Nitrile- and Amide-hydrolysing Activity in Kluyveromyces thermotolerans MGBY 37 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2005-12

AUTHORS

Shreenath Prasad, Deep Raj Sharma, Tek Chand Bhalla

ABSTRACT

Forty yeast strains were screened for nitrile-hydrolysing activity. Among them Kluyveromyces thermotolerans MGBY 37 exhibited highest nitrile-hydrolysing activity (0.030 μmol/h/mg dry cell weight). This yeast contained a two-enzyme system i.e. nitrile hydratase (NHase, EC 4.2.1.84) and amidase (EC 3.5.1.4) for the hydrolysis of nitriles/amides to corresponding acids and ammonia. However, these enzymes had more affinity for N-heterocyclic aromatic and aromatic nitriles/amides rather than unsaturated and saturated aliphatic nitriles/amides. The NHase–amidase activity was constitutively produced by K. thermotolerence MGBY 37. Addition of acetonitrile in the medium enhanced the production of this activity while other nitriles and amides lowered the production of NHase–amidase activity. This organism thus exhibited two types of amidase i.e. a constitutive amidase having affinity for N-heterocyclic aromatic, unsaturated and saturated aliphatic amides and another inducible amidase with affinity for aromatic amides. Formamide proved to be the best inducer of the latter amidase activity. This is the first report on nitrile- and amide-hydrolysing activity in Kluyveromyces. More... »

PAGES

1447-1450

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s11274-005-6563-4

DOI

http://dx.doi.org/10.1007/s11274-005-6563-4

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1049507827


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