Počet záznamů: 1
Purification and characterization of nitrilase from Fusarium solani IMI196840
- 1.0348214 - MBÚ 2011 RIV GB eng J - Článek v odborném periodiku
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
Grant CEP: GA AV ČR IAA500200708; GA MŠMT(CZ) LC06010; GA MŠMT OC09046; GA ČR GD305/09/H008; GA MPO FT-TA5/043
Výzkumný záměr: CEZ:AV0Z50200510
Klíčová slova: fusarium solani * nitrilase * purification
Kód oboru RIV: EE - Mikrobiologie, virologie
Impakt faktor: 2.648, rok: 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
Trvalý link: http://hdl.handle.net/11104/0188801
Počet záznamů: 1