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Registro Completo |
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Biblioteca(s): |
Embrapa Agroenergia. |
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Data corrente: |
04/08/2022 |
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Data da última atualização: |
04/08/2022 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
MARTINS, P. A.; TROBO-MASEDA, L.; LIMA, F. A.; MORAIS JÚNIOR, W. G. DE; MARCO, J. LISBOA DE; SALUM, T. F. C.; GUISAN, J. M. |
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Afiliação: |
PEDRO ALVES MARTINS, Universidade de Brasília; LARA TROBO-MASEDA, Instituto de Catalisis y Petroleoquímica, Madrid, Spain; FREDERICO ALVES LIMA, Instituto de Catalisis y Petroleoquímica, Madrid, Spain; WILSON GALVAO DE MORAIS JÚNIOR, Instituto de Catalisis y Petroleoquímica, Madrid, Spain; JANICE LISBOA DE MARCO, Universidade de Brasília; THAIS FABIANA CHAN SALUM, CNPAE; JOSE MANUEL GUISAN, Instituto de Catalisis y Petroleoquímica, Madrid, Spain. |
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Título: |
Omega-3 production by fish oil hydrolysis using a lipase from Burkholderia gladioli BRM58833 immobilized and stabilized by post-immobilization techniques. |
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Ano de publicação: |
2022 |
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Fonte/Imprenta: |
Biochemistry and Biophysics Reports, v. 29, 101193, 2022. |
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Idioma: |
Português |
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Conteúdo: |
Immobilization of lipase from Burkholderia gladioli BRM58833 on octyl sepharose (OCT) resulted in catalysts with higher activity and stability. Following, strategies were studied to further stabilize and secure the enzyme to the support using functionalized polymers, like polyethylenimine (PEI) and aldehyde-dextran (DEXa), to cover the catalyst with layers at different combinations. Alternatively, the construction of a bifunctional layer was studied using methoxypolyethylene glycol amine (NH 2 -PEG) and glycine. The catalyst OCT-PEI-DEXa was the most thermostable, with a 263.8-fold increase in stability when compared to the control condition. When evaluated under alkaline conditions, OCT-DEXa-PEG 10 /Gly was the most stable, reaching stability 70.1 times greater than the control condition. Proportionally, the stabilization obtained for B. gladioli BRM58833 lipase was superior to that obtained for the commercial B. cepacia lipase. Preliminary results in the hydrolysis of fish oil demonstrated the potential of the coating technique with bifunctional polymers, resulting in a stable catalyst with greater catalytic capacity for the production of omega-3 PUFAs. According to the results obtained, it is possible to modulate B. gladioli BRM58833 lipase properties like stability and catalytic activity for enrichment of omega-3 fatty acids. |
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Palavras-Chave: |
Enzyme stabilization. |
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Thesagro: |
Lípase. |
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Categoria do assunto: |
-- |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/doc/1145248/1/SALUM-et-al.-Artigo-SI-12.15.00.007.00.05.001.pdf
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Marc: |
LEADER 02071naa a2200217 a 4500
001 2145248
005 2022-08-04
008 2022 bl uuuu u00u1 u #d
100 1 $aMARTINS, P. A.
245 $aOmega-3 production by fish oil hydrolysis using a lipase from Burkholderia gladioli BRM58833 immobilized and stabilized by post-immobilization techniques.$h[electronic resource]
260 $c2022
520 $aImmobilization of lipase from Burkholderia gladioli BRM58833 on octyl sepharose (OCT) resulted in catalysts with higher activity and stability. Following, strategies were studied to further stabilize and secure the enzyme to the support using functionalized polymers, like polyethylenimine (PEI) and aldehyde-dextran (DEXa), to cover the catalyst with layers at different combinations. Alternatively, the construction of a bifunctional layer was studied using methoxypolyethylene glycol amine (NH 2 -PEG) and glycine. The catalyst OCT-PEI-DEXa was the most thermostable, with a 263.8-fold increase in stability when compared to the control condition. When evaluated under alkaline conditions, OCT-DEXa-PEG 10 /Gly was the most stable, reaching stability 70.1 times greater than the control condition. Proportionally, the stabilization obtained for B. gladioli BRM58833 lipase was superior to that obtained for the commercial B. cepacia lipase. Preliminary results in the hydrolysis of fish oil demonstrated the potential of the coating technique with bifunctional polymers, resulting in a stable catalyst with greater catalytic capacity for the production of omega-3 PUFAs. According to the results obtained, it is possible to modulate B. gladioli BRM58833 lipase properties like stability and catalytic activity for enrichment of omega-3 fatty acids.
650 $aLípase
653 $aEnzyme stabilization
700 1 $aTROBO-MASEDA, L.
700 1 $aLIMA, F. A.
700 1 $aMORAIS JÚNIOR, W. G. DE
700 1 $aMARCO, J. LISBOA DE
700 1 $aSALUM, T. F. C.
700 1 $aGUISAN, J. M.
773 $tBiochemistry and Biophysics Reports$gv. 29, 101193, 2022.
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Registro original: |
Embrapa Agroenergia (CNPAE) |
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| 1. |  | MARTINS, P. A.; TROBO-MASEDA, L.; LIMA, F. A.; MORAIS JÚNIOR, W. G. DE; MARCO, J. LISBOA DE; SALUM, T. F. C.; GUISAN, J. M. Omega-3 production by fish oil hydrolysis using a lipase from Burkholderia gladioli BRM58833 immobilized and stabilized by post-immobilization techniques. Biochemistry and Biophysics Reports, v. 29, 101193, 2022.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: B - 3 |
| Biblioteca(s): Embrapa Agroenergia. |
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