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Immobilized lipase YlLip2-catalyzed resolution of (±)α-phenylethyl amine in a medium with organic cosolvent

Paper ID Volume ID Publish Year Pages File Format Full-Text
35317 45086 2008 6 PDF Available
Title
Immobilized lipase YlLip2-catalyzed resolution of (±)α-phenylethyl amine in a medium with organic cosolvent
Abstract

In this paper, we studied the enantioselective aminolysis activity of an immobilized extracellular lipase LIP2 (YlLip2) from Yarrowia lipolytica by catalyzing enantioselective acylation of (±)α-phenylethyl amine with acetic ester in a medium containing cosolvent. The reaction parameters including cosolvent concentration, reaction temperature, amount of the immobilized lipase and the reaction time were optimized. When the reaction was carried out in hexane with the presence of 3% DMSO and six pieces of immobilized lipase at 45 °C for 6 days, the enantiomeric excess of product (e.e.p) markedly increased from 0.35 (in neat hexane) to 0.96 and the enantiomeric ratio (E) improved from 2.5 (in neat hexane) to 190. The immobilized lipase could be reused at least five consecutive batches at high E (≈190).

Keywords
Yarrowia lipolytica lipase LIP2; Enantioselective aminolysis; (±)α-Phenylethyl amine; Cosolvent; Organic medium; Dimethylsulfoxide
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Immobilized lipase YlLip2-catalyzed resolution of (±)α-phenylethyl amine in a medium with organic cosolvent
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 43, Issue 11, November 2008, Pages 1259–1264
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