Hydrolysis of Nitriles Using an Immobilized Nitrilase: Applications to the Synthesis of Methionine Hydroxy Analogue Derivatives

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Abstract
Mild and selective hydrolysis of a large range of nitriles leading to carboxylic acids was achieved under neutral conditions by an immobilized and genetically modified enzyme preparation from Alcaligenes faecalis ATCC8750. This immobilized nitrilase has been shown to be an effective catalyst for the stereoselective hydrolysis of mandelonitrile 1a to R-(−)-mandelic acid 1c. This method is particularly useful for the production of hydroxy analogues of methionine derivatives 2c−4c that could have an interest in cattle feeding and for the transformation of compounds containing other acid- or base-sensitive groups 3a−10a. A series of aliphatic dinitriles 11a−15a was hydrolyzed to the corresponding cyano acids. The suitability of the immobilized catalyst as a robust and versatile biocatalyst is discussed, and models to account for the stereoselectivity of the enzymic hydrolysis have been proposed. Keywords: Biotransformation; enzymes; hydrolases; methionine hydroxy analogue derivatives; dinitriles