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Lipase immobilization on O-propargyl and O-pentynyl dextrans and its application for the synthesis of click beetle pheromones

Paper ID Volume ID Publish Year Pages File Format Full-Text
35099 45074 2009 8 PDF Available
Title
Lipase immobilization on O-propargyl and O-pentynyl dextrans and its application for the synthesis of click beetle pheromones
Abstract

Lipase of Rhizopus arrhizus was immobilized on O-propargyl dextran (PgD) and O-pentynyl dextran (PyD). Compared with Lewatit VP OC 1600 cation ion exchange resin, wood shaves, fuller earth, silica and alumina, PgD with degree of substitution (DS) of 0.68 and a surface of 10 m2/g was found to be the most effective immobilization support and an excellent biocatalyst for esterification reactions in organic solvents as the synthesis of click beetle pheromone geranyl octanoate. PyD (DS 0.44) with a surface of 3.3 m2/g was of similar high efficiency. For the enzymatic esterification the optimum concentration of geraniol and octanoic acid was 0.4 mol L−1 each. The biocatalyst worked the best in hexane at a moisture level of 0.02%. The enzyme could be repeatedly used and conversion dropped from 80% to 70% after four cycles, while reaction rate even increased when repeatedly employed.

Keywords
O-Alkynyl dextran; Lipase immobilization; Geranyl octanoate; Click beetles; Rhizopus arrhizus lipase; Enzyme activity in organic solvent
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Lipase immobilization on O-propargyl and O-pentynyl dextrans and its application for the synthesis of click beetle pheromones
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 44, Issue 11, November 2009, Pages 1276–1283
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