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Registro Completo |
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Biblioteca(s): |
Embrapa Agroindústria Tropical. |
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Data corrente: |
12/01/2024 |
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Data da última atualização: |
12/01/2024 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
BRIGIDA, A. I. S.; BUARQUE, F. S.; NOGUEIRA, V. L. R.; MELO, V. M. M.; GUISÁN SEIJAS, J. M.; RIBEIRO, B. D.; GONÇALVES, L. R. B.; COELHO, M. A. Z. |
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Afiliação: |
ANA IRAIDY SANTA BRIGIDA, CNPAT; FILIPE SMITH BUARQUE, UNIVERSIDADE FEDERAL DO RIO DE JANEIRO; VANESSA LÚCIA RODRIGUES NOGUEIRA, UNIVERSIDADE FEDERAL DO CEARÁ; VÂNIA MARIA MACIEL MELO, UNIVERSIDADE FEDERAL DO CEARÁ; JOSÉ MANUEL GUISÁN SEIJAS, INSTITUTE OF CATALYSIS AND PETROCHEMISTRY; BERNARDO DIAS RIBEIRO, UNIVERSIDADE FEDERAL DO RIO DE JANEIRO; LUCIANA ROCHA BARROS GONÇALVES, UNIVERSIDADE FEDERAL DO CEARÁ; MARIA ALICE ZARUR COELHO, UNIVERSIDADE FEDERAL DO RIO DE JANEIRO. |
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Título: |
Partial purification of crude lipase extract from Yarrowia lipolytica: precipitation, aqueous two-phase systems (ATPS), and immobilization methods. |
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Ano de publicação: |
2023 |
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Fonte/Imprenta: |
Cleaner Chemical Engineering, v. 6, 11 p., art. 100105, June 2023. |
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DOI: |
10.1016/j.clce.2023.100105 |
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Idioma: |
Inglês |
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Conteúdo: |
Efforts have been concentrated on developing alternative methods of enzyme purification that are less costly and highly efficient. In this work, we evaluated three different methods for lipase purification from Yarrowia lipolytica, such as precipitation using ammonium sulfate, ethanol, or acetone; aqueous two-phase systems (ATPS) based on polyethylene glycol (PEG) and potassium phosphate; and direct immobilization. It was impossible to obtain stable precipitates of the enzyme due to the low concentration of total protein and the presence of biosurfactant produced by the microorganism. Different mixture compositions were selected for the partitioning study. Three ATPS showed selective partitioning of the target enzymes, i.e., lipase and protease migrated to opposite phases. In the ATPS composed of 13 wt% PEG-4000 and 10 wt% salts, it was possible to achieve a purification factor for lipase of 4.2. Purification by immobilization performed by lipase-lipase interactions showed three lipases of distinct sizes in the crude extract. In the immobilization method by hydrophobic supports, phenyl-agarose and butyl‑agarose were more selective in immobilizing than octyl-agarose. In the ion exchange immobilization method, only the lipases identified at 66 kDa and 41 kDa have an attraction for DEAE-agarose (anionic) and sulfopropyl-agarose (cationic) matrices. |
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Palavras-Chave: |
Aqueous biphasic system; Aqueous two-phase system; Sistema aquoso bifásico; Sistema aquoso em duas fases. |
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Thesaurus Nal: |
Chemical precipitation; Purification methods; Yarrowia lipolytica. |
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Categoria do assunto: |
W Química e Física |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/doc/1160760/1/ART-23038.pdf
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Marc: |
LEADER 02400naa a2200301 a 4500
001 2160760
005 2024-01-12
008 2023 bl uuuu u00u1 u #d
024 7 $a10.1016/j.clce.2023.100105$2DOI
100 1 $aBRIGIDA, A. I. S.
245 $aPartial purification of crude lipase extract from Yarrowia lipolytica$bprecipitation, aqueous two-phase systems (ATPS), and immobilization methods.$h[electronic resource]
260 $c2023
520 $aEfforts have been concentrated on developing alternative methods of enzyme purification that are less costly and highly efficient. In this work, we evaluated three different methods for lipase purification from Yarrowia lipolytica, such as precipitation using ammonium sulfate, ethanol, or acetone; aqueous two-phase systems (ATPS) based on polyethylene glycol (PEG) and potassium phosphate; and direct immobilization. It was impossible to obtain stable precipitates of the enzyme due to the low concentration of total protein and the presence of biosurfactant produced by the microorganism. Different mixture compositions were selected for the partitioning study. Three ATPS showed selective partitioning of the target enzymes, i.e., lipase and protease migrated to opposite phases. In the ATPS composed of 13 wt% PEG-4000 and 10 wt% salts, it was possible to achieve a purification factor for lipase of 4.2. Purification by immobilization performed by lipase-lipase interactions showed three lipases of distinct sizes in the crude extract. In the immobilization method by hydrophobic supports, phenyl-agarose and butyl‑agarose were more selective in immobilizing than octyl-agarose. In the ion exchange immobilization method, only the lipases identified at 66 kDa and 41 kDa have an attraction for DEAE-agarose (anionic) and sulfopropyl-agarose (cationic) matrices.
650 $aChemical precipitation
650 $aPurification methods
650 $aYarrowia lipolytica
653 $aAqueous biphasic system
653 $aAqueous two-phase system
653 $aSistema aquoso bifásico
653 $aSistema aquoso em duas fases
700 1 $aBUARQUE, F. S.
700 1 $aNOGUEIRA, V. L. R.
700 1 $aMELO, V. M. M.
700 1 $aGUISÁN SEIJAS, J. M.
700 1 $aRIBEIRO, B. D.
700 1 $aGONÇALVES, L. R. B.
700 1 $aCOELHO, M. A. Z.
773 $tCleaner Chemical Engineering$gv. 6, 11 p., art. 100105, June 2023.
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Embrapa Agroindústria Tropical (CNPAT) |
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