Immobilization of Moniliella spathulata R25L270 lipase on ionic, hydrophobic and covalent supports: Functional properties and hydrolysis of sardine oil
This article belongs to the Special Issue Lipases and Lipases Modification.
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Multidisciplinary Digital Publishing Institute
2017
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| Subjects: | Lipase, Moniliella spathulata, Immobilization, Fish oil, Omega-3, |
| Online Access: | http://hdl.handle.net/10261/194146 http://dx.doi.org/10.13039/501100007392 http://dx.doi.org/10.13039/501100004901 http://dx.doi.org/10.13039/501100002322 http://dx.doi.org/10.13039/501100003593 |
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dig-cial-es-10261-1941462019-11-08T03:12:18Z Immobilization of Moniliella spathulata R25L270 lipase on ionic, hydrophobic and covalent supports: Functional properties and hydrolysis of sardine oil Souza, Lívia T. A. Moreno-Pérez, Sonia Fernández-Lorente, Gloria Cipolatti, Eliane P. Oliveira, Débora de Resende, Rodrigo R. Pessela, Benevides C. Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasil) Instituto Nacional de Ciência e Tecnologia em Nanomateriais de Carbono (Brasil) Fundações de Amparo à Pesquisa (Brasil) Fundação de Amparo à Pesquisa do Estado de São Paulo Minas Gerais Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brasil) Cipolatti, Eliane P. [0000-0002-3272-712X] Lipase Moniliella spathulata Immobilization Fish oil Omega-3 This article belongs to the Special Issue Lipases and Lipases Modification. The oleaginous yeast Moniliella spathulata R25L270 was the first yeast able to grow and produce extracellular lipase using Macaúba (Acrocomia aculeate) cake as substrate. The novel lipase was recently identified, and presented promising features for biotechnological applications. The M. spathulata R25L270 lipase efficiently hydrolyzed vegetable and animal oils, and showed selectivity for generating cis-5,8,11,15,17-eicosapentaenoic acid from sardine oil. The enzyme can act in a wide range of temperatures (25–48 °C) and pH (6.5–8.4). The present study deals with the immobilization of M. spathulata R25L270 lipase on hydrophobic, covalent and ionic supports to select the most active biocatalyst capable to obtain omega-3 fatty acids (PUFA) from sardine oil. Nine immobilized agarose derivatives were prepared and biochemically characterized for thermostability, pH stability and catalytic properties (KM and Vmax). Ionic supports improved the enzyme–substrate affinity; however, it was not an effective strategy to increase the M. spathulata R25L270 lipase stability against pH and temperature. Covalent support resulted in a biocatalyst with decreased activity, but high thermostability. The enzyme was most stabilized when immobilized on hydrophobic supports, especially Octyl-Sepharose. Compared with the free enzyme, the half-life of the Octyl-Sepharose derivative at 60 °C increased 10-fold, and lipase stability under acidic conditions was achieved. The Octyl-Sepharose derivative was selected to obtain omega-3 fatty acids from sardine oil, and the maximal enzyme selectivity was achieved at pH 5.0. This research was supported by Brazilian agencies: Instituto Nanocell, CNPq (Conselho Nacional de Desenvolvimento Científico e Tecnológico), INCT (Instituto Nacional de Ciência e Tecnologia) de Nanomateriais de Carbono, FAPEMIG (Fundação de Amparo à Pesquisa do Estado de Minas Gerais), Rede Mineira de Toxinas com Ação Terapêutica, Pro-Reitoria de Pesquisa da UFMG and CAPES (Coordenação de Aperfeiçoamento de Pessoal de Nível Superior- Processo: BEX 2703/14-9). Peer reviewed 2019-11-07T12:47:15Z 2019-11-07T12:47:15Z 2017 artículo http://purl.org/coar/resource_type/c_6501 Molecules 22(10): 1508 (2017) http://hdl.handle.net/10261/194146 10.3390/molecules22101508 1420-3049 http://dx.doi.org/10.13039/501100007392 http://dx.doi.org/10.13039/501100004901 http://dx.doi.org/10.13039/501100002322 http://dx.doi.org/10.13039/501100003593 28946698 en Publisher's version https://doi.org/10.3390/molecules22101508 Sí open Multidisciplinary Digital Publishing Institute |
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Lipase Moniliella spathulata Immobilization Fish oil Omega-3 Lipase Moniliella spathulata Immobilization Fish oil Omega-3 |
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Lipase Moniliella spathulata Immobilization Fish oil Omega-3 Lipase Moniliella spathulata Immobilization Fish oil Omega-3 Souza, Lívia T. A. Moreno-Pérez, Sonia Fernández-Lorente, Gloria Cipolatti, Eliane P. Oliveira, Débora de Resende, Rodrigo R. Pessela, Benevides C. Immobilization of Moniliella spathulata R25L270 lipase on ionic, hydrophobic and covalent supports: Functional properties and hydrolysis of sardine oil |
| description |
This article belongs to the Special Issue Lipases and Lipases Modification. |
| author2 |
Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasil) |
| author_facet |
Conselho Nacional de Desenvolvimento Científico e Tecnológico (Brasil) Souza, Lívia T. A. Moreno-Pérez, Sonia Fernández-Lorente, Gloria Cipolatti, Eliane P. Oliveira, Débora de Resende, Rodrigo R. Pessela, Benevides C. |
| format |
artículo |
| topic_facet |
Lipase Moniliella spathulata Immobilization Fish oil Omega-3 |
| author |
Souza, Lívia T. A. Moreno-Pérez, Sonia Fernández-Lorente, Gloria Cipolatti, Eliane P. Oliveira, Débora de Resende, Rodrigo R. Pessela, Benevides C. |
| author_sort |
Souza, Lívia T. A. |
| title |
Immobilization of Moniliella spathulata R25L270 lipase on ionic, hydrophobic and covalent supports: Functional properties and hydrolysis of sardine oil |
| title_short |
Immobilization of Moniliella spathulata R25L270 lipase on ionic, hydrophobic and covalent supports: Functional properties and hydrolysis of sardine oil |
| title_full |
Immobilization of Moniliella spathulata R25L270 lipase on ionic, hydrophobic and covalent supports: Functional properties and hydrolysis of sardine oil |
| title_fullStr |
Immobilization of Moniliella spathulata R25L270 lipase on ionic, hydrophobic and covalent supports: Functional properties and hydrolysis of sardine oil |
| title_full_unstemmed |
Immobilization of Moniliella spathulata R25L270 lipase on ionic, hydrophobic and covalent supports: Functional properties and hydrolysis of sardine oil |
| title_sort |
immobilization of moniliella spathulata r25l270 lipase on ionic, hydrophobic and covalent supports: functional properties and hydrolysis of sardine oil |
| publisher |
Multidisciplinary Digital Publishing Institute |
| publishDate |
2017 |
| url |
http://hdl.handle.net/10261/194146 http://dx.doi.org/10.13039/501100007392 http://dx.doi.org/10.13039/501100004901 http://dx.doi.org/10.13039/501100002322 http://dx.doi.org/10.13039/501100003593 |
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