Biotransformation of nitriles to amidases using soluble and immobilized nitrile hydratase from Rhodococcus erythropolis A4

Publication Type
Journal contribution (peer reviewed)
Authors
Kubac, D., Kaplan, O., Elisakova, V., Patek, M., Vejoda, V., Slamova, K., Tothova, A., Lemaire, M., Gallienne, E., Lutz-Wahl, S., Fischer, L., Kuzma, M., Pelantova, H., van Pelt, S., Bolte, J., Kren, V., Martinkova, L.
Year of publication
2008
Published in
Journal of Molecular Catalysis
Pubisher
Elsevier
Series/labeling
B: Enzymatic
DOI
10.1016/j.molcatb.2007.09.007
Page (from - to)
107 - 113
Abstract

A semi-purified nitrile hydratase from Rhodococcus erythropolis A4 was applied to biotransformations of 3-oxonitriles, 3-hydroxy-2-hethylenenitriles, 4-hydroxy-2-methylenenitriles, 3-hydroxynitriles and 3-acyloxynitrile into amides. Crosslinked enzyme aggregates (CLEAs) with nitrile hydratase and amidase activities (88% and 77% of the initial activities, respectively) were prepared from cell-free extract of this microorganism and used for nitrile hydration in presence of ammonium sulfate, which selectively inhibited amidase activity. The genes nha1 and nha2 coding for alpha and beta subunits of nitrile hydratase were cloned and sequenced.

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