Mini-Review: Recent Developments in Hydroxynitrile Lyases for Industrial Biotechnology
Elisa Lanfranchi, Kerstin Steiner, Anton Glieder, Ivan Hajnal, Roger A. Sheldon, Sander van Pelt and Margit Winkler
Affiliation: ACIB GmbH (Austrian Centre of Industrial Biotechnology GmbH), Petersgasse 14/III, A-8010 Graz, Austria.
Keywords: Asymmetric synthesis, biocatalysis, biotransformation, cascade reactions, C-C coupling, chiral building blocks,
cyanogenesis, cyanohydrin, enantioselectivity, enzyme engineering, HNL, hydrocyanic acid, hydroxynitrile lyase, industrial
process, mandelonitrile lyase, plant enzymes, oxynitrilase, stereoselective.
Hydroxynitrile lyases (HNLs) catalyze the cleavage as well as the formation of cyanohydrins. The latter reaction
is valuable for the stereoselective C-C bond formation by condensation of HCN with carbonyl compounds. The resulting
cyanohydrins serve as versatile building blocks for a broad range of chemical and enzymatic follow-up reactions.
A significant number of (R)- and (S)-selective HNLs are known today and the number is still increasing. HNLs not only
exhibit varying substrate scope but also differ in sequence and structure. Tailor-made enzymes for large-scale manufacturing
of cyanohydrins with improved yield and enantiomeric excess are very interesting targets, which is reflected in a solid
number of patents. This review will complement and extend our recent review with a strong focus on applications of
HNLs for the synthesis of highly functionalized, chiral compounds with newest literature, recent and current patent literature.
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