| |
|
|
 | Acesso ao texto completo restrito à biblioteca da Embrapa Recursos Genéticos e Biotecnologia. Para informações adicionais entre em contato com cenargen.biblioteca@embrapa.br. |
|
Registro Completo |
|
Biblioteca(s): |
Embrapa Recursos Genéticos e Biotecnologia. |
|
Data corrente: |
26/02/2013 |
|
Data da última atualização: |
07/03/2023 |
|
Tipo da produção científica: |
Artigo em Periódico Indexado |
|
Autoria: |
NOGUEIRA, F. C.; SILVA, C. P.; ALEXANDRE, D.; SAMUELS, R. I; SOARES, E. L.; ARAGAO, F. J. L.; PALMISANO, G.; DOMONT, G. B.; ROEPSTORFF, P.; CAMPOS, F. A. |
|
Afiliação: |
Universidade Federal do Rio de Janeiro; Universidade Federal de Santa Catarina; Universidade Federal de Santa Catarina; Universidade Estadual do Norte Fluminense; Universidade Federal do Ceará; FRANCISCO JOSE LIMA ARAGAO, CENARGEN; University of Southern Denmark; Universidade Federal do Rio de Janeiro; University of Southern Denmark; Universidade Federal do Ceará. |
|
Título: |
Global proteome changes in larvae of Callosobruchus maculatus Coleoptera:Chrysomelidae:Bruchinae) following ingestion of a cysteine proteinase inhibitor. |
|
Ano de publicação: |
2012 |
|
Fonte/Imprenta: |
Proteomics, v. 12, n. 17, p. 2704-2715, 2012. |
|
Idioma: |
Inglês |
|
Conteúdo: |
The seed-feeding beetle Callosobruchus maculatus is an important cowpea pest (Vigna unguiculata) as well as an interesting model to study insect digestive physiology. The larvae of C. maculatus rely on cysteine and aspartic peptidases to digest proteins in their diet. In this work, the global proteomic changes induced in the intestinal tract of larval C. maculatus challenged by the ingestion of cystatin, a cysteine peptidase inhibitor, was investigated by a nanoLC-MS/MS approach. The ingestion of cystatin caused a delay in the development of the larvae, but the mortality was not high, indicating that C. maculatus is able to adapt to this inhibitor. This proteomic strategy resulted in the identification of 752 and 550 protein groups in the midgut epithelia and midgut contents, respectively, and quantitative analyses allowed us to establish relative differences of the identified proteins. Ingestion of cystatin led to significant changes in the proteome of both the midgut epithelia and midgut contents. We have observed that proteins related to plant cell wall degradation, particularly the key glycoside hydrolases of the families GH5 (endo-?-1,4-mannanase) and GH 28 (polygalacturonase) were overexpressed. Conversely, ?-amylases were downexpressed, indicating that an increase in hemicelluloses digestion helps the larvae to cope with the challenge of cystatin ingestion. Furthermore, a number of proteins associated with transcription/translation and antistress reactions were among the cystatin-responsive proteins, implying that a substantial rearrangement in the proteome occurred in C. maculatus exposed to the inhibitor. MenosThe seed-feeding beetle Callosobruchus maculatus is an important cowpea pest (Vigna unguiculata) as well as an interesting model to study insect digestive physiology. The larvae of C. maculatus rely on cysteine and aspartic peptidases to digest proteins in their diet. In this work, the global proteomic changes induced in the intestinal tract of larval C. maculatus challenged by the ingestion of cystatin, a cysteine peptidase inhibitor, was investigated by a nanoLC-MS/MS approach. The ingestion of cystatin caused a delay in the development of the larvae, but the mortality was not high, indicating that C. maculatus is able to adapt to this inhibitor. This proteomic strategy resulted in the identification of 752 and 550 protein groups in the midgut epithelia and midgut contents, respectively, and quantitative analyses allowed us to establish relative differences of the identified proteins. Ingestion of cystatin led to significant changes in the proteome of both the midgut epithelia and midgut contents. We have observed that proteins related to plant cell wall degradation, particularly the key glycoside hydrolases of the families GH5 (endo-?-1,4-mannanase) and GH 28 (polygalacturonase) were overexpressed. Conversely, ?-amylases were downexpressed, indicating that an increase in hemicelluloses digestion helps the larvae to cope with the challenge of cystatin ingestion. Furthermore, a number of proteins associated with transcription/translation and antistress reactions were among ... Mostrar Tudo |
|
Palavras-Chave: |
Peptidase inhibitors; Plant proteomics. |
|
Thesagro: |
Callosobruchus Maculatus; Vigna Unguiculata. |
|
Categoria do assunto: |
-- |
|
Marc: |
LEADER 02507naa a2200277 a 4500
001 1951245
005 2023-03-07
008 2012 bl uuuu u00u1 u #d
100 1 $aNOGUEIRA, F. C.
245 $aGlobal proteome changes in larvae of Callosobruchus maculatus Coleoptera$bChrysomelidae:Bruchinae) following ingestion of a cysteine proteinase inhibitor.$h[electronic resource]
260 $c2012
520 $aThe seed-feeding beetle Callosobruchus maculatus is an important cowpea pest (Vigna unguiculata) as well as an interesting model to study insect digestive physiology. The larvae of C. maculatus rely on cysteine and aspartic peptidases to digest proteins in their diet. In this work, the global proteomic changes induced in the intestinal tract of larval C. maculatus challenged by the ingestion of cystatin, a cysteine peptidase inhibitor, was investigated by a nanoLC-MS/MS approach. The ingestion of cystatin caused a delay in the development of the larvae, but the mortality was not high, indicating that C. maculatus is able to adapt to this inhibitor. This proteomic strategy resulted in the identification of 752 and 550 protein groups in the midgut epithelia and midgut contents, respectively, and quantitative analyses allowed us to establish relative differences of the identified proteins. Ingestion of cystatin led to significant changes in the proteome of both the midgut epithelia and midgut contents. We have observed that proteins related to plant cell wall degradation, particularly the key glycoside hydrolases of the families GH5 (endo-?-1,4-mannanase) and GH 28 (polygalacturonase) were overexpressed. Conversely, ?-amylases were downexpressed, indicating that an increase in hemicelluloses digestion helps the larvae to cope with the challenge of cystatin ingestion. Furthermore, a number of proteins associated with transcription/translation and antistress reactions were among the cystatin-responsive proteins, implying that a substantial rearrangement in the proteome occurred in C. maculatus exposed to the inhibitor.
650 $aCallosobruchus Maculatus
650 $aVigna Unguiculata
653 $aPeptidase inhibitors
653 $aPlant proteomics
700 1 $aSILVA, C. P.
700 1 $aALEXANDRE, D.
700 1 $aSAMUELS, R. I
700 1 $aSOARES, E. L.
700 1 $aARAGAO, F. J. L.
700 1 $aPALMISANO, G.
700 1 $aDOMONT, G. B.
700 1 $aROEPSTORFF, P.
700 1 $aCAMPOS, F. A.
773 $tProteomics$gv. 12, n. 17, p. 2704-2715, 2012.
Download
Esconder MarcMostrar Marc Completo |
|
Registro original: |
Embrapa Recursos Genéticos e Biotecnologia (CENARGEN) |
|
|
Biblioteca |
ID |
Origem |
Tipo/Formato |
Classificação |
Cutter |
Registro |
Volume |
Status |
URL |
Voltar
|
|
|
Registro Completo
|
Biblioteca(s): |
Embrapa Soja. |
|
Data corrente: |
31/08/2012 |
|
Data da última atualização: |
02/08/2017 |
|
Tipo da produção científica: |
Resumo em Anais de Congresso |
|
Autoria: |
MOREIRA, A. A.; SANTOS, R. F.; MANDARINO, J. M. G.; VARÉA, G. S.; IDA, E. I.; RIBEIRO, M. L. L. |
|
Afiliação: |
AMANDA A. MOREIRA, UEL; RAFAEL F. SANTOS, UEL; JOSE MARCOS GONTIJO MANDARINO, CNPSO; GENI S. VARÉA, UEL - Professora; ELZA I. IDA, UEL; MARA L. L. RIBEIRO, UEL. |
|
Título: |
Conversion of isoflavone glucosides to aglycones in whole soybean flour thermally treated and with endogenous B-glucosidase of soybean. |
|
Ano de publicação: |
2012 |
|
Fonte/Imprenta: |
In: WORLD CONGRESS OF FOOD SCIENCE AND TECHNOLOGY, 16.; LATIN AMERICAN SEMINAR OF FOOD SCIENCE AND TECHNOLOGY, 17., 2012, Foz do Iguaçu. Addressing global food security and wellness through food science and technology: [proceedings]. Foz do Iguaçu: IUFoST, 2012. 1 CD-ROM. |
|
Idioma: |
Inglês |
|
Conteúdo: |
The B-glucosidase hydrolyze isoflavone glucosides releasing aglycones. Its application in the food industry is relevant to the production of soybean foods with higher levels of isoflavone aglycones, with benefits for human health. The objective of this study was to apply endogenous B-glucosidase of soybean in whole soybean flour (WSF) and evaluate the conversion of isoflavone glucosides to aglycones. The B-glucosidase was fractionated by 40-85% ammonium sulfate saturation, concentrated by ultrafiltration (MWCO 100 kDa) and was applied in WSF thermally treated under different conditions. WSF without heat treatment and without application of enzyme was used as control (WSFC). Thermal pretreatment was performed in WSFC for 1h at 100°C (WSF100) or autoclaved for 30min at 121°C (WSF121). In these treatments were added 10U or 50U of B-glucosidase and incubated at 30°C for 2 or 6h. The aglycones content was determined by HPLC and the results were expressed as μg g-1 of samples. Thermal pretreatment increased the aglycone content of WSF100 and WSF121 in 2.6 and 2.8 times, respectively, relative to WSFC. The application of 50U of -glucosidase for 6h at 30°C in and CSF100 and CSF121 increased aglycones content of 7.1 and 8.5 times, respectively, relative to WSFC. The -glucosidase was efficient in the conversion of isoflavone glucosides to aglycones in all treatments compared with the control. |
|
Palavras-Chave: |
Isoflavona. |
|
Thesagro: |
Soja; Tecnologia de alimento. |
|
Thesaurus NAL: |
Food technology; Isoflavones; Soybeans. |
|
Categoria do assunto: |
Q Alimentos e Nutrição Humana |
|
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/65350/1/05324.pdf
|
|
Marc: |
LEADER 02378nam a2200241 a 4500
001 1932726
005 2017-08-02
008 2012 bl uuuu u00u1 u #d
100 1 $aMOREIRA, A. A.
245 $aConversion of isoflavone glucosides to aglycones in whole soybean flour thermally treated and with endogenous B-glucosidase of soybean.
260 $aIn: WORLD CONGRESS OF FOOD SCIENCE AND TECHNOLOGY, 16.; LATIN AMERICAN SEMINAR OF FOOD SCIENCE AND TECHNOLOGY, 17., 2012, Foz do Iguaçu. Addressing global food security and wellness through food science and technology: [proceedings]. Foz do Iguaçu: IUFoST, 2012. 1 CD-ROM.$c2012
520 $aThe B-glucosidase hydrolyze isoflavone glucosides releasing aglycones. Its application in the food industry is relevant to the production of soybean foods with higher levels of isoflavone aglycones, with benefits for human health. The objective of this study was to apply endogenous B-glucosidase of soybean in whole soybean flour (WSF) and evaluate the conversion of isoflavone glucosides to aglycones. The B-glucosidase was fractionated by 40-85% ammonium sulfate saturation, concentrated by ultrafiltration (MWCO 100 kDa) and was applied in WSF thermally treated under different conditions. WSF without heat treatment and without application of enzyme was used as control (WSFC). Thermal pretreatment was performed in WSFC for 1h at 100°C (WSF100) or autoclaved for 30min at 121°C (WSF121). In these treatments were added 10U or 50U of B-glucosidase and incubated at 30°C for 2 or 6h. The aglycones content was determined by HPLC and the results were expressed as μg g-1 of samples. Thermal pretreatment increased the aglycone content of WSF100 and WSF121 in 2.6 and 2.8 times, respectively, relative to WSFC. The application of 50U of -glucosidase for 6h at 30°C in and CSF100 and CSF121 increased aglycones content of 7.1 and 8.5 times, respectively, relative to WSFC. The -glucosidase was efficient in the conversion of isoflavone glucosides to aglycones in all treatments compared with the control.
650 $aFood technology
650 $aIsoflavones
650 $aSoybeans
650 $aSoja
650 $aTecnologia de alimento
653 $aIsoflavona
700 1 $aSANTOS, R. F.
700 1 $aMANDARINO, J. M. G.
700 1 $aVARÉA, G. S.
700 1 $aIDA, E. I.
700 1 $aRIBEIRO, M. L. L.
Download
Esconder MarcMostrar Marc Completo |
|
Registro original: |
Embrapa Soja (CNPSO) |
|
|
Biblioteca |
ID |
Origem |
Tipo/Formato |
Classificação |
Cutter |
Registro |
Volume |
Status |
Fechar
|
| Nenhum registro encontrado para a expressão de busca informada. |
|
|
