFA, L. M.; ALMEIDA, M. J. O.; SILVA, L. R. F. da. Caracterização fenotípica de três rebanhos bovinos da raça Pé-duro em ambientes distintos do Piauí. In: SIMPÓSIO BRASILEIRO DE RECURSOS GENÉTICOS, 2., 2008, Brasília, DF. Anais... Brasília, DF: Embrapa Recursos Genéticos e Biotecnologia, 2008. p. 504Tipo: Resumo em Anais de Congresso |
Biblioteca(s): Embrapa Meio-Norte. |
| ![Visualizar detalhes do registro](/consulta/web/img/visualizar.png) ![Imprime registro no formato completo](/consulta/web/img/print.png) |
2. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | CARVALHO, G. M. C.; MACIEL, G. A.; ALMEIDA, M. J. de O.; SILVA, L. R. F. da. Avaliação de características fenotípicas de pelagens em bovinos da raça Pé-Duro (Bos taurus taurus). In: CONGRESSO BRASILEIRO DE RECURSOS GENÉTICOS; WORKSHOP EM BIOPROSPECÇÃO E CONSERVAÇÃO DE PLANTAS NATIVAS DO SEMI-ÁRIDO, 3.; WORKSHOP INTERNACIONAL SOBRE BIOENERGIA E MEIO AMBIENTE, 2010, Salvador. Bancos de germoplasma: descobrir a riqueza, garantir o futuro: anais. Brasília, DF: Embrapa Recursos Genéticos e Biotecnologia, 2010. Ref. Animais. p. 15 1 CD-ROM. (Embrapa Recursos Genéticos e Biotecnologia. Documentos, 304).Tipo: Resumo em Anais de Congresso |
Biblioteca(s): Embrapa Meio-Norte. |
| ![Visualizar detalhes do registro](/consulta/web/img/visualizar.png) ![Acesso ao objeto digital](/consulta/web/img/pdf.png) ![Imprime registro no formato completo](/consulta/web/img/print.png) |
3. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | CARVALHO, G. M. C.; AZEVEDO, D. M. M. R.; ALMEIDA, M. J. de O.; SILVA, L. R. F. da. Avaliação do desenvolvimento ponderal de bovinos da raça Pé-Duro (Bos taurus taurus), Nelore (Bos taurus indicus) e de seus mestiços F1. In: CONGRESSO BRASILEIRO DE RECURSOS GENÉTICOS; WORKSHOP EM BIOPROSPECÇÃO E CONSERVAÇÃO DE PLANTAS NATIVAS DO SEMI-ÁRIDO, 3.; WORKSHOP INTERNACIONAL SOBRE BIOENERGIA E MEIO AMBIENTE, 2010, Salvador. Bancos de germoplasma: descobrir a riqueza, garantir o futuro: anais. Brasília, DF: Embrapa Recursos Genéticos e Biotecnologia, 2010. Ref. Animais. p. 50 1 CD-ROM. (Embrapa Recursos Genéticos e Biotecnologia. Documentos, 304).Tipo: Resumo em Anais de Congresso |
Biblioteca(s): Embrapa Meio-Norte. |
| ![Visualizar detalhes do registro](/consulta/web/img/visualizar.png) ![Acesso ao objeto digital](/consulta/web/img/pdf.png) ![Imprime registro no formato completo](/consulta/web/img/print.png) |
4. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | SILVA, L. R. F. da; ALVES, A. A.; VASCONCELOS, V. R.; NASCIMENTO, H. T. S. do; MOREIRA FILHO, M. A. Nutritive value of diets containing pods of faveira (Parkia platycephala Benth.) for confined finishing sheep. Revista Brasileira de Zootecnia, Viçosa, MG, v. 41, n. 4, p. 1065-1069, 2012.Tipo: Artigo em Periódico Indexado | Circulação/Nível: B - 1 |
Biblioteca(s): Embrapa Meio-Norte. |
| ![Visualizar detalhes do registro](/consulta/web/img/visualizar.png) ![Acesso ao objeto digital](/consulta/web/img/pdf.png) ![Imprime registro no formato completo](/consulta/web/img/print.png) |
5. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | AZAR, G. S.; COSTA, J. V.; SILVA, L. R. F. da; RODRIGUES, M. M.; OLIVEIRA, M. E. de; AZEVEDO, D. M. M. R. Características do pasto de capim-marandu irrigado sob sistemas de monocultura e silvipastoril em duas condições de pastejo. In: REUNIÃO ANUAL DA SOCIEDADE BRASILEIRA DE ZOOTECNIA, 48., 2011, Belém, PA. O desenvolvimento da produção animal e a responsabilidade frente a novos desafios: anais. Belém, PA: SBZ, 2011. 1 CD-ROM.Tipo: Artigo em Anais de Congresso |
Biblioteca(s): Embrapa Meio-Norte. |
| ![Visualizar detalhes do registro](/consulta/web/img/visualizar.png) ![Acesso ao objeto digital](/consulta/web/img/pdf.png) ![Imprime registro no formato completo](/consulta/web/img/print.png) |
6. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | CARVALHO, G. M. C.; ALMEIDA, M. J. de O.; LEAL, J. A.; SALES, F. S. M.; SILVA, L. R. F. da. Características fenotípicas del ganado curraleiro del Brasil. In: SIMPOSIO DE RECURSOS GENÉTICOS PARA AMÉRICA LATINA Y EL CARIBE, SIRGEALC, 5., 2005, Montevideo, Uruguay. Resúmenes... Montevideo: Instituto Nacional de Investigación Agropecuaria: Universidad de la República, Facultad de Agronomía, 2005. n. 311, p. 106.Tipo: Resumo em Anais de Congresso |
Biblioteca(s): Embrapa Meio-Norte. |
| ![Visualizar detalhes do registro](/consulta/web/img/visualizar.png) ![Acesso ao objeto digital](/consulta/web/img/pdf.png) ![Imprime registro no formato completo](/consulta/web/img/print.png) |
7. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | ALVES, A. A.; SALES, R. de O.; NEIVA, J. N. M.; MEDEIROS, A. N.; BRAGA, A. P.; AZEVEDO, D. M. M. R.; SILVA, L. R. F. da. Metabolismo de compostos nitrogenados em ovinos alimentados com dietas contendo vagens de faveira. Revista Brasileira de Saúde e Produção Animal, Salvador, v. 12, n. 4, p. 1051-1066, out./dez 2011. 1519-9940Tipo: Artigo em Periódico Indexado | Circulação/Nível: B - 3 |
Biblioteca(s): Embrapa Meio-Norte. |
| ![Visualizar detalhes do registro](/consulta/web/img/visualizar.png) ![Acesso ao objeto digital](/consulta/web/img/pdf.png) ![Imprime registro no formato completo](/consulta/web/img/print.png) |
8. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | LOPES, L. D; SILVA, L. R. F, da; ROMAGNOLI, E. M; FERREIRA, C.; TAKETANI, R. G.; ABDALLA, A. L.; LOUVANDINI, H.; MENDES, R. Metagenomics of sheep rumen microbiome under two diet. XXI ALAM Congresso Latinoamericano de Microbiologia, Santos-Brasil 28/10/12 a 01/11/2012.Tipo: Resumo em Anais de Congresso |
Biblioteca(s): Embrapa Meio Ambiente. |
| ![Visualizar detalhes do registro](/consulta/web/img/visualizar.png) ![Acesso ao objeto digital](/consulta/web/img/pdf.png) ![Imprime registro no formato completo](/consulta/web/img/print.png) |
9. | ![Imagem marcado/desmarcado](/consulta/web/img/desmarcado.png) | ROMAGNOLI, E. M; LOPES, L. D.; SILVA, L. R. F, da; NAKAMURA, F. M; SBARDELLA, M.; PEREIRA, R.; SILVA, W. D.; TSAI, S. M.; ANDREOTE, F. D.; MENDES, R. Quantification of Archaea and bacteria domains in the sheep rumen incubated under two diet conditions. The International Sodety for Microblal EcoJogy(ISME), organlzer of the 14th International SympoSium on Microblal Eco!ogy (ISME14 )in Copenhagen, Denmark, from 19 - 24 August 2012.Tipo: Resumo em Anais de Congresso |
Biblioteca(s): Embrapa Meio Ambiente. |
| ![Visualizar detalhes do registro](/consulta/web/img/visualizar.png) ![Acesso ao objeto digital](/consulta/web/img/pdf.png) ![Imprime registro no formato completo](/consulta/web/img/print.png) |
Registros recuperados : 9 | |
|
Nenhum registro encontrado para a expressão de busca informada. |
|
|