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Registro Completo |
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Biblioteca(s): |
Embrapa Milho e Sorgo. |
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Data corrente: |
04/09/1997 |
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Data da última atualização: |
13/07/2018 |
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Autoria: |
VALICENTE, F. H.; FONSECA, M. M.; CARVALHO, C. H. S. de; PAIVA, E.; FIGUEIREDO, J. E. F. |
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Afiliação: |
FERNANDO HERCOS VALICENTE, CNPMS; JOSE EDSON FONTES FIGUEIREDO, CNPMS. |
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Título: |
Efeito do Bacillus thuringiensis sobre a mortalidade da lagarta-do-cartucho, Spodoptera frugiperda. |
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Ano de publicação: |
1994 |
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Fonte/Imprenta: |
In: EMBRAPA. Centro de Nacional de Pesquisa de Milho e Sorgo. Relatório técnico anual do Centro Nacional de Pesquisa de Milho e Sorgo: período 1992-1993. Sete Lagoas, 1994. v. 6, p. 119-120. |
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Idioma: |
Português |
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Palavras-Chave: |
Lagarta do cartucho. |
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Thesagro: |
Bacillus Thuringiensis; Controle Biológico; Spodoptera Frugiperda. |
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Thesaurus Nal: |
biological control. |
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Categoria do assunto: |
H Saúde e Patologia |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/41282/1/Efeito-bacillus.pdf
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Marc: |
LEADER 00842naa a2200217 a 4500
001 1476230
005 2018-07-13
008 1994 bl uuuu u00u1 u #d
100 1 $aVALICENTE, F. H.
245 $aEfeito do Bacillus thuringiensis sobre a mortalidade da lagarta-do-cartucho, Spodoptera frugiperda.$h[electronic resource]
260 $c1994
650 $abiological control
650 $aBacillus Thuringiensis
650 $aControle Biológico
650 $aSpodoptera Frugiperda
653 $aLagarta do cartucho
700 1 $aFONSECA, M. M.
700 1 $aCARVALHO, C. H. S. de
700 1 $aPAIVA, E.
700 1 $aFIGUEIREDO, J. E. F.
773 $tIn: EMBRAPA. Centro de Nacional de Pesquisa de Milho e Sorgo. Relatório técnico anual do Centro Nacional de Pesquisa de Milho e Sorgo: período 1992-1993. Sete Lagoas, 1994.$gv. 6, p. 119-120.
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Registro original: |
Embrapa Milho e Sorgo (CNPMS) |
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 | Acesso ao texto completo restrito à biblioteca da Embrapa Mandioca e Fruticultura. Para informações adicionais entre em contato com cnpmf.biblioteca@embrapa.br. |
Registro Completo
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Biblioteca(s): |
Embrapa Mandioca e Fruticultura; Embrapa Meio Ambiente. |
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Data corrente: |
07/06/2022 |
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Data da última atualização: |
08/06/2022 |
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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: |
AMARAL, M. do; FREITAS, A. C. O.; SANTOS, A. S.; SANTOS, E. C. dos; FERREIRA, M. M.; GESTEIRA, A. da S.; GRAMACHO, K. P.; MARINHO-PRADO, J. S.; PIROVANI, C. P. |
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Afiliação: |
MILENA DO AMARAL, UESC; ANA CAMILA OLIVEIRA FREITAS, UESC; ARIANA SILVA SANTOS, UESC; EVERTON CRUZ DOS SANTOS, Instituto do Câncer José Alencar Gomes da Silva; MONALIZA MACÊDO FERREIRA, UESC; ABELMON DA SILVA GESTEIRA, CNPMF; KARINA PERES GRAMACHO, CEPEC; JEANNE SCARDINI MARINHO PRADO, CNPMA; CARLOS PRIMINHO PIROVANI, UESC. |
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Título: |
TcTI, a Kunitz-type trypsin inhibitor from cocoa associated with defense against pathogens. |
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Ano de publicação: |
2022 |
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Fonte/Imprenta: |
Scientific Reports, v. 12, n. 1, article 680, 2022. |
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DOI: |
https://doi.org/10.1038/s41598-021-04700-y |
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Idioma: |
Inglês |
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Conteúdo: |
Abstract: Protease inhibitors (PIs) are important biotechnological tools of interest in agriculture. Usually they are the first proteins to be activated in plant-induced resistance against pathogens. Therefore, the aim of this study was to characterize a Theobroma cacao trypsin inhibitor called TcTI. The ORF has 740 bp encoding a protein with 219 amino acids, molecular weight of approximately 23 kDa. rTcTI was expressed in the soluble fraction of Escherichia coli strain Rosetta [DE3]. The purified His-Tag rTcTI showed inhibitory activity against commercial porcine trypsin. The kinetic model demonstrated that rTcTI is a competitive inhibitor, with a Ki value of 4.08 × 10-7 mol L-1. The thermostability analysis of rTcTI showed that 100% inhibitory activity was retained up to 60 °C and that at 70-80 °C, inhibitory activity remained above 50%. Circular dichroism analysis indicated that the protein is rich in loop structures and beta-conformations. Furthermore, in vivo assays against Helicoverpa armigera larvae were also performed with rTcTI in 0.1 mg mL-1 spray solutions on leaf surfaces, which reduced larval growth by 70% compared to the control treatment. Trials with cocoa plants infected with Mp showed a greater accumulation of TcTI in resistant varieties of T. cacao, so this regulation may be associated with different isoforms of TcTI. This inhibitor has biochemical characteristics suitable for biotechnological applications as well as in resistance studies of T. cacao and other crops. MenosAbstract: Protease inhibitors (PIs) are important biotechnological tools of interest in agriculture. Usually they are the first proteins to be activated in plant-induced resistance against pathogens. Therefore, the aim of this study was to characterize a Theobroma cacao trypsin inhibitor called TcTI. The ORF has 740 bp encoding a protein with 219 amino acids, molecular weight of approximately 23 kDa. rTcTI was expressed in the soluble fraction of Escherichia coli strain Rosetta [DE3]. The purified His-Tag rTcTI showed inhibitory activity against commercial porcine trypsin. The kinetic model demonstrated that rTcTI is a competitive inhibitor, with a Ki value of 4.08 × 10-7 mol L-1. The thermostability analysis of rTcTI showed that 100% inhibitory activity was retained up to 60 °C and that at 70-80 °C, inhibitory activity remained above 50%. Circular dichroism analysis indicated that the protein is rich in loop structures and beta-conformations. Furthermore, in vivo assays against Helicoverpa armigera larvae were also performed with rTcTI in 0.1 mg mL-1 spray solutions on leaf surfaces, which reduced larval growth by 70% compared to the control treatment. Trials with cocoa plants infected with Mp showed a greater accumulation of TcTI in resistant varieties of T. cacao, so this regulation may be associated with different isoforms of TcTI. This inhibitor has biochemical characteristics suitable for biotechnological applications as well as in resistance studies of T. cacao and ot... Mostrar Tudo |
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Thesagro: |
Cacau; Inibidor de Enzima; Praga de Planta; Protease; Resistência; Theobroma Cacao. |
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Thesaurus NAL: |
Disease resistance; Helicoverpa armigera; Insecticide resistance; Trypsin inhibitors. |
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Categoria do assunto: |
H Saúde e Patologia |
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Marc: |
LEADER 02552naa a2200349 a 4500
001 2143860
005 2022-06-08
008 2022 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.1038/s41598-021-04700-y$2DOI
100 1 $aAMARAL, M. do
245 $aTcTI, a Kunitz-type trypsin inhibitor from cocoa associated with defense against pathogens.$h[electronic resource]
260 $c2022
520 $aAbstract: Protease inhibitors (PIs) are important biotechnological tools of interest in agriculture. Usually they are the first proteins to be activated in plant-induced resistance against pathogens. Therefore, the aim of this study was to characterize a Theobroma cacao trypsin inhibitor called TcTI. The ORF has 740 bp encoding a protein with 219 amino acids, molecular weight of approximately 23 kDa. rTcTI was expressed in the soluble fraction of Escherichia coli strain Rosetta [DE3]. The purified His-Tag rTcTI showed inhibitory activity against commercial porcine trypsin. The kinetic model demonstrated that rTcTI is a competitive inhibitor, with a Ki value of 4.08 × 10-7 mol L-1. The thermostability analysis of rTcTI showed that 100% inhibitory activity was retained up to 60 °C and that at 70-80 °C, inhibitory activity remained above 50%. Circular dichroism analysis indicated that the protein is rich in loop structures and beta-conformations. Furthermore, in vivo assays against Helicoverpa armigera larvae were also performed with rTcTI in 0.1 mg mL-1 spray solutions on leaf surfaces, which reduced larval growth by 70% compared to the control treatment. Trials with cocoa plants infected with Mp showed a greater accumulation of TcTI in resistant varieties of T. cacao, so this regulation may be associated with different isoforms of TcTI. This inhibitor has biochemical characteristics suitable for biotechnological applications as well as in resistance studies of T. cacao and other crops.
650 $aDisease resistance
650 $aHelicoverpa armigera
650 $aInsecticide resistance
650 $aTrypsin inhibitors
650 $aCacau
650 $aInibidor de Enzima
650 $aPraga de Planta
650 $aProtease
650 $aResistência
650 $aTheobroma Cacao
700 1 $aFREITAS, A. C. O.
700 1 $aSANTOS, A. S.
700 1 $aSANTOS, E. C. dos
700 1 $aFERREIRA, M. M.
700 1 $aGESTEIRA, A. da S.
700 1 $aGRAMACHO, K. P.
700 1 $aMARINHO-PRADO, J. S.
700 1 $aPIROVANI, C. P.
773 $tScientific Reports$gv. 12, n. 1, article 680, 2022.
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