Purification of a hyperactive nitrile hydratase from resting cells of Rhodococcus rhodochrous PA-34 View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2009-06-06

AUTHORS

S. Prasad, J. Raj, T. C. Bhalla

ABSTRACT

A propionitrile-induced nitrile hydratase (NHase), a promising biocatalyst for synthesis of organic amides has been purified from cell-free extract of Rhodococcus rhodochrous PA-34. About 11-fold purification of NHase was achieved with 52% yield. The SDS-PAGE of the purified enzyme revealed that it consisted of two subunits of 25.04 kD and 30.6 kD. However, the molecular weight of holoenzyme was speculated to be 86 kD by native-PAGE. This NHase exhibited maximum activity at pH 8.0 and temperature 40°C. Half-life was 2 h at 40°C and 0.5 h at 50°C. The Km and Vmax were 167 mM and 250 μmole/min/mg using 25 mM 3-cyanopyridine as substrate. AgNO3, Pb(CH3COO)2 and HgCl2 inhibited the NHase to extent of 89–100%. More... »

PAGES

237-242

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s12088-009-0033-x

DOI

http://dx.doi.org/10.1007/s12088-009-0033-x

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1041679039

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/23100776


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