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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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Biblioteca |
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Origem |
Tipo/Formato |
Classificação |
Cutter |
Registro |
Volume |
Status |
URL |
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Registro Completo
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Biblioteca(s): |
Embrapa Semiárido. |
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Data corrente: |
04/11/2003 |
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Data da última atualização: |
07/06/2018 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
Nacional - B |
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Autoria: |
LEAO, P. C. de S. |
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Afiliação: |
PATRICIA COELHO DE SOUZA LEAO, CPATSA. |
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Título: |
Thompson Seedless: potencial para cultivo no Vale do São Francisco. |
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Ano de publicação: |
2003 |
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Fonte/Imprenta: |
Item, Brasília, n 59, p. 16-20, 2003. |
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Idioma: |
Português |
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Conteúdo: |
Características da variedade Thompson Seedless no Vale do São Francisco; Fenologia; Fertilidade da gema. |
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Palavras-Chave: |
Cultivo; Uva sem sementes; Vale do São Francisco. |
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Thesagro: |
Fenologia; Uva; Variedade. |
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Thesaurus NAL: |
Grapes. |
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Categoria do assunto: |
F Plantas e Produtos de Origem Vegetal |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/178283/1/Patricia-1.pdf
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Marc: |
LEADER 00631naa a2200205 a 4500
001 1152196
005 2018-06-07
008 2003 bl uuuu u00u1 u #d
100 1 $aLEAO, P. C. de S.
245 $aThompson Seedless$bpotencial para cultivo no Vale do São Francisco.
260 $c2003
520 $aCaracterísticas da variedade Thompson Seedless no Vale do São Francisco; Fenologia; Fertilidade da gema.
650 $aGrapes
650 $aFenologia
650 $aUva
650 $aVariedade
653 $aCultivo
653 $aUva sem sementes
653 $aVale do São Francisco
773 $tItem, Brasília, n 59, p. 16-20, 2003.
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Embrapa Semiárido (CPATSA) |
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