Application of immobilized <scp> <i>Burkholderia cepacia</i> </scp> lipase on clay in the production of ethyl esters

Abstract The present work aimed to use commercial Spectrogel clay (type C) as a support for immobilizing Burkholderia cepacia lipase to produce ethyl esters. The highest yield in ethyl ester production was obtained under the following conditions: 1% water (kg kg −1 oil), oil‐to‐ethanol molar ratio of 1:3, and 15% immobilized biocatalyst (kg kg −1 oil). A kinetic assay was conducted under the optimal conditions obtained to validate the experiment, which already showed a high yield within 6 h (78.82 ± 2.28% for LBC‐ADS and 89.42 ± 2.65% for LBC‐CB) and reaction equilibrium in 18 h (84.76 ± 0.36% for LBC‐ADS and 98.05 ± 1.24% for LBC‐CB). Heterogeneity tests were conducted at 1 and 12 h of reaction to analyze the interaction between the support and the enzyme, showing that after the removal of the biocatalysts after 1 h of reaction, there was no significant release of enzymes into the reaction medium.

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Publication Details

Journal
The Canadian Journal of Chemical Engineering
Published
2025-02-18
DOI
https://doi.org/10.1002/cjce.25648
Primary Topic
Enzyme Catalysis and Immobilization
Type
article
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article

Application of immobilized Burkholderia cepacia lipase on clay in the production of ethyl esters

Edson Antônio da Silva, Sirlei Marques Paschoal, Deise Molinari, Ana Caroline Raimundini Aranha et al.
The Canadian Journal of Chemical Engineering
Enzyme Catalysis and Immobilization
article

Application of immobilized Burkholderia cepacia lipase on clay in the production of ethyl esters

Edson Antônio da Silva, Sirlei Marques Paschoal, Deise Molinari, Ana Caroline Raimundini Aranha, Pedro Augusto Arroyo, Gisella Maria Zanin, Lucas Silva Figueiredo, Emerson Barrios Mogollón
article en

Abstract

Abstract The present work aimed to use commercial Spectrogel clay (type C) as a support for immobilizing Burkholderia cepacia lipase to produce ethyl esters. The highest yield in ethyl ester production was obtained under the following conditions: 1% water (kg kg −1 oil), oil‐to‐ethanol molar ratio of 1:3, and 15% immobilized biocatalyst (kg kg −1 oil). A kinetic assay was conducted under the optimal conditions obtained to validate the experiment, which already showed a high yield within 6 h (78.82 ± 2.28% for LBC‐ADS and 89.42 ± 2.65% for LBC‐CB) and reaction equilibrium in 18 h (84.76 ± 0.36% for LBC‐ADS and 98.05 ± 1.24% for LBC‐CB). Heterogeneity tests were conducted at 1 and 12 h of reaction to analyze the interaction between the support and the enzyme, showing that after the removal of the biocatalysts after 1 h of reaction, there was no significant release of enzymes into the reaction medium.

The Canadian Journal of Chemical EngineeringVol. 103(9)
Universidade Estadual de Maringá (BR), Universidade Estadual do Oeste do Paraná (BR)
Clean water and sanitation
Openalex Percentile: Top 97%
Enzyme Catalysis and Immobilization
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Application of immobilized <scp> <i>Burkholderia cepacia</i> </scp> lipase on clay in the production of ethyl esters — Edson Antônio da Silva, Sirlei Marques Paschoal, et al. · The Canadian Journal of Chemical Engineering (2025) | TGRS Research Map | TGRS