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Registro Completo |
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Biblioteca(s): |
Embrapa Milho e Sorgo. |
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Data corrente: |
22/09/2008 |
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Data da última atualização: |
24/05/2018 |
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Tipo da produção científica: |
Artigo em Anais de Congresso / Nota Técnica |
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Autoria: |
TEIXEIRA, F. F.; GOMIDE, R. L.; ALBUQUERQUE, P. E. P. de; ANDRADE, C. L. T. de; LEITE, C. E. P.; PARENTONI, S. N.; GUIMARAES, P. E.; GUIMARAES, L. J. M.; SILVA, A. R. da; CARDOSO, M. J. |
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Afiliação: |
FLAVIA FRANCA TEIXEIRA, CNPMS; REINALDO LUCIO GOMIDE, CNPMS; PAULO EMILIO PEREIRA DE ALBUQUERQUE, CNPMS; CAMILO DE LELIS TEIXEIRA DE ANDRADE, CNPMS; SIDNEY NETTO PARENTONI, CNPMS; PAULO EVARISTO DE O GUIMARAES, CNPMS; LAURO JOSE MOREIRA GUIMARAES, CNPMS; ADELMO RESENDE DA SILVA, CNPMS; MILTON JOSE CARDOSO, CPAMN. |
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Título: |
Desempenho de acessos da coleção núcleo de milho quanto a tolerância à seca. |
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Ano de publicação: |
2008 |
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Fonte/Imprenta: |
In: CONGRESSO NACIONAL DE MILHO E SORGO, 27.; SIMPOSIO BRASILEIRO SOBRE A LAGARTA-DO-CARTUCHO, SPODOPTERA FRUGIPERDA, 3.; WORKSHOP SOBRE MANEJO E ETIOLOGIA DA MANCHA BRANCA DO MILHO, 2008, Londrina. Agroenergia, produção de alimentos e mudanças climáticas: desafios para milho e sorgo: trabalhos e palestras. [Londrina]: IAPAR; [Sete Lagoas]: Embrapa Milho e Sorgo, 2008. |
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Descrição Física: |
1 CD-ROM. |
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Idioma: |
Português |
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Palavras-Chave: |
Estresse abióticos; Pré-melhoramento. |
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Thesagro: |
Banco de Germoplasma; Zea Mays. |
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Categoria do assunto: |
S Ciências Biológicas |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/30064/1/Desempenho-acesso.pdf
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Marc: |
LEADER 01129nam a2200265 a 4500
001 1491335
005 2018-05-24
008 2008 bl uuuu u00u1 u #d
100 1 $aTEIXEIRA, F. F.
245 $aDesempenho de acessos da coleção núcleo de milho quanto a tolerância à seca.$h[electronic resource]
260 $aIn: CONGRESSO NACIONAL DE MILHO E SORGO, 27.; SIMPOSIO BRASILEIRO SOBRE A LAGARTA-DO-CARTUCHO, SPODOPTERA FRUGIPERDA, 3.; WORKSHOP SOBRE MANEJO E ETIOLOGIA DA MANCHA BRANCA DO MILHO, 2008, Londrina. Agroenergia, produção de alimentos e mudanças climáticas: desafios para milho e sorgo: trabalhos e palestras. [Londrina]: IAPAR; [Sete Lagoas]: Embrapa Milho e Sorgo$c2008
300 $c1 CD-ROM.
650 $aBanco de Germoplasma
650 $aZea Mays
653 $aEstresse abióticos
653 $aPré-melhoramento
700 1 $aGOMIDE, R. L.
700 1 $aALBUQUERQUE, P. E. P. de
700 1 $aANDRADE, C. L. T. de
700 1 $aLEITE, C. E. P.
700 1 $aPARENTONI, S. N.
700 1 $aGUIMARAES, P. E.
700 1 $aGUIMARAES, L. J. M.
700 1 $aSILVA, A. R. da
700 1 $aCARDOSO, M. J.
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Registro original: |
Embrapa Milho e Sorgo (CNPMS) |
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Biblioteca |
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Origem |
Tipo/Formato |
Classificação |
Cutter |
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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. |
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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Circulação/Nível: |
A - 1 |
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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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