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Lipase-catalyzed production of a bioactive terpene ester in supercritical carbon dioxide

Paper ID Volume ID Publish Year Pages File Format Full-Text
24392 43511 2010 6 PDF Available
Title
Lipase-catalyzed production of a bioactive terpene ester in supercritical carbon dioxide
Abstract

Direct esterification of α-terpineol and acetic anhydride catalyzed by Candida rugosa lipase was performed in supercritical carbon dioxide (SC-CO2) with organic solvent serving as co-solvents. The highest yield of terpinyl acetate after 1.5 h of reaction performance (95.1%) was obtained in SC-CO2 with n-heptane serving as a co-solvent and immobilized Candida rugosa lipase as an enzyme at 50 °C. The optimal pressure for terpinyl acetate synthesis in SC-CO2 medium was 10 MPa. Acetic anhydride was the best substrate among all acyl donors. Anhydrous enzyme was found to be the best for the esterification reaction. Lipase immobilization increased the catalytic efficiency up to 1.8-fold. The analysis of the initial rate data showed that reaction followed a Ping-Pong Bi–Bi mechanism with inhibition by acetic anhydride. The kinetic constants were obtained by multiple regression analysis of experimental findings. The reaction went smoothly without the use of hazardous reactants, and the developed method is useful for industrial application.

Keywords
Terpene ester; Terpinyl acetate; Supercritical carbon dioxide; Esterification; Lipase
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Lipase-catalyzed production of a bioactive terpene ester in supercritical carbon dioxide
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 146, Issue 4, 15 April 2010, Pages 215–220
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us