Ontology type: schema:ScholarlyArticle
2006-10-24
AUTHORSOndřej Kaplan, Vojtěch Vejvoda, Ondřej Plíhal, Petr Pompach, Daniel Kavan, Pavla Bojarová, Karel Bezouška, Martina Macková, Maria Cantarella, Vladimír Jirků, Vladimír Křen, Ludmila Martínková
ABSTRACTAspergillus niger K10 cultivated on 2-cyanopyridine produced high levels of an intracellular nitrilase, which was partially purified (18.6-fold) with a 24% yield. The N-terminal amino acid sequence of the enzyme was highly homologous with that of a putative nitrilase from Aspergillus fumigatus Af293. The enzyme was copurified with two proteins, the N-terminal amino acid sequences of which revealed high homology with those of hsp60 and an ubiquitin-conjugating enzyme. The nitrilase exhibited maximum activity (91.6 U mg-1) at 45°C and pH 8.0. Its preferred substrates, in the descending order, were 4-cyanopyridine, benzonitrile, 1,4-dicyanobenzene, thiophen-2-acetonitrile, 3-chlorobenzonitrile, 3-cyanopyridine, and 4-chlorobenzonitrile. Formation of amides as by-products was most intensive, in the descending order, for 2-cyanopyridine, 4-chlorobenzonitrile, 4-cyanopyridine, and 1,4-dicyanobenzene. The enzyme stability was markedly improved in the presence of d-sorbitol or xylitol (20% w/v each). p-Hydroxymercuribenzoate and heavy metal ions were the most powerful inhibitors of the enzyme. More... »
PAGES567-575
http://scigraph.springernature.com/pub.10.1007/s00253-006-0503-6
DOIhttp://dx.doi.org/10.1007/s00253-006-0503-6
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PUBMEDhttps://www.ncbi.nlm.nih.gov/pubmed/17061133
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