Purification and characterization of nitrilase from Fusarium solani IMI196840

0348214 - MBÚ 2011 RIV GB eng J - Journal Article
Vejvoda, Vojtěch - Kubáč, David - Davidová, A. - Kaplan, Ondřej - Šulc, Miroslav - Šveda, Ondřej - Chaloupková, R. - Martínková, Ludmila
Purification and characterization of nitrilase from Fusarium solani IMI196840.
Process Biochemistry. Roč. 45, č. 7 (2010), s. 1115-1120. ISSN 1359-5113. E-ISSN 1873-3298
R&D Projects: GA AV ČR IAA500200708; GA MŠMT(CZ) LC06010; GA MŠMT OC09046; GA ČR GD305/09/H008; GA MPO FT-TA5/043
Institutional research plan: CEZ:AV0Z50200510
Keywords : fusarium solani * nitrilase * purification
Subject RIV: EE - Microbiology, Virology
Impact factor: 2.648, year: 2010

Nitrilase activity in Fusarium solani IMI196840 (approx. 1500Ul of culture broth) was induced by 2-cyanopyridine. The enzyme was purified by a factor of 20.3 at a yield of 26.9 percent. According to gel filtration, the holoenzyme was an approx. 550-kDa homooligomer consisting of subunits with a molecular weight of approximately 40 kDa, as determined by SDS-PAGE. Mass spectrometry analysis of the tryptic fragments suggested a high similarity of this enzyme to the hypothetical CN hydrolases from Aspergillus oryzae, Gibberella zeae, Gibberella moniliformis and Nectria haematococca. Circular dichroism and fluorescence spectra indicated that secondary structure content and overall tertiary structure, respectively, were almost identical in nitrilases from F. solani IMI196840 and F. solani O1
Permanent Link: http://hdl.handle.net/11104/0188801