Enzyme stabilization by deposition of silicone coatings
Research output: Contribution to journal › Research article › Contributed › peer-review
Contributors
Abstract
One of the major limitations that prohibit the more frequent use
of biocatalysis in the production of specialty and bulk chemicals
is the insufficient long-term stability of commercially available
enzyme preparations. Especially stability in terms of enzyme
leaching and carrier integrity under process conditions is still an
issue. Herein, we report on the fabrication of enzyme preparations
of superb mechanical stability and outstanding stability towards
leaching. For the first time, such immobilisates have been obtained
by deposition of silicone coatings, available from cheap silicone
building blocks under simple reaction conditions. Using an immobilized
lipase (Novozyme 435) as a model compound, the
obtained coated particles showed activity yields of more than 92%.
The outstanding robustness has been proven by showing the
stability towards mechanical stress and towards enzyme desorption
by subjection to an assay mimicking harsh leaching conditions.
of biocatalysis in the production of specialty and bulk chemicals
is the insufficient long-term stability of commercially available
enzyme preparations. Especially stability in terms of enzyme
leaching and carrier integrity under process conditions is still an
issue. Herein, we report on the fabrication of enzyme preparations
of superb mechanical stability and outstanding stability towards
leaching. For the first time, such immobilisates have been obtained
by deposition of silicone coatings, available from cheap silicone
building blocks under simple reaction conditions. Using an immobilized
lipase (Novozyme 435) as a model compound, the
obtained coated particles showed activity yields of more than 92%.
The outstanding robustness has been proven by showing the
stability towards mechanical stress and towards enzyme desorption
by subjection to an assay mimicking harsh leaching conditions.
Details
Original language | English |
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Pages (from-to) | 617-620 |
Journal | Organic Process Research and Development |
Volume | 2009 |
Issue number | 13 |
Publication status | Published - 2009 |
Peer-reviewed | Yes |
Externally published | Yes |
External IDs
Scopus | 66249091218 |
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ORCID | /0000-0002-2912-546X/work/171551896 |
Keywords
Research priority areas of TU Dresden
DFG Classification of Subject Areas according to Review Boards
Sustainable Development Goals
Keywords
- Biokatalyse, Immobilisierung, silCoat, CalB, Lipase, Emollientester