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Enantioselective transacetylation of (R,S)-β-citronellol by propanol rinsed immobilized Rhizomucor miehei lipase

Enantioselective transacetylation of (R,S)-β-citronellol by propanol rinsed immobilized... Background: Use of enzymes in low water media is now widely used for synthesis and kinetic resolution of organic compounds. The frequently used enzyme form is the freeze-dried powders. It has been shown earlier that removal of water molecules from enzyme by rinsing with n-propanol gives preparation (PREP) which show higher activity in low water media. The present work evaluates PREP of the lipase (from Rhizomucor miehei) for kinetic resolution of (R,S)-β-citronellol. The acylating agent was vinyl acetate and the reaction was carried out in solvent free media. Results: The PREP, with 0.75% (v/v, reaction media) water, was indeed found to be more efficient and gave 95% conversion to the ester. Using this PREP, with no added water, 90% ee for (R)-(+)- β-citronellyl acetate at 45% conversion (E = 42) was obtained in 4 h. The control with freeze-dried enzyme, with zero water content, gave 78% ee at 30% conversion (E = 13). FT-IR analysis showed that PREP had retained the α-helical content of the enzyme. On the other hand, freeze-dried enzyme showed considerable loss in the α-helical content. Conclusion: The results show that PREP may be a superior biocatalyst for enantioselective conversion by enzymes in low-water media. lective http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Chemistry Central Journal Springer Journals

Enantioselective transacetylation of (R,S)-β-citronellol by propanol rinsed immobilized Rhizomucor miehei lipase

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References (20)

Publisher
Springer Journals
Copyright
Copyright © 2007 by Majumder et al
Subject
Chemistry; Chemistry/Food Science, general
eISSN
1752-153X
DOI
10.1186/1752-153X-1-10
pmid
17880741
Publisher site
See Article on Publisher Site

Abstract

Background: Use of enzymes in low water media is now widely used for synthesis and kinetic resolution of organic compounds. The frequently used enzyme form is the freeze-dried powders. It has been shown earlier that removal of water molecules from enzyme by rinsing with n-propanol gives preparation (PREP) which show higher activity in low water media. The present work evaluates PREP of the lipase (from Rhizomucor miehei) for kinetic resolution of (R,S)-β-citronellol. The acylating agent was vinyl acetate and the reaction was carried out in solvent free media. Results: The PREP, with 0.75% (v/v, reaction media) water, was indeed found to be more efficient and gave 95% conversion to the ester. Using this PREP, with no added water, 90% ee for (R)-(+)- β-citronellyl acetate at 45% conversion (E = 42) was obtained in 4 h. The control with freeze-dried enzyme, with zero water content, gave 78% ee at 30% conversion (E = 13). FT-IR analysis showed that PREP had retained the α-helical content of the enzyme. On the other hand, freeze-dried enzyme showed considerable loss in the α-helical content. Conclusion: The results show that PREP may be a superior biocatalyst for enantioselective conversion by enzymes in low-water media. lective

Journal

Chemistry Central Journal – Springer Journals

Published: Apr 18, 2007

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