Immobilization of lipase with alginate hydrogel beads and the lipase‐catalyzed kinetic resolution of α‐phenyl ethanol
ABSTRACT The immobilization of enzymes is one of the key issues in both the field of enzymatic research and industrialization. In this article, we report a facile method for immobilizing Candida antarctica lipase B in an alginate carrier. In the presence of calcium cations, an enzyme–alginate suspen...
| Published in: | Journal of Applied Polymer Science |
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| Main Authors: | , , , , , , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
Wiley
2013
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| Subjects: | |
| Online Access: | http://dx.doi.org/10.1002/app.40178 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fapp.40178 https://onlinelibrary.wiley.com/doi/pdf/10.1002/app.40178 |
| Summary: | ABSTRACT The immobilization of enzymes is one of the key issues in both the field of enzymatic research and industrialization. In this article, we report a facile method for immobilizing Candida antarctica lipase B in an alginate carrier. In the presence of calcium cations, an enzyme–alginate suspension was crosslinked to form beads with a porous structure at room temperature, and the enzymes were well dispersed in the beads. The chiral resolution of α‐phenyl ethanol in the organic phase was tested by the enzyme–alginate beads. The effects of the reaction parameters, such as the enzyme concentration, temperature, and molar ratio of the substrate to the solvent, on the resolution behavior are discussed. Reuse cycle experiments for the chiral resolution of α‐phenyl ethanol demonstrated that the activity of the enzyme–alginate beads was maintained without marked deactivation up to five repeated cycles. © 2013 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2014 , 131 , 40178. |
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