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Fabrication of heterogeneous biocatalyst tethering artificial prosthetic groups to obtain omega-3-fatty acids by selective hydrolysis of fish oils

The active site of lipase from Bacillus thermocathenolatus was selectively modified with allyl and naphthyl chains at different positions. Lipase immobilization and selective tethering of a naphthyl side chain to its position 320 improve both the hydrolysis rate of fish oils and the selectivity towa...

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Bibliographic Details
Published in:RSC advances 2016-01, Vol.6 (100), p.97659-97663
Main Authors: Moreno-Pérez, S., Fernández-Lorente, G., Romero, O., Guisán, J. M., López-Gallego, F.
Format: Article
Language:English
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Summary:The active site of lipase from Bacillus thermocathenolatus was selectively modified with allyl and naphthyl chains at different positions. Lipase immobilization and selective tethering of a naphthyl side chain to its position 320 improve both the hydrolysis rate of fish oils and the selectivity towards the eicosapentaenoic acid acyl chains.
ISSN:2046-2069
2046-2069
DOI:10.1039/C6RA21121F