Hydrophobic immobilization of Burkholderia cepacia lipase onto octyl-silica for synthesis of flavors esters / Imobilização hidrofóbica da lipase de Burkholderia cepacia sobre octil-sílica para síntese de ésteres de sabores
Burkholderia cepacia lipase (BCL) was immobilized onto silica modified with octyl groups (OS) and the biocatalyst (BCL-OS) was evaluated as its performance in the synthesis in organic medium (synthesis of flavor esters as a model). The maximum support loading was 0.375 genzyme/gsupport, yielding a b...
| Autores: | , , , , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2020 |
| País: | Brasil |
| Institución: | Instituto Superior de Educação Vera Cruz (VeraCruz) |
| Repositorio: | Revista Veras |
| Idioma: | portugués |
| OAI Identifier: | oai:ojs2.ojs.brazilianjournals.com.br:article/9975 |
| Acceso en línea: | https://ojs.brazilianjournals.com.br/ojs/index.php/BRJD/article/view/9975 |
| Access Level: | acceso abierto |
| Palabra clave: | octyl-modified silica hydrophobic immobilization lipase esterification flavor esters. |
| Sumario: | Burkholderia cepacia lipase (BCL) was immobilized onto silica modified with octyl groups (OS) and the biocatalyst (BCL-OS) was evaluated as its performance in the synthesis in organic medium (synthesis of flavor esters as a model). The maximum support loading was 0.375 genzyme/gsupport, yielding a biocatalyst with an activity of 1197 U/gsupport at pH 7.0 and 50 °C in the hydrolysis of olive oil. The biocatalyst BCL-OS showed to be 9-fold more stable than the free lipase at 60°C in buffer solution (absence of substrates), with an increase of half-life from 16 to 144 h. The physical-chemical characterization of silica, octyl silica, and BCL-OS biocatalyst allowed confirming the immobilization of BCL onto the modified silica. The biocatalyst had an excellent performance in the synthesis of flavor esters, yielding more than 85% esterification yield (based on acid consumption) for acetic and butyric acids as acyl donors, and ethanol, butanol and hexanol as acyl acceptors. The biocatalyst could be recycled by ten 5 h-cycles of butyl butyrate syntheses at 37°C in heptane, retaining around 80% of its initial activity. Therefore, these results indicate that the BCL immobilized onto silica modified with octyl groups is a promising biocatalyst for application in organic syntheses. |
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