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Protein & Peptide Letters


ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Purification, Characterization and In-silico Analysis of Nitrilase from Gordonia terrae

Author(s): Vijay Kumar, Amit Seth, Vijaya Kumari, Virender Kumar and Tek C. Bhalla

Volume 22, Issue 1, 2015

Page: [52 - 62] Pages: 11

DOI: 10.2174/0929866521666140909154537

Price: $65


An inducible and aromatic nitrilase from Gordonia terrae was purified with a yield of 19%. The enzyme had turnover number of 63 s-1x 10-3, Km 1.4 mM and Vmax 95 Umg-1 protein for benzonitrile. The nitrilase of G. terrae was active at basic pH (7-10), moderate temperature (20-45 °C) and has a half-life of 4 h at 35 °C. MALDI analysis and amino acid sequence deduced from cloned nucleotide fragment showed 97% homology with putative amidohydrolase of Gordonia sputi NBRC 100414 and G. namibiensis. The enzyme showed regioselectivity towards hydroxybenzonitriles, as different position of hydroxyl group i.e. meta-, para- and orthosubstitutions on benzonitrile effect enzyme activity. The in-silico interactions of these substrates with the predicted 3D model of this enzyme also showed differential interaction between hydroxyl group of substrates and the polar amino acids surrounding enzyme’s active site. This leads to different proximity and orientation of substrates vis-a-vis their interaction with catalytic residues.

Keywords: Gordonia terrae, in-silico analysis, nitrilase, purification.

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