Enabling industrial biocatalytic processes by application of silicone-coated enzyme preparations
Research output: Contribution to journal › Research article › Contributed › peer-review
Contributors
Abstract
Composite particles of the commercial lipase preparation NZ435 and silicone (silcoat-NZ435) have recently been described as promising biocatalysts for synthetic use. In this study, their actual potential for enhanced performance in industrial applications was evaluated, focusing on scenarios where carrier disintegration and catalyst leaching constitute key limitations. All three investigated model reactions, the syntheses of myristyl myristate, poly(ethylene glycol) 400-coconut fatty acid monoester and ethylene oxide and propylene oxide co-polymer (EO/PO)-oleic acid diester, were considerably improved in terms of the maximal number of reaction cycles performed with the same batch of catalyst, and consequently in terms of the obtainable product amount. The total turnover numbers (TTN) increased by a factor up to 50, making the realization of this type of reactions in an industrial process more feasible. The utility of silcoat-NZ435 for stereoselective transformations was demonstrated with the enantioselective acylation of 1-phenylethanol with vinyl butyrate, in which full retention of the excellent stereoselectivity of native NZ435 was observed. Moreover, it was demonstrated for the first time that
the methodology by which silcoat-catalysts are obtained can be successfully transferred to alternative carriers and enzymes (e.g., protease, esterase and laccase), opening a broad field for the implementation and advancement of biocatalysis in industrial processes.
the methodology by which silcoat-catalysts are obtained can be successfully transferred to alternative carriers and enzymes (e.g., protease, esterase and laccase), opening a broad field for the implementation and advancement of biocatalysis in industrial processes.
Details
Original language | English |
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Pages (from-to) | 2522-2528 |
Journal | Advanced synthesis & catalysis |
Volume | 2011 |
Issue number | 353 |
Publication status | Published - 2011 |
Peer-reviewed | Yes |
Externally published | Yes |
External IDs
Scopus | 80052802797 |
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ORCID | /0000-0002-2912-546X/work/171551977 |
Keywords
Keywords
- Biokatalyse, Emollientester, Lipase, silCoat, Immobilisierung