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Linum usitatissimum Hydroxynitrile Lyase Cross‐Linked Enzyme Aggregates: A Recyclable Enantioselective Catalyst
Author(s) -
Cabirol Fabien L.,
Tan Pei Loo,
Tay Benson,
Cheng Shiryn,
Hanefeld Ulf,
Sheldon Roger A.
Publication year - 2008
Publication title -
advanced synthesis and catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.541
H-Index - 155
eISSN - 1615-4169
pISSN - 1615-4150
DOI - 10.1002/adsc.200800309
Subject(s) - cyanohydrin , chemistry , linum , biocatalysis , yield (engineering) , hydrolysis , organic chemistry , catalysis , enantioselective synthesis , reaction mechanism , botany , materials science , metallurgy , biology
An immobilized form of the hydroxynitrile lyase from Linum usitatissimum ( Lu HNL) as cross‐linked enzyme aggregate (CLEA) with high specific activity (303.5 U/g) and recovery (33%) was developed. Molecular imprinting using 2‐butanone as additive in the immobilization process improved the synthetic activity of the biocatalyst. Lu CLEA could be partially recycled for the synthesis of ( R )‐2‐butanone cyanohydrin on a preparative scale over two batches. The enantioenriched cyanohydrin obtained was further hydrolyzed to give ( R )‐2‐hydroxy‐2‐methylbutyric acid in 85% yield (from 2‐butanone) and 87% ee .
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