Purification and characterization of a nitrilase from Aspergillus niger K10 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2006-10-24

AUTHORS

Ondřej Kaplan, Vojtěch Vejvoda, Ondřej Plíhal, Petr Pompach, Daniel Kavan, Pavla Bojarová, Karel Bezouška, Martina Macková, Maria Cantarella, Vladimír Jirků, Vladimír Křen, Ludmila Martínková

ABSTRACT

Aspergillus 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... »

PAGES

567-575

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00253-006-0503-6

DOI

http://dx.doi.org/10.1007/s00253-006-0503-6

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1044847715

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/17061133


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