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| Registros recuperados : 926 | |
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Registro Completo
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Biblioteca(s): |
Embrapa Instrumentação. |
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Data corrente: |
14/05/2024 |
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Data da última atualização: |
11/06/2024 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
A - 2 |
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Autoria: |
CORREA, K. C. S.; FACCHINATO, W. M.; HABITZREUTER, F. B.; RIBEIRO, G. H.; RODRIGUES, L. G.; MICOCCI, K. C.; CAMPANA-FILHO, S. P.; COLNAGO, L. A.; SOUZA, D. H. F. |
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Afiliação: |
FEDERAL UNIVERSITY OF SAO CARLOS; UNIVERSITY OF AVEIRO, ST. SANTIAGO; UNIVERSITY OF SAO PAULO; FEDERAL UNIVERSITY OF SAO CARLOS; FEDERAL UNIVERSITY OF SAO CARLOS; UNIVERSITY OF SAO PAULO; LUIZ ALBERTO COLNAGO, CNPDIA; FEDERAL UNIVERSITY OF SAO CARLOS. |
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Título: |
Activity of a Recombinant Chitinase of the Atta sexdens Ant on Different Forms of Chitin and Its Fungicidal Effect against Lasiodiplodia theobromae. |
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Ano de publicação: |
2024 |
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Fonte/Imprenta: |
Polymers, v. 16, 529, 2014. |
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Páginas: |
1 - 17 |
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DOI: |
https:// doi.org/10.3390/polym16040529 |
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Idioma: |
Inglês |
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Conteúdo: |
Abstract: This study evaluates the activity of a recombinant chitinase from the leaf-cutting ant Atta sexdens (AsChtII-C4B1) against colloidal and solid α- and β-chitin substrates. 1H NMR analyses of the reaction media showed the formation of N-acetylglucosamine (GlcNAc) as the hydrolysis product. Viscometry analyses revealed a reduction in the viscosity of chitin solutions, indicating that the enzyme decreases their molecular masses. Both solid state 13C NMR and XRD analyses showed minor differences in chitin crystallinity pre- and post-reaction, indicative of partial hydrolysis under the studied conditions, resulting in the formation of GlcNAc and a reduction in molecular mass. However, the enzyme was unable to completely degrade the chitin samples, as they retained most of their solid-state structure. It was also observed that the enzyme acts progressively and with a greater activity on α-chitin than on β-chitin. AsChtII-C4B1 significantly changed the hyphae of the phytopathogenic fungus Lasiodiplodia theobromae, hindering its growth in both solid and liquid media and reducing its dry biomass by approximately 61%. The results demonstrate that AsChtIIC4B1 could be applied as an agent for the bioproduction of chitin derivatives and as a potential antifungal agent. |
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Palavras-Chave: |
Fungicide; Insect chitinase. |
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Categoria do assunto: |
-- |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/doc/1164249/1/P-Activity-of-a-Recombinant-Chitinase-of-the-Atta-sexdens-Ant-on.pdf
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Marc: |
LEADER 02121naa a2200265 a 4500
001 2164249
005 2024-06-11
008 2024 bl uuuu u00u1 u #d
024 7 $ahttps:// doi.org/10.3390/polym16040529$2DOI
100 1 $aCORREA, K. C. S.
245 $aActivity of a Recombinant Chitinase of the Atta sexdens Ant on Different Forms of Chitin and Its Fungicidal Effect against Lasiodiplodia theobromae.$h[electronic resource]
260 $c2024
300 $a1 - 17
520 $aAbstract: This study evaluates the activity of a recombinant chitinase from the leaf-cutting ant Atta sexdens (AsChtII-C4B1) against colloidal and solid α- and β-chitin substrates. 1H NMR analyses of the reaction media showed the formation of N-acetylglucosamine (GlcNAc) as the hydrolysis product. Viscometry analyses revealed a reduction in the viscosity of chitin solutions, indicating that the enzyme decreases their molecular masses. Both solid state 13C NMR and XRD analyses showed minor differences in chitin crystallinity pre- and post-reaction, indicative of partial hydrolysis under the studied conditions, resulting in the formation of GlcNAc and a reduction in molecular mass. However, the enzyme was unable to completely degrade the chitin samples, as they retained most of their solid-state structure. It was also observed that the enzyme acts progressively and with a greater activity on α-chitin than on β-chitin. AsChtII-C4B1 significantly changed the hyphae of the phytopathogenic fungus Lasiodiplodia theobromae, hindering its growth in both solid and liquid media and reducing its dry biomass by approximately 61%. The results demonstrate that AsChtIIC4B1 could be applied as an agent for the bioproduction of chitin derivatives and as a potential antifungal agent.
653 $aFungicide
653 $aInsect chitinase
700 1 $aFACCHINATO, W. M.
700 1 $aHABITZREUTER, F. B.
700 1 $aRIBEIRO, G. H.
700 1 $aRODRIGUES, L. G.
700 1 $aMICOCCI, K. C.
700 1 $aCAMPANA-FILHO, S. P.
700 1 $aCOLNAGO, L. A.
700 1 $aSOUZA, D. H. F.
773 $tPolymers$gv. 16, 529, 2014.
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Registro original: |
Embrapa Instrumentação (CNPDIA) |
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