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| Registros recuperados : 32 | |
| 5. |  | FUJIMOTO, R. Y.; CASTRO, M. P. de; HONORATO, C. A.; MORAES, F. R. de. Composição corporal e eficiência de utilização de nutrientes por pacus alimentados com ração suplementada com cromo trivalente. Pesquisa Agropecuária Brasileira, Brasília, DF, v. 42, n. 12, p. 1763-1768, dez. 2007 Título em inglês: Body composition and nutrient efficiency use by pacus fed on ration supplemented with chromium.| Biblioteca(s): Embrapa Algodão; Embrapa Unidades Centrais. |
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| 7. | | CHAGAS, E. C.; PILARSKI, F.; SAKABE, R.; MORAES, F. R. de. Desempenho produtivo e respostas fisiopatológicas de tambaquis alimentados com ração suplementada com b-glucano. Pesquisa Agropecuária Brasileira, Brasília, DF, v. 48, n. 8, p. 899-905, ago. 2013.| Biblioteca(s): Embrapa Amazônia Ocidental; Embrapa Unidades Centrais. |
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| 8. | | NESHICH, I. A. P.; MORAES, F. R. de; SALIM, J. A.; MAZONI, I.; MANCINI, A.; JARDINE, J. G.; NESHICH, G. Surface hydrophobicity index (SHI): insight into the mechanisms of protein-protein associations. In: INTERNATIONAL CONFERENCE OF THE BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 5., 2009, Angra dos Reis. Abstracts book... Angra dos Reis: ABBCB, 2009. Não paginado. X-Meeting 2009| Biblioteca(s): Embrapa Agricultura Digital. |
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| 9. | | MAZONI, I.; SALIM, J. A; NESHICH, I. A. P.; MORAES, F. R. de; NISHIMURA, L.; JARDINE, J. G.; NESHICH, G. Structure function relationship de convoluted to a level of physical chemical descriptors: case study - lysozyme / lactalbumine differences. In: ANNUAL MEETING OF THE SBBq, 40., 2011, Foz do Iguaçu. [Proceedings...]. São Paulo, SP: Brazilian Society for Biochemistry and Molecular Biology, 2011. Não paginado.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 10. | | JARDINE, J. G.; NESHICH, I. A. P.; MORAES, F. R. de; MAZONI, I.; MANCINI, A.; SALIM, J. A.; NESHICH, G. Generation of lipase B mutants with increased surface hydrophobicity in order to improve biodiesel catalysis. In: INTERNATIONAL CONFERENCE OF THE BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 5., 2009, Angra dos Reis. Abstracts book... Angra dos Reis: ABBCB, 2009. Não paginado. X-Meeting 2009.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 13. | | SAKABE, R.; MORAES, F. R. de; BELO, M. A. de A.; PILARSKI, F.; MORAES, J. R. E. de. Kinetics of chronic inflammation in Nile tilapia fed n-3 and n-6 essential fatty acids. Pesquisa Agropecuária Brasileira, Brasília, DF, v. 48, n. 3, p. 313-319, mar. 2013. Título em português: Cinética da inflamação crônica em tilápia?do?nilo alimentada com ácidos graxos essenciais n?3 e n?6.| Biblioteca(s): Embrapa Unidades Centrais. |
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| 14. | | NESHICH, I. A. P.; MAZONI, I.; SALIM, J. A.; MORAES, F. R. de; NISHIMURA, L.; JARDINE, J. G.; NESHICH, G. Pathogenic Prion Proteins (PrP) have higher electrostatic potential pattern than normal cellular prion protein in a specific region. In: ANNUAL MEETING OF THE SBBq, 40., 2011, Foz do Iguaçu. [Proceedings...]. São Paulo, SP: Brazilian Society for Biochemistry and Molecular Biology, 2011. Não paginado.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 15. | | VARANDAS, D. N; MARTINS, M. L; MORAES, F. R. de; RAMOS, F. M.; SANTOS, R. F. B.; FUJIMOTO, R. Y. Pesque-solte: pesca repetitiva, variáveis hematológicas e parasitismo no peixe híbrido tambacu. Pesquisa Agropecuária Brasileira, Brasília, DF, v. 48, n. 8, p. 1058-1063, ago. 2013.| Biblioteca(s): Embrapa Tabuleiros Costeiros; Embrapa Unidades Centrais. |
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| 16. | | NOMURA, D. T.; MENESES, J. O.; PILARSKI, F.; MORAES, F. R. de; ABE, H. A.; FUJIMOTO, R. Y. Respostas fisiológicas da tilápia-do-nilo e variáveis limnológicas após decomposição de macrófitas utilizando herbicidas. Boletim do Instituto de Pesca, São Paulo, v. 43, n. 4, p. 631-637, 2017.| Biblioteca(s): Embrapa Tabuleiros Costeiros. |
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| 18. | | SALIM, J. A.; VON ZUBEN, F. J.; MORAES, F. R. de; NESHICH, I. A. P.; MAZONI, I.; JARDINE, J.; NESHICH, G. Characterization of catalytic site residues using STING_DB structural descriptors. In: ANNUAL INTERNATIONAL CONFERENCE ON INTELLIGENT SYSTEMS FOR MOLECULAR BIOLOGY; STRUCTURAL BIOINFORMATICS AND COMPUTATIONAL BIOPHYSICS CONFERENCE MEETING, 8., 2012, Long Beach, California. Abstracts... California: ISCB, 2012. Não paginado. Poster. 3DSIG 2012.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 19. | | MORAES, F. R. de; VILLANUEVA, W. J. P.; NESHICH, I. A. P.; MAZONI, I.; NISHIMURA, L.; SALIM, J. A.; JARDINE, J. G.; VON ZUBEN, F.; NESHICH, G. SIPEPPI, a systematic neuron network-based methodology for predicting protein-protein interfaces using STING database descriptors. In: ANNUAL MEETING OF THE SBBq, 40., 2011, Foz do Iguaçu. [Proceedings...]. São Paulo, SP: Brazilian Society for Biochemistry and Molecular Biology, 2011. Não paginado.| Biblioteca(s): Embrapa Agricultura Digital. |
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| Registros recuperados : 32 | |
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 | Acesso ao texto completo restrito à biblioteca da Embrapa Agricultura Digital. Para informações adicionais entre em contato com cnptia.biblioteca@embrapa.br. |
Registro Completo
|
Biblioteca(s): |
Embrapa Agricultura Digital. |
|
Data corrente: |
26/11/2009 |
|
Data da última atualização: |
15/01/2020 |
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Tipo da produção científica: |
Resumo em Anais de Congresso |
|
Autoria: |
JARDINE, J. G.; NESHICH, I. A. P.; MORAES, F. R. de; MAZONI, I.; MANCINI, A.; SALIM, J. A.; NESHICH, G. |
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Afiliação: |
JOSE GILBERTO JARDINE, CNPTIA; IZABELLA AGOSTINHO PENA NESHICH, Estagiária/CNPTIA; FABIO ROGERIO DE MORAES, Bolsista/CNPTIA; IVAN MAZONI, CNPTIA; ADAUTO LUIZ MANCINI, CNPTIA; JOSÉ AUGUSTO SALIM, Estagiário/CNPTIA; GORAN NESHICH, CNPTIA. |
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Título: |
Generation of lipase B mutants with increased surface hydrophobicity in order to improve biodiesel catalysis. |
|
Ano de publicação: |
2009 |
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Fonte/Imprenta: |
In: INTERNATIONAL CONFERENCE OF THE BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 5., 2009, Angra dos Reis. Abstracts book... Angra dos Reis: ABBCB, 2009. |
|
Páginas: |
Não paginado. |
|
Idioma: |
Inglês |
|
Notas: |
X-Meeting 2009. |
|
Conteúdo: |
Biodiesel is a mixture of mono-alkyl esters of long-chain fatty acids and is considered to be a promise as an alternative fuel considering its favorable properties. The industrial production of biodiesel is generally based on transesterification of vegetal oils, in the presence of non-selective inorganic base or acid catalysts. It has been used for decades, but associated problems such as removal of catalysts, excessive energy requirements and the difficulties for purification of glycerol, still have not been solved. An alternative for the high cost to produce Biodiesel is based on enzymatic processes using Lipases as biocatalysts, a methodology that is undergoing a rapid development in accordance with the world demand for clean and selective processes. The use of Lipases as biocatalysts allows easy recovery of glycerol without purification or chemical waste production. Nevertheless, the yield of the process is lower than the one which uses inorganic catalysts. In order to create enzymes more suitable for this procedure, we hypothesized that a Lipase with a more hydrophobic surface would interact better with the substrate in the conversion of oil to biodiesel in a solvent-free system, generating a higher production compared to normal Lipases. Thus, we used the structure of Lipase Novozyme 435 from Candida Antarctica (PDB: 1TCB), which is widely used for this purpose and studied the accessibility to solvent, contact patterns and hydrophobicity of structure. We aimed to identify surface hydrophilic aminoacids which do not neighbor catalytic site nor do they influence important structural features. This enabled us to create mutant proteins with more surface Hydrophobicity. First, using Blue Star STING, we selected hydrophilic aminoacids which are located at surface with high solvent exposure (more than 40% of their total areas) and without contacts with other residues. The selected aminoacids were: Ser5, Thr244 and Arg309 which have, respectively, 111.8, 141.38 and 167.82 °A2 of exposed area at surface. We replaced these hydrophilic aminoacids by hydrophobic ones which have similar total area. The Serine 5 was substituted by an Alanine, the Threonine 244 by a Valine and the Arginine 309 by a Methionine. Finally, we created four modeled mutants using Modeller: the LIP1, which has the Ser5Ala mutation; the LIP2 with the Thr244Val mutation; LIP3, with Arg309Met; and LIP4 with the three mutations together: Ser5Ala, Thr244Val and Arg309Met. Models were validated with Ramanchandran plot analysis and ProSA web. We used the program SurfV to calculate solvent accessibility of the aminoacids, and calculated the Surface Hydrophobicity Index (SHI) with our new (unpublished) methodology using Perl scripts and MySQL. Java Protein Dossier was used to get contacts data and perform select procedure based on multiple selection conditions. We found that these mutations have no consequence on the internal contacts pattern of Lipase and we predict that probably they will not have an influence on catalytic site. Analysis of HSI revealed that the LIP4 mutant had the highest Hydrophobicity on surface (SHI: 0.839) compared to the other mutants and the wild type 1TCB (SHI: 0.712). We suggest LIP4 mutant as a good candidate for experimental test. In addition, the ratio of volume to surface (in A° ) is similar between mutants and wild type, showing there are no significant alterations in volume and total area of protein. Considering the percentage of surface occupied by each group of aminoacids, the LIP4 mutant has 47.4% of surface occupied by hydrophobic aminoacids, and wild type (1TCB) has 43.2%. Hence, we suggest using LIP4 mutant as biocatalyst for Biodiesel production and we expect that it will have a higher efficiency than the wild type. MenosBiodiesel is a mixture of mono-alkyl esters of long-chain fatty acids and is considered to be a promise as an alternative fuel considering its favorable properties. The industrial production of biodiesel is generally based on transesterification of vegetal oils, in the presence of non-selective inorganic base or acid catalysts. It has been used for decades, but associated problems such as removal of catalysts, excessive energy requirements and the difficulties for purification of glycerol, still have not been solved. An alternative for the high cost to produce Biodiesel is based on enzymatic processes using Lipases as biocatalysts, a methodology that is undergoing a rapid development in accordance with the world demand for clean and selective processes. The use of Lipases as biocatalysts allows easy recovery of glycerol without purification or chemical waste production. Nevertheless, the yield of the process is lower than the one which uses inorganic catalysts. In order to create enzymes more suitable for this procedure, we hypothesized that a Lipase with a more hydrophobic surface would interact better with the substrate in the conversion of oil to biodiesel in a solvent-free system, generating a higher production compared to normal Lipases. Thus, we used the structure of Lipase Novozyme 435 from Candida Antarctica (PDB: 1TCB), which is widely used for this purpose and studied the accessibility to solvent, contact patterns and hydrophobicity of structure. We aimed to identi... Mostrar Tudo |
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Palavras-Chave: |
Catálise de biodiesel; Hidrofobicidade; Modeller; Mutantes de lipase B. |
|
Thesaurus NAL: |
Biodiesel; Hydrophobicity; Mutants. |
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Categoria do assunto: |
-- |
|
Marc: |
LEADER 04751nam a2200289 a 4500
001 1576258
005 2020-01-15
008 2009 bl uuuu u00u1 u #d
100 1 $aJARDINE, J. G.
245 $aGeneration of lipase B mutants with increased surface hydrophobicity in order to improve biodiesel catalysis.$h[electronic resource]
260 $aIn: INTERNATIONAL CONFERENCE OF THE BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 5., 2009, Angra dos Reis. Abstracts book... Angra dos Reis: ABBCB$c2009
300 $aNão paginado.
500 $aX-Meeting 2009.
520 $aBiodiesel is a mixture of mono-alkyl esters of long-chain fatty acids and is considered to be a promise as an alternative fuel considering its favorable properties. The industrial production of biodiesel is generally based on transesterification of vegetal oils, in the presence of non-selective inorganic base or acid catalysts. It has been used for decades, but associated problems such as removal of catalysts, excessive energy requirements and the difficulties for purification of glycerol, still have not been solved. An alternative for the high cost to produce Biodiesel is based on enzymatic processes using Lipases as biocatalysts, a methodology that is undergoing a rapid development in accordance with the world demand for clean and selective processes. The use of Lipases as biocatalysts allows easy recovery of glycerol without purification or chemical waste production. Nevertheless, the yield of the process is lower than the one which uses inorganic catalysts. In order to create enzymes more suitable for this procedure, we hypothesized that a Lipase with a more hydrophobic surface would interact better with the substrate in the conversion of oil to biodiesel in a solvent-free system, generating a higher production compared to normal Lipases. Thus, we used the structure of Lipase Novozyme 435 from Candida Antarctica (PDB: 1TCB), which is widely used for this purpose and studied the accessibility to solvent, contact patterns and hydrophobicity of structure. We aimed to identify surface hydrophilic aminoacids which do not neighbor catalytic site nor do they influence important structural features. This enabled us to create mutant proteins with more surface Hydrophobicity. First, using Blue Star STING, we selected hydrophilic aminoacids which are located at surface with high solvent exposure (more than 40% of their total areas) and without contacts with other residues. The selected aminoacids were: Ser5, Thr244 and Arg309 which have, respectively, 111.8, 141.38 and 167.82 °A2 of exposed area at surface. We replaced these hydrophilic aminoacids by hydrophobic ones which have similar total area. The Serine 5 was substituted by an Alanine, the Threonine 244 by a Valine and the Arginine 309 by a Methionine. Finally, we created four modeled mutants using Modeller: the LIP1, which has the Ser5Ala mutation; the LIP2 with the Thr244Val mutation; LIP3, with Arg309Met; and LIP4 with the three mutations together: Ser5Ala, Thr244Val and Arg309Met. Models were validated with Ramanchandran plot analysis and ProSA web. We used the program SurfV to calculate solvent accessibility of the aminoacids, and calculated the Surface Hydrophobicity Index (SHI) with our new (unpublished) methodology using Perl scripts and MySQL. Java Protein Dossier was used to get contacts data and perform select procedure based on multiple selection conditions. We found that these mutations have no consequence on the internal contacts pattern of Lipase and we predict that probably they will not have an influence on catalytic site. Analysis of HSI revealed that the LIP4 mutant had the highest Hydrophobicity on surface (SHI: 0.839) compared to the other mutants and the wild type 1TCB (SHI: 0.712). We suggest LIP4 mutant as a good candidate for experimental test. In addition, the ratio of volume to surface (in A° ) is similar between mutants and wild type, showing there are no significant alterations in volume and total area of protein. Considering the percentage of surface occupied by each group of aminoacids, the LIP4 mutant has 47.4% of surface occupied by hydrophobic aminoacids, and wild type (1TCB) has 43.2%. Hence, we suggest using LIP4 mutant as biocatalyst for Biodiesel production and we expect that it will have a higher efficiency than the wild type.
650 $aBiodiesel
650 $aHydrophobicity
650 $aMutants
653 $aCatálise de biodiesel
653 $aHidrofobicidade
653 $aModeller
653 $aMutantes de lipase B
700 1 $aNESHICH, I. A. P.
700 1 $aMORAES, F. R. de
700 1 $aMAZONI, I.
700 1 $aMANCINI, A.
700 1 $aSALIM, J. A.
700 1 $aNESHICH, G.
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