Publication at Faculty of Science |
2010
Abstract
Nitrilase activity in Fusarium solani IMI196840 was induced by 2-cyanopyridine.and the enzyme was purified (holoenzyme homooligomer MW was an approx. 550-kDa, subunit MW was an approx. 40 kDa). Mass spectrometry analysis suggested a high similarity of this enzyme to the hypothetical CN hydrolases from A. oryzae, G.a zeae, G. moniliformis and N. haematococca.
The best substrates were benzonitrile and 4-cyanopyridine, which were hydrolyzed under the optimum conditions of pH 8 and 45 ◦C. The enzyme was highly chemoselective, producing ≤2% amides as by-products.