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Registro Completo |
Biblioteca(s): |
Embrapa Agroenergia. |
Data corrente: |
09/07/2013 |
Data da última atualização: |
20/08/2013 |
Tipo da produção científica: |
Resumo em Anais de Congresso |
Autoria: |
FAHEEM, M.; VIDAL, J. F. D.; FERNANDES, J. P. C.; OLIVEIRA. G. M.; CAROLINE, C. F.; SOUTO, B. de M.; PARACHIN, N. S.; QUIRINO, B. F.; BARBOSA, J. A. R. G. |
Afiliação: |
UCB; UCB; UCB; UCB; UCB; BETULIA DE MORAIS SOUTO, CNPAE; UNB; BETANIA FERRAZ QUIRINO, CNPAE; Barbosa, J.A.R.G., UNB. |
Título: |
Cloning and initial characterization of cellulolytic enzymes selected in a metagenomic approach. |
Ano de publicação: |
2013 |
Fonte/Imprenta: |
In: REUNIÃO ANUAL DA SBBQ, 42., 2013, Foz do Iguaçu, PR. [Anais...] São Paulo: SBBq, 2013. |
Idioma: |
Inglês |
Palavras-Chave: |
Biofuel; Cellulose degradation; Enzymatic activity; Metagenome. |
Thesaurus Nal: |
protein structure. |
Categoria do assunto: |
-- |
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/85756/1/Faheem-poster-SBBq-2013.pdf
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Marc: |
LEADER 00816nam a2200253 a 4500 001 1961702 005 2013-08-20 008 2013 bl uuuu u00u1 u #d 100 1 $aFAHEEM, M. 245 $aCloning and initial characterization of cellulolytic enzymes selected in a metagenomic approach.$h[electronic resource] 260 $aIn: REUNIÃO ANUAL DA SBBQ, 42., 2013, Foz do Iguaçu, PR. [Anais...] São Paulo: SBBq$c2013 650 $aprotein structure 653 $aBiofuel 653 $aCellulose degradation 653 $aEnzymatic activity 653 $aMetagenome 700 1 $aVIDAL, J. F. D. 700 1 $aFERNANDES, J. P. C. 700 1 $aOLIVEIRA. G. M. 700 1 $aCAROLINE, C. F. 700 1 $aSOUTO, B. de M. 700 1 $aPARACHIN, N. S. 700 1 $aQUIRINO, B. F. 700 1 $aBARBOSA, J. A. R. G.
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Registro original: |
Embrapa Agroenergia (CNPAE) |
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Registro Completo
Biblioteca(s): |
Embrapa Instrumentação. |
Data corrente: |
24/05/2022 |
Data da última atualização: |
23/01/2024 |
Tipo da produção científica: |
Artigo em Periódico Indexado |
Circulação/Nível: |
A - 2 |
Autoria: |
RIBEIRO, T. S.; SCRAMIN, J. A.; RODRIGUES, J. A. S.; BERNARDES FILHO, R.; COLNAGO, L. A.; FORATO, L. A. |
Afiliação: |
RUBENS BERNARDES FILHO, CNPDIA; LUIZ ALBERTO COLNAGO, CNPDIA; LUCIMARA APARECIDA FORATO, CNPDIA. |
Título: |
13C ss-NMR Singular value decomposition and fitting for sorghum proteins conformation elucidation. |
Ano de publicação: |
2022 |
Fonte/Imprenta: |
Polímeros, v. 32, n. 1, e2022009, 2022. |
Páginas: |
6 p. |
ISSN: |
1678-5169 |
DOI: |
10.1590/0104-1428.20210082 |
Idioma: |
Inglês |
Conteúdo: |
Kafirins, water-insoluble proteins from Sweet Sorghum BR501 grains, have been an alternative to prepare edible coatings for food due to their hydrophobic character. In this work, the secondary structures (SS) content of reduced (SSr) and unreduced (SSu) kafirins were determined by 13C solid-state-NMR spectroscopy using areas of carbonyl peak. The SS elucidate by fitting the signal with the Lorentzian function shows 56% and 59% of α-helix and 40% and 12% of β-sheet structures for SSr and SSu, respectively. The SS also were elucidated by a Singular value decomposition- SVD method shows 55% and 49% of α-helix and 12% and 8% of β-sheet structure for SSr and SSu, respectively. Since SVD does not depend on the operator and has higher correlation coefficients for α-helix (0.96%) and β-sheet (0.91%), it is a reliable method to quantify the SS of insoluble proteins using the 13C NMR signal. |
Palavras-Chave: |
13C NMR spectroscopy; Kafirin; Secondary structures proteins. |
Categoria do assunto: |
-- |
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/doc/1143402/1/P-3C-ss-NMR-Singular-value-decomposition-and-fitting-for.pdf
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Marc: |
LEADER 01652naa a2200253 a 4500 001 2143402 005 2024-01-23 008 2022 bl uuuu u00u1 u #d 022 $a1678-5169 024 7 $a10.1590/0104-1428.20210082$2DOI 100 1 $aRIBEIRO, T. S. 245 $a13C ss-NMR Singular value decomposition and fitting for sorghum proteins conformation elucidation.$h[electronic resource] 260 $c2022 300 $a6 p. 520 $aKafirins, water-insoluble proteins from Sweet Sorghum BR501 grains, have been an alternative to prepare edible coatings for food due to their hydrophobic character. In this work, the secondary structures (SS) content of reduced (SSr) and unreduced (SSu) kafirins were determined by 13C solid-state-NMR spectroscopy using areas of carbonyl peak. The SS elucidate by fitting the signal with the Lorentzian function shows 56% and 59% of α-helix and 40% and 12% of β-sheet structures for SSr and SSu, respectively. The SS also were elucidated by a Singular value decomposition- SVD method shows 55% and 49% of α-helix and 12% and 8% of β-sheet structure for SSr and SSu, respectively. Since SVD does not depend on the operator and has higher correlation coefficients for α-helix (0.96%) and β-sheet (0.91%), it is a reliable method to quantify the SS of insoluble proteins using the 13C NMR signal. 653 $a13C NMR spectroscopy 653 $aKafirin 653 $aSecondary structures proteins 700 1 $aSCRAMIN, J. A. 700 1 $aRODRIGUES, J. A. S. 700 1 $aBERNARDES FILHO, R. 700 1 $aCOLNAGO, L. A. 700 1 $aFORATO, L. A. 773 $tPolímeros$gv. 32, n. 1, e2022009, 2022.
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