Comparison between Lipase Performance Distributed at the O/W Interface by Membrane Emulsification and by Mechanical Stirring
Multiphase bioreactors using interfacial biocatalysts are unique tools in life sciences such as pharmaceutical and biotechnology. In such systems, the formation of microdroplets promotes the mass transfer of reagents between two different phases, and the reaction occurs at the liquid–liquid interfac...
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MDPI AG
2021-02-01
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Series: | Membranes |
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Online Access: | https://www.mdpi.com/2077-0375/11/2/137 |
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author | Emma Piacentini Rosalinda Mazzei Lidietta Giorno |
author_facet | Emma Piacentini Rosalinda Mazzei Lidietta Giorno |
author_sort | Emma Piacentini |
collection | DOAJ |
description | Multiphase bioreactors using interfacial biocatalysts are unique tools in life sciences such as pharmaceutical and biotechnology. In such systems, the formation of microdroplets promotes the mass transfer of reagents between two different phases, and the reaction occurs at the liquid–liquid interface. Membrane emulsification is a technique with unique properties in terms of precise manufacturing of emulsion droplets in mild operative conditions suitable to preserve the stability of bioactive labile components. In the present work, membrane emulsification technology was used for the production of a microstructured emulsion bioreactor using lipase as a catalyst and as a surfactant at the same time. An emulsion bioreaction system was also prepared by the stirring method. The kinetic resolution of (<i>S</i>,<i>R</i>)-naproxen methyl ester catalyzed by the lipase from <i>Candida rugosa</i> to obtain (<i>S</i>)-naproxen acid was used as a model reaction. The catalytic performance of the enzyme in the emulsion systems formulated with the two methods was evaluated in a stirred tank reactor and compared. Lipase showed maximum enantioselectivity (100%) and conversion in the hydrolysis of (<i>S</i>)-naproxen methyl ester when the membrane emulsification technique was used for biocatalytic microdroplets production. Moreover, the controlled formulation of uniform and stable droplets permitted the evaluation of lipase amount distributed at the interface and therefore the evaluation of enzyme specific activity as well as the estimation of the hydrodynamic radius of the enzyme at the oil/water (o/w) interface in its maximum enantioselectivity. |
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institution | Directory Open Access Journal |
issn | 2077-0375 |
language | English |
last_indexed | 2024-03-09T00:50:23Z |
publishDate | 2021-02-01 |
publisher | MDPI AG |
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series | Membranes |
spelling | doaj.art-3e9d82e9622446e7a8ce4f8b1717cf042023-12-11T17:13:21ZengMDPI AGMembranes2077-03752021-02-0111213710.3390/membranes11020137Comparison between Lipase Performance Distributed at the O/W Interface by Membrane Emulsification and by Mechanical StirringEmma Piacentini0Rosalinda Mazzei1Lidietta Giorno2National Research Council, Institute on Membrane Technology, CNR-ITM, Via P. Bucci 17 C, 87036 Rende, ItalyNational Research Council, Institute on Membrane Technology, CNR-ITM, Via P. Bucci 17 C, 87036 Rende, ItalyNational Research Council, Institute on Membrane Technology, CNR-ITM, Via P. Bucci 17 C, 87036 Rende, ItalyMultiphase bioreactors using interfacial biocatalysts are unique tools in life sciences such as pharmaceutical and biotechnology. In such systems, the formation of microdroplets promotes the mass transfer of reagents between two different phases, and the reaction occurs at the liquid–liquid interface. Membrane emulsification is a technique with unique properties in terms of precise manufacturing of emulsion droplets in mild operative conditions suitable to preserve the stability of bioactive labile components. In the present work, membrane emulsification technology was used for the production of a microstructured emulsion bioreactor using lipase as a catalyst and as a surfactant at the same time. An emulsion bioreaction system was also prepared by the stirring method. The kinetic resolution of (<i>S</i>,<i>R</i>)-naproxen methyl ester catalyzed by the lipase from <i>Candida rugosa</i> to obtain (<i>S</i>)-naproxen acid was used as a model reaction. The catalytic performance of the enzyme in the emulsion systems formulated with the two methods was evaluated in a stirred tank reactor and compared. Lipase showed maximum enantioselectivity (100%) and conversion in the hydrolysis of (<i>S</i>)-naproxen methyl ester when the membrane emulsification technique was used for biocatalytic microdroplets production. Moreover, the controlled formulation of uniform and stable droplets permitted the evaluation of lipase amount distributed at the interface and therefore the evaluation of enzyme specific activity as well as the estimation of the hydrodynamic radius of the enzyme at the oil/water (o/w) interface in its maximum enantioselectivity.https://www.mdpi.com/2077-0375/11/2/137multiphasic bioreactor systemsmembrane emulsificationlipasekinetic resolutionemulsionenantiomer |
spellingShingle | Emma Piacentini Rosalinda Mazzei Lidietta Giorno Comparison between Lipase Performance Distributed at the O/W Interface by Membrane Emulsification and by Mechanical Stirring Membranes multiphasic bioreactor systems membrane emulsification lipase kinetic resolution emulsion enantiomer |
title | Comparison between Lipase Performance Distributed at the O/W Interface by Membrane Emulsification and by Mechanical Stirring |
title_full | Comparison between Lipase Performance Distributed at the O/W Interface by Membrane Emulsification and by Mechanical Stirring |
title_fullStr | Comparison between Lipase Performance Distributed at the O/W Interface by Membrane Emulsification and by Mechanical Stirring |
title_full_unstemmed | Comparison between Lipase Performance Distributed at the O/W Interface by Membrane Emulsification and by Mechanical Stirring |
title_short | Comparison between Lipase Performance Distributed at the O/W Interface by Membrane Emulsification and by Mechanical Stirring |
title_sort | comparison between lipase performance distributed at the o w interface by membrane emulsification and by mechanical stirring |
topic | multiphasic bioreactor systems membrane emulsification lipase kinetic resolution emulsion enantiomer |
url | https://www.mdpi.com/2077-0375/11/2/137 |
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