Ionic liquid supported hydrogel-lipase biocatalytic systems in asymmetric synthesis of enantiomerically pure S-ibuprofen.
- Publisher:
- ELSEVIER
- Publication Type:
- Journal Article
- Citation:
- Int J Biol Macromol, 2024, 281, (Pt 1), pp. 136221
- Issue Date:
- 2024-11
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Field | Value | Language |
---|---|---|
dc.contributor.author | Degórska, O | |
dc.contributor.author | Szada, D | |
dc.contributor.author |
Fu, Q |
|
dc.contributor.author | Nghiem, LD | |
dc.contributor.author | Biadasz, A | |
dc.contributor.author | Jesionowski, T | |
dc.contributor.author | Zdarta, J | |
dc.date.accessioned | 2025-02-27T21:44:21Z | |
dc.date.available | 2024-09-30 | |
dc.date.available | 2025-02-27T21:44:21Z | |
dc.date.issued | 2024-11 | |
dc.identifier.citation | Int J Biol Macromol, 2024, 281, (Pt 1), pp. 136221 | |
dc.identifier.issn | 0141-8130 | |
dc.identifier.issn | 1879-0003 | |
dc.identifier.uri | http://hdl.handle.net/10453/185399 | |
dc.description.abstract | Novel hydrogel biocatalysts with immobilized lipase, stabilized by ionic liquids (ILs) of different hydrophobicity, were synthesized and evaluated. Variations of the time of immobilization and ratio of substrates during hydrogel synthesis were considered to obtain the most stable biocatalyst with the highest activity. Physicochemical characterization proved the success of the hydrogel synthesis and enzyme deposition on the surface of the support. Nevertheless, the key objective was to produce a biocatalyst for further application in ibuprofen methyl ester resolution, with the aim of obtaining an enantiomerically pure product. The hydrogel biocatalysts obtained in the presence of 5 wt% ILs after 8 h of immobilization achieved the highest activity recovery of 62 %. After 10 reaction cycles, enzymatic activity was still above 60 %, and the negative effect of pH and temperature on the activity of immobilized lipase was much lower than in the case of the free enzyme. After application of the catalyst in the resolution of ibuprofen methyl ester, the enantiomeric excess and conversion rate of the process were obtained for the dynamic kinetic resolution in isooctane. A conversion rate of 95 % was achieved due to the stabilization of the biocatalyst with IL and its resulting high catalytic activity. The study thus provides the pharmaceutical industry with a new potential approach with a strong scientific foundation. | |
dc.format | Print-Electronic | |
dc.language | eng | |
dc.publisher | ELSEVIER | |
dc.relation | http://purl.org/au-research/grants/arc/FT180100312 | |
dc.relation.ispartof | Int J Biol Macromol | |
dc.relation.isbasedon | 10.1016/j.ijbiomac.2024.136221 | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.subject | 0601 Biochemistry and Cell Biology | |
dc.subject.classification | Polymers | |
dc.subject.classification | 3101 Biochemistry and cell biology | |
dc.subject.mesh | Ibuprofen | |
dc.subject.mesh | Lipase | |
dc.subject.mesh | Ionic Liquids | |
dc.subject.mesh | Enzymes, Immobilized | |
dc.subject.mesh | Biocatalysis | |
dc.subject.mesh | Stereoisomerism | |
dc.subject.mesh | Temperature | |
dc.subject.mesh | Hydrogen-Ion Concentration | |
dc.subject.mesh | Hydrogels | |
dc.subject.mesh | Kinetics | |
dc.subject.mesh | Ibuprofen | |
dc.subject.mesh | Enzymes, Immobilized | |
dc.subject.mesh | Lipase | |
dc.subject.mesh | Hydrogels | |
dc.subject.mesh | Temperature | |
dc.subject.mesh | Kinetics | |
dc.subject.mesh | Stereoisomerism | |
dc.subject.mesh | Hydrogen-Ion Concentration | |
dc.subject.mesh | Ionic Liquids | |
dc.subject.mesh | Biocatalysis | |
dc.subject.mesh | Ibuprofen | |
dc.subject.mesh | Lipase | |
dc.subject.mesh | Ionic Liquids | |
dc.subject.mesh | Enzymes, Immobilized | |
dc.subject.mesh | Biocatalysis | |
dc.subject.mesh | Stereoisomerism | |
dc.subject.mesh | Temperature | |
dc.subject.mesh | Hydrogen-Ion Concentration | |
dc.subject.mesh | Hydrogels | |
dc.subject.mesh | Kinetics | |
dc.title | Ionic liquid supported hydrogel-lipase biocatalytic systems in asymmetric synthesis of enantiomerically pure S-ibuprofen. | |
dc.type | Journal Article | |
utslib.citation.volume | 281 | |
utslib.location.activity | Netherlands | |
utslib.for | 0601 Biochemistry and Cell Biology | |
pubs.organisational-group | University of Technology Sydney | |
pubs.organisational-group | University of Technology Sydney/Faculty of Engineering and Information Technology | |
pubs.organisational-group | University of Technology Sydney/Faculty of Engineering and Information Technology/School of Civil and Environmental Engineering | |
pubs.organisational-group | University of Technology Sydney/UTS Groups | |
pubs.organisational-group | University of Technology Sydney/UTS Groups/Centre for Technology in Water and Wastewater (CTWW) | |
utslib.copyright.status | open_access | * |
dc.rights.license | This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0). To view a copy of this license, visit https://creativecommons.org/licenses/by/4.0/ | |
dc.date.updated | 2025-02-27T21:44:18Z | |
pubs.issue | Pt 1 | |
pubs.publication-status | Published | |
pubs.volume | 281 | |
utslib.citation.issue | Pt 1 |
Abstract:
Novel hydrogel biocatalysts with immobilized lipase, stabilized by ionic liquids (ILs) of different hydrophobicity, were synthesized and evaluated. Variations of the time of immobilization and ratio of substrates during hydrogel synthesis were considered to obtain the most stable biocatalyst with the highest activity. Physicochemical characterization proved the success of the hydrogel synthesis and enzyme deposition on the surface of the support. Nevertheless, the key objective was to produce a biocatalyst for further application in ibuprofen methyl ester resolution, with the aim of obtaining an enantiomerically pure product. The hydrogel biocatalysts obtained in the presence of 5 wt% ILs after 8 h of immobilization achieved the highest activity recovery of 62 %. After 10 reaction cycles, enzymatic activity was still above 60 %, and the negative effect of pH and temperature on the activity of immobilized lipase was much lower than in the case of the free enzyme. After application of the catalyst in the resolution of ibuprofen methyl ester, the enantiomeric excess and conversion rate of the process were obtained for the dynamic kinetic resolution in isooctane. A conversion rate of 95 % was achieved due to the stabilization of the biocatalyst with IL and its resulting high catalytic activity. The study thus provides the pharmaceutical industry with a new potential approach with a strong scientific foundation.
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