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Registro Completo |
Biblioteca(s): |
Embrapa Meio Ambiente. |
Data corrente: |
22/12/2021 |
Data da última atualização: |
23/12/2021 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
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. |
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. |
Título: |
Atlantic Forest's and Caatinga's semiarid soils and their potential as a source for halothermotolerant actinomycetes and proteolytic enzymes. |
Ano de publicação: |
2021 |
Fonte/Imprenta: |
Environmental Technology, 2021. |
ISSN: |
0959-3330 |
DOI: |
https://doi.org/10.1080/09593330.2021.2008015 |
Idioma: |
Inglês |
Notas: |
On-line first |
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 |
Palavras-Chave: |
FRET peptide; Metalloprotease. |
Thesagro: |
Actinomiceto; Cerrado; Rizosfera; Solo. |
Thesaurus Nal: |
Cerrado soils; Peptides; Proteolytic bacteria; Rhizosphere; Serine. |
Categoria do assunto: |
P Recursos Naturais, Ciências Ambientais e da Terra |
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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