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 | Acesso ao texto completo restrito à biblioteca da Embrapa Meio Ambiente. Para informações adicionais entre em contato com cnpma.biblioteca@embrapa.br. |
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Registro Completo |
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Biblioteca(s): |
Embrapa Meio Ambiente. |
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Data corrente: |
22/12/2021 |
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Data da última atualização: |
23/12/2021 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
SILVEIRA, M. A. V.; SANTOS, S. M. B. dos; OKAMOTO, D. N.; MELO, I. S. de; JULIANO, M. A.; CHAGAS, J. R.; VASCONCELLOS, S. P. |
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Afiliação: |
MARGHUEL APARECIDA VIEIRA SILVEIRA, EPM-UNIFESP; SAARA M BATISTA DOS SANTOS, EPM-UNIFESP; DÉBORA NOMA OKAMOTO, Instituto de Ciências Ambientais, Químicas e Farmacêuticas - UNIFESP; ITAMAR SOARES DE MELO, CNPMA; MARIA A JULIANO; JAIR RIBEIRO CHAGAS, EPM-UNIFESP; SUZAN P VASCONCELLOS, EPM-UNIFESP. |
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Título: |
Atlantic Forest's and Caatinga's semiarid soils and their potential as a source for halothermotolerant actinomycetes and proteolytic enzymes. |
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Ano de publicação: |
2021 |
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Fonte/Imprenta: |
Environmental Technology, 2021. |
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ISSN: |
0959-3330 |
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DOI: |
https://doi.org/10.1080/09593330.2021.2008015 |
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Idioma: |
Inglês |
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Notas: |
On-line first |
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Conteúdo: |
Abstract: Actinomycetes are versatile about their metabolism, displaying high capacity to produce bioactive metabolites. Enzymes from actinomycetes represent new opportunities for industrial applications. However, proteases from actinomycetes are poorly described by literature. Thereby, to verify proteolytic potential of actinomycetes, the present study aimed the investigation of bacterial isolates from Caatinga and Atlantic Forest rhizosphere. Fluorescence resonance energy transfer (FRET) peptide libraries were adopted for the evaluations, since they are faster and more qualitative methods, if compared with others described by most reports. A total of 52 microorganisms were inoculated in different culture media (PMB, potato dextrose agar, brain heart infusion agar, Starch Casein Agar and Reasoner's 2A agar), temperatures (12, 20, 30, 37, 45 and 60°C), and saline conditions (0-4 M NaCl), during 7 days. The actinomycetes named as AC 01, 02 and 52 were selected and showed enzymatic abilities under the peptide probes Abz-KLRSSKQ-EDDnp and Abz-KLYSSKQ-EDDnp, achieving enhanced performance at 30 °C. Biochemical parameters were established, showing a predominance of alkaline proteases with activity under saline conditions. Secreted proteases hydrolysed preferentially polar uncharged residues (Y and N) and positively charged groups (R). Phenylmethylsulfonyl fluoride and ethylenediaminetetraacetic acid inhibited the proteins, a characteristic of serine (AC 01 e 02) and metalloproteases (AC 52). All selected strains belonged to Streptomyces genera. In summary, actinomycete strains with halophilic proteolytic abilities were selected, which improve possibilities for their use in detergent formulations, food processing, waste management and industrial bioconversion. It is important to highlight that this is the first report using FRET libraries for proteolytic screening from Caatinga and Atlantic Forest actinobacteria. MenosAbstract: Actinomycetes are versatile about their metabolism, displaying high capacity to produce bioactive metabolites. Enzymes from actinomycetes represent new opportunities for industrial applications. However, proteases from actinomycetes are poorly described by literature. Thereby, to verify proteolytic potential of actinomycetes, the present study aimed the investigation of bacterial isolates from Caatinga and Atlantic Forest rhizosphere. Fluorescence resonance energy transfer (FRET) peptide libraries were adopted for the evaluations, since they are faster and more qualitative methods, if compared with others described by most reports. A total of 52 microorganisms were inoculated in different culture media (PMB, potato dextrose agar, brain heart infusion agar, Starch Casein Agar and Reasoner's 2A agar), temperatures (12, 20, 30, 37, 45 and 60°C), and saline conditions (0-4 M NaCl), during 7 days. The actinomycetes named as AC 01, 02 and 52 were selected and showed enzymatic abilities under the peptide probes Abz-KLRSSKQ-EDDnp and Abz-KLYSSKQ-EDDnp, achieving enhanced performance at 30 °C. Biochemical parameters were established, showing a predominance of alkaline proteases with activity under saline conditions. Secreted proteases hydrolysed preferentially polar uncharged residues (Y and N) and positively charged groups (R). Phenylmethylsulfonyl fluoride and ethylenediaminetetraacetic acid inhibited the proteins, a characteristic of serine (AC 01 e 02) and metalloprotea... Mostrar Tudo |
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Palavras-Chave: |
FRET peptide; Metalloprotease. |
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Thesagro: |
Actinomiceto; Cerrado; Rizosfera; Solo. |
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Thesaurus Nal: |
Cerrado soils; Peptides; Proteolytic bacteria; Rhizosphere; Serine. |
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Categoria do assunto: |
P Recursos Naturais, Ciências Ambientais e da Terra |
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Marc: |
LEADER 02989naa a2200361 a 4500
001 2138282
005 2021-12-23
008 2021 bl uuuu u00u1 u #d
022 $a0959-3330
024 7 $ahttps://doi.org/10.1080/09593330.2021.2008015$2DOI
100 1 $aSILVEIRA, M. A. V.
245 $aAtlantic Forest's and Caatinga's semiarid soils and their potential as a source for halothermotolerant actinomycetes and proteolytic enzymes.$h[electronic resource]
260 $c2021
500 $aOn-line first
520 $aAbstract: Actinomycetes are versatile about their metabolism, displaying high capacity to produce bioactive metabolites. Enzymes from actinomycetes represent new opportunities for industrial applications. However, proteases from actinomycetes are poorly described by literature. Thereby, to verify proteolytic potential of actinomycetes, the present study aimed the investigation of bacterial isolates from Caatinga and Atlantic Forest rhizosphere. Fluorescence resonance energy transfer (FRET) peptide libraries were adopted for the evaluations, since they are faster and more qualitative methods, if compared with others described by most reports. A total of 52 microorganisms were inoculated in different culture media (PMB, potato dextrose agar, brain heart infusion agar, Starch Casein Agar and Reasoner's 2A agar), temperatures (12, 20, 30, 37, 45 and 60°C), and saline conditions (0-4 M NaCl), during 7 days. The actinomycetes named as AC 01, 02 and 52 were selected and showed enzymatic abilities under the peptide probes Abz-KLRSSKQ-EDDnp and Abz-KLYSSKQ-EDDnp, achieving enhanced performance at 30 °C. Biochemical parameters were established, showing a predominance of alkaline proteases with activity under saline conditions. Secreted proteases hydrolysed preferentially polar uncharged residues (Y and N) and positively charged groups (R). Phenylmethylsulfonyl fluoride and ethylenediaminetetraacetic acid inhibited the proteins, a characteristic of serine (AC 01 e 02) and metalloproteases (AC 52). All selected strains belonged to Streptomyces genera. In summary, actinomycete strains with halophilic proteolytic abilities were selected, which improve possibilities for their use in detergent formulations, food processing, waste management and industrial bioconversion. It is important to highlight that this is the first report using FRET libraries for proteolytic screening from Caatinga and Atlantic Forest actinobacteria.
650 $aCerrado soils
650 $aPeptides
650 $aProteolytic bacteria
650 $aRhizosphere
650 $aSerine
650 $aActinomiceto
650 $aCerrado
650 $aRizosfera
650 $aSolo
653 $aFRET peptide
653 $aMetalloprotease
700 1 $aSANTOS, S. M. B. dos
700 1 $aOKAMOTO, D. N.
700 1 $aMELO, I. S. de
700 1 $aJULIANO, M. A.
700 1 $aCHAGAS, J. R.
700 1 $aVASCONCELLOS, S. P.
773 $tEnvironmental Technology, 2021.
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Registro original: |
Embrapa Meio Ambiente (CNPMA) |
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| Registros recuperados : 188 | |
| 3. |  | MARTINS-DA-SILVA, R. C. V. Eperua Aubl. In: FORZZA, R. C.; BAUMGRATZ, J. F. A.; BICUDO, C. E. M.; CARVALHO JÚNIOR, A. A.; COSTA, A.; COSTA, D. P.; HOPKINS, M.; LEITMAN, P. M.; LOHMANN, L. G.; MAIA, L. C.; MARTINELLI, G.; MENEZES, M.; MORIM, M. P.; COELHO, M. A. N.; PEIXOTO, A. L.; PIRANI, J. R.; PRADO, J.; QUEIROZ, L. P.; SOUZA, V. C.; STEHMANN, J. R.; SYLVESTRE, L. S.; WALTER, B. M. T.; ZAPPI, D. (Ed.). Catálogo de plantas e fungos do Brasil. Rio de Janeiro: Andrea Jakobsson Estúdio: Instituto de Pesquisas Jardim Botânico do Rio de Janeiro, 2010. v. 2, p. 1035.| Biblioteca(s): Embrapa Amazônia Oriental. |
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| 5. | | MARTINS-DA-SILVA, R. C. V. Heterostemon Desf. In: FORZZA, R. C.; BAUMGRATZ, J. F. A.; BICUDO, C. E. M.; CARVALHO JÚNIOR, A. A.; COSTA, A.; COSTA, D. P.; HOPKINS, M.; LEITMAN, P. M.; LOHMANN, L. G.; MAIA, L. C.; MARTINELLI, G.; MENEZES, M.; MORIM, M. P.; COELHO, M. A. N.; PEIXOTO, A. L.; PIRANI, J. R.; PRADO, J.; QUEIROZ, L. P.; SOUZA, V. C.; STEHMANN, J. R.; SYLVESTRE, L. S.; WALTER, B. M. T.; ZAPPI, D. (Ed.). Catálogo de plantas e fungos do Brasil. Rio de Janeiro: Andrea Jakobsson Estúdio: Instituto de Pesquisas Jardim Botânico do Rio de Janeiro, 2010. v. 2, p. 1039-1040.| Biblioteca(s): Embrapa Amazônia Oriental. |
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| 13. | | FERREIRA, G. C.; MARTINS-DA-SILVA, R. C. V. Informatização da família Vochysiaceae do Herbário IAN, da Embrapa Amazônia Oriental, Belém, PA. In: REUNIÃO DOS BOTÂNICOS DA AMAZÔNIA, 2., 1997, Salinópolis, PA. Programas e resumos Belém, PA: Sociedade Botânica do Brasil-Seccional da Amazônia: MPEG, 1997. p. 18.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Amazônia Oriental. |
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| 14. | | FERREIRA, G. C.; MARTINS-DA-SILVA, R. C. V. Informatização da familia Vochysiaceae do Herbário IAN, da Embrapa Amazônia Oriental, Belém, PA. In: SIMPÓSIO SILVICULTURA NA AMAZÔNIA ORIENTAL: contribuições do Projeto Embrapa/DFID, 1999, Belém, PA. Resumos expandidos. Belém, PA: EMBRAPA-CPATU: DFID, 1999. p. 98-103. (EMBRAPA-CPATU. Documentos, 123).| Biblioteca(s): Embrapa Amazônia Oriental. |
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| 15. | | FERREIRA, G. C.; MARTINS-DA-SILVA, R. C. V. Informatização da família Vochysiaceae do herbário IAN, da Embrapa Oriental, Belém-PA. In: SEMINÁRIO DE INICIAÇÃO CIENTIFICA DA FCAP, 7.; SEMINÁRIO DE INICIAÇÃO CIENTIFICA DA EMBRAPA AMAZÔNIA ORIENTAL, 1., 1997, Belém, PA. Resumos. Belém, PA: FCAP, 1997. p. 147.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Amazônia Oriental. |
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| 19. | | MARTINS-DA-SILVA, R. C. V.; FERREIRA, G. C. Levantamento preliminar das espécies arbutivas e arboreas ocorrentes na reserva florestal da Embrapa, localizada no município do Moju, Estado do Pará. In: SIMPÓSIO SILVICULTURA NA AMAZÔNIA ORIENTAL: contribuições do Projeto Embrapa/DFID, 1999, Belém, PA. Resumos expandidos. Belém, PA: EMBRAPA-CPATU: DFID, 1999. p. 46-50. (EMBRAPA-CPATU. Documentos, 123).| Biblioteca(s): Embrapa Amazônia Oriental. |
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| 20. | | REIS, I. P. dos; MARTINS-DA-SILVA, R. C. V. Levantamento, no herbário IAN, das Papilionoideae (Leguminosae) ocorrentes no Estado do Pará. In: SEMINÁRIO DE INICIAÇÃO CIENTÍFICA DA UFRA, 6.; SEMINÁRIO DE INICIAÇÃO CIENTÍFICA DA EMBRAPA AMAZÔNIA ORIENTAL (AVALIAÇÃO - 2008), 12., 2008, Belém, PA. A importância da iniciação científica para a pós-graduação: anais. Belém, PA: UFRA: Embrapa Amazônia Oriental, 2008.| Tipo: Artigo em Anais de Congresso / Nota Técnica |
| Biblioteca(s): Embrapa Amazônia Oriental. |
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| Registros recuperados : 188 | |
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| Nenhum registro encontrado para a expressão de busca informada. |
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