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Immobilized Hydroxynitrile Lyases for Enantioselective Synthesis of Cyanohydrins: Sol‐Gels and Cross‐Linked Enzyme Aggregates
Author(s) -
Cabirol Fabien L.,
Hanefeld Ulf,
Sheldon Roger A.
Publication year - 2006
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.200606139
Subject(s) - chemistry , enantioselective synthesis , diisopropyl ether , ether , hydrolysis , organic chemistry , catalysis
The hydroxynitrile lyases (HNLs) from Prunus amygdalus ( Pa HNL), Manihot esculenta ( Me HNL), and Hevea brasiliensis ( Hb HNL) were successfully immobilized in sol‐gels. The cross‐linked enzyme aggregate (CLEA) of Hb HNL was also prepared. These immobilized enzymes and the commercial Pa HNL‐ and Me HNL‐CLEAs were employed for the enantioselective synthesis of cyanohydrins. The sol‐gels were highly efficient at low catalyst loading and particularly stable towards the organic solvent (diisopropyl ether) and substrate/product deactivation. The stabilization effect was inconsistent for CLEAs of different HNLs and significant deactivation of Pa HNL‐ and Hb HNL‐CLEAs in diisopropyl ether was observed. In contrast commercial Me HNL‐CLEA proved to be a remarkably robust and efficient biocatalyst in diisopropyl ether.