Stability and activity of enzyme aggregates of Calb in supercritical CO2
The activity and stability of a cross-linked enzyme aggregate of Candida antarctica lipase B (CLEA-Calb) in supercrit. carbon dioxide (SC-CO2) have been studied. The model reaction used is the esterification of isoamyl alc. with acetic acid. The catalytic performance of CLEA-Calb is evaluated both i...
| Published in: | The Journal of Supercritical Fluids |
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| Main Authors: | , , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
2007
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| Subjects: | |
| Online Access: | https://research.tue.nl/en/publications/fe1d1380-e3b7-45f1-8c7e-b7ddb79f39f0 https://doi.org/10.1016/j.supflu.2006.08.013 |
| Summary: | The activity and stability of a cross-linked enzyme aggregate of Candida antarctica lipase B (CLEA-Calb) in supercrit. carbon dioxide (SC-CO2) have been studied. The model reaction used is the esterification of isoamyl alc. with acetic acid. The catalytic performance of CLEA-Calb is evaluated both in batch and in continuous expts., with a focus on the effect of water prodn. upon reaction. The results of the batch expts. show a decreasing initial activity of the CLEA-Calb with an increase in pressure. Moreover, CLEAs appear to be highly stable in supercrit. carbon dioxide and also remain active during continuous reactions. Suggestions for improved process designs are given for which the optimal design depends on the specific reaction requirements. |
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