Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
36641 | Process Biochemistry | 2005 | 4 Pages |
Abstract
The lipase-catalyzed synthesis of ascorbyloleate was studied using different preparations of lipases from Candida antarctica. Conversion to ascorbyloleate was influenced by the type of lipase, the carrier used for immobilization, water activity and organic solvent. The highest conversion (63%) was found using Chirazyme L-2 immobilized on carrier C2, in acetone, using methyloleate as acyl donor (4-fold excess), at water activity 0.11 and in the presence of molecular sieves.
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Authors
Marek Adamczak, Uwe T. Bornscheuer, Wlodzimierz Bednarski,