A Comparative Study of Nitrilases Identified by Genome Mining

• DOI: 10.1007/s12033-013-9656-6
• Publication Date: 2013-03-07T23:58:41Z
• Authors: Ondřej Kaplan; Alicja B. Veselá; Alena Petříčková; Fabrizia Pasquarelli; Martina Pičmanová; Anna Rinágelová; Tek Chand Bhalla; Miroslav Pátek; Ludmila Martínková
• Keywords: 0303 health sciences; Sequence Homology, Amino Acid; Fungi; Genomics; Sequence Analysis, DNA; Recombinant Proteins; Substrate Specificity; 3. Good health; Fungal Proteins; 03 medical and health sciences; Aminohydrolases; Escherichia coli; Genome, Fungal; Sequence Alignment; Hydro-Lyases

Escherichia coli strains expressing different nitrilases transformed nitriles or KCN. Six nitrilases (from Aspergillus niger (2), A. oryzae, Neurospora crassa, Arthroderma benhamiae, and Nectria haematococca) were arylacetonitrilases, two enzymes (from A. niger and Penicillium chrysogenum) were cyanide hydratases and the others (from P. chrysogenum, P. marneffei, Gibberella moniliformis, Meyerozyma guilliermondi, Rhodococcus rhodochrous, and R. ruber) preferred (hetero)aromatic nitriles as substrates. Promising nitrilases for the transformation of industrially important substrates were found: the nitrilase from R. ruber for 3-cyanopyridine, 4-cyanopyridine and bromoxynil, the nitrilases from N. crassa and A. niger for (R,S)-mandelonitrile, and the cyanide hydratase from A. niger for KCN and 2-cyanopyridine.