Abstract
The effects of relative humidity and temperature on lipase-catalyzed transesterification reaction was studied to optimize the dual role of water in the reactions. Commercial crude porcine lipase containing 25 percent protein was immobilized on glass wool to form a biocatalyst for the reactions carried out in several reactor configurations. Ethyl acetate and isoamyl alcohol which were used as feed for the continuous loop recycle system were converted into isomyl acetate and ethanol in a reversible reactions by the biocatalyst. Most of the enzyme activity was lost on increasing the relative humidity and temperature.
Original language | English |
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Pages (from-to) | 2 |
Number of pages | 1 |
Journal | Industrial Bioprocessing |
Volume | 24 |
Issue number | 4 |
State | Published - Apr 2002 |