Stabilization of lipase from Thermomyces lanuginosus by crosslinking in PEGylated polyurethane particles by polymerization: Application on fish oil ethanolysis
The adsorption of Thermomyces lanuginosus lipase (TLL) on PEGylated polyurethane particles as support permitted the development of several strategies to improve the properties of this commercial low-cost enzyme. The supports were synthesized by miniemulsion technique using isophoronediisocyanate (IPDI) and poly(ε-caprolactone) diol (PCL530) as monomers. The aqueous phase was composed of distilled water, surfactant sodium dodecyl sulfate (SDS), and poly(ethylene glycol) with different molar mass (PEG 400, 4000 or 6000). Polyethyleneimine (PEI) and trehalose were used to coat the PU-PEG polyurethane particles in order to increase the stability. In general, the coating with PEI (20%) allowed a greater stability of the derivatives. (100% of relative activity at 50 °C during 8 h). TLL immobilized on PEGylated polyurethane particles was efficiently used in the production of ethyl esters from fish oil compared to the free TLL (data not shown). The values of ethyl esters production of EPA and DHA were dependent on the support used for immobilization, which proved to be a determining factor in the activity. The highest selectivity obtained value was 45.8 for the PU-PEG4000-PEI20 derivative.
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Elsevier
2016
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Subjects: | Immobilized enzymes, Enzyme biocatalysis, Lipase, Biocatalysis, Enzyme activity, Adsorption, |
Online Access: | http://hdl.handle.net/10261/150071 http://dx.doi.org/10.13039/501100002322 |
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dig-cial-es-10261-1500712018-09-20T10:51:55Z Stabilization of lipase from Thermomyces lanuginosus by crosslinking in PEGylated polyurethane particles by polymerization: Application on fish oil ethanolysis Pereira Cipolatti, Eliane Oliveira, Débora de Pessela, Benevides C. Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brasil) Immobilized enzymes Enzyme biocatalysis Lipase Biocatalysis Enzyme activity Adsorption The adsorption of Thermomyces lanuginosus lipase (TLL) on PEGylated polyurethane particles as support permitted the development of several strategies to improve the properties of this commercial low-cost enzyme. The supports were synthesized by miniemulsion technique using isophoronediisocyanate (IPDI) and poly(ε-caprolactone) diol (PCL530) as monomers. The aqueous phase was composed of distilled water, surfactant sodium dodecyl sulfate (SDS), and poly(ethylene glycol) with different molar mass (PEG 400, 4000 or 6000). Polyethyleneimine (PEI) and trehalose were used to coat the PU-PEG polyurethane particles in order to increase the stability. In general, the coating with PEI (20%) allowed a greater stability of the derivatives. (100% of relative activity at 50 °C during 8 h). TLL immobilized on PEGylated polyurethane particles was efficiently used in the production of ethyl esters from fish oil compared to the free TLL (data not shown). The values of ethyl esters production of EPA and DHA were dependent on the support used for immobilization, which proved to be a determining factor in the activity. The highest selectivity obtained value was 45.8 for the PU-PEG4000-PEI20 derivative. The authors thank the financial support from CAPES (Coordenação de Aperfeiçoamento de Pessoal de Nível Superior) for the Programa de Doutorado Sanduíche no Exterior, Project BEX 2569/14-0 and the direction of the Instituto de Investigación en Ciencias de la Alimentación for helping in the development of this work. Peer Reviewed 2017-05-22T07:38:00Z 2017-05-22T07:38:00Z 2016 2017-05-22T07:38:00Z artículo http://purl.org/coar/resource_type/c_6501 doi: 10.1016/j.bej.2016.04.006 issn: 1369-703X Biochemical Engineering Journal 112: 54-60 (2016) http://hdl.handle.net/10261/150071 10.1016/j.bej.2016.04.006 http://dx.doi.org/10.13039/501100002322 Sí none Elsevier |
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Immobilized enzymes Enzyme biocatalysis Lipase Biocatalysis Enzyme activity Adsorption Immobilized enzymes Enzyme biocatalysis Lipase Biocatalysis Enzyme activity Adsorption |
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Immobilized enzymes Enzyme biocatalysis Lipase Biocatalysis Enzyme activity Adsorption Immobilized enzymes Enzyme biocatalysis Lipase Biocatalysis Enzyme activity Adsorption Pereira Cipolatti, Eliane Oliveira, Débora de Pessela, Benevides C. Stabilization of lipase from Thermomyces lanuginosus by crosslinking in PEGylated polyurethane particles by polymerization: Application on fish oil ethanolysis |
description |
The adsorption of Thermomyces lanuginosus lipase (TLL) on PEGylated polyurethane particles as support permitted the development of several strategies to improve the properties of this commercial low-cost enzyme. The supports were synthesized by miniemulsion technique using isophoronediisocyanate (IPDI) and poly(ε-caprolactone) diol (PCL530) as monomers. The aqueous phase was composed of distilled water, surfactant sodium dodecyl sulfate (SDS), and poly(ethylene glycol) with different molar mass (PEG 400, 4000 or 6000). Polyethyleneimine (PEI) and trehalose were used to coat the PU-PEG polyurethane particles in order to increase the stability. In general, the coating with PEI (20%) allowed a greater stability of the derivatives. (100% of relative activity at 50 °C during 8 h). TLL immobilized on PEGylated polyurethane particles was efficiently used in the production of ethyl esters from fish oil compared to the free TLL (data not shown). The values of ethyl esters production of EPA and DHA were dependent on the support used for immobilization, which proved to be a determining factor in the activity. The highest selectivity obtained value was 45.8 for the PU-PEG4000-PEI20 derivative. |
author2 |
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brasil) |
author_facet |
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (Brasil) Pereira Cipolatti, Eliane Oliveira, Débora de Pessela, Benevides C. |
format |
artículo |
topic_facet |
Immobilized enzymes Enzyme biocatalysis Lipase Biocatalysis Enzyme activity Adsorption |
author |
Pereira Cipolatti, Eliane Oliveira, Débora de Pessela, Benevides C. |
author_sort |
Pereira Cipolatti, Eliane |
title |
Stabilization of lipase from Thermomyces lanuginosus by crosslinking in PEGylated polyurethane particles by polymerization: Application on fish oil ethanolysis |
title_short |
Stabilization of lipase from Thermomyces lanuginosus by crosslinking in PEGylated polyurethane particles by polymerization: Application on fish oil ethanolysis |
title_full |
Stabilization of lipase from Thermomyces lanuginosus by crosslinking in PEGylated polyurethane particles by polymerization: Application on fish oil ethanolysis |
title_fullStr |
Stabilization of lipase from Thermomyces lanuginosus by crosslinking in PEGylated polyurethane particles by polymerization: Application on fish oil ethanolysis |
title_full_unstemmed |
Stabilization of lipase from Thermomyces lanuginosus by crosslinking in PEGylated polyurethane particles by polymerization: Application on fish oil ethanolysis |
title_sort |
stabilization of lipase from thermomyces lanuginosus by crosslinking in pegylated polyurethane particles by polymerization: application on fish oil ethanolysis |
publisher |
Elsevier |
publishDate |
2016 |
url |
http://hdl.handle.net/10261/150071 http://dx.doi.org/10.13039/501100002322 |
work_keys_str_mv |
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