Advanced Synthesis and Catalysis p. 1645 - 1654 (2006)
Update date:2022-08-11
Topics:
Cabirol, Fabien L.
Hanefeld, Ulf
Sheldon, Roger A.
The hydroxynitrile lyases (HNLs) from Prunus amygdalus (paHNL), Manihot esculenta (MeHNL), and Hevea brasiliensis (HbHNL) were successfully immobilized in sol-gels. The cross-linked enzyme aggregate (CLEA) of HbHNL was also prepared. These immobilized enzymes and the commercial PaHNL- and MeHNL-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 PaHNL- and HbHNL-CLEAs in diisopropyl ether was observed. In contrast commercial MeHNL-CLEA proved to be a remarkably robust and efficient biocatalyst in diisopropyl ether.
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