ArticleWorld journal of microbiology & biotechnology2014
A novel nitrilase from Rhodobacter sphaeroides LHS-305: cloning, heterologous expression and biochemical characterization.
Article in World journal of microbiology & biotechnology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 20 citations in OpenAlex.
- Nitrilase GiNIT fromInternational journal of molecular sciences · 2024Article
- Purification and Characterization of NitFrontiers in bioengineering and biotechnology · 2021Article
- Cloning, overexpression, and characterization of a thermostable nitrilase from an Antarctic Pyrococcus sp.Extremophiles : life under extreme conditions · 2017Article
- Bioengineering of Nitrilases Towards Its Use as Green Catalyst: Applications and Perspectives.Indian journal of microbiology · 2017Review
- Red Sea Atlantis II brine pool nitrilase with unique thermostability profile and heavy metal tolerance.BMC biotechnology · 2016Article
- Cloning and functional characterization of nitrilase from Fusarium proliferatum AUF-2 for detoxification of nitriles.Functional & integrative genomics · 2015Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
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Abstract
In this study, a novel nitrilase gene from Rhodobacter sphaeroides was cloned and overexpressed in Escherichia coli. The open reading frame of the nitrilase gene includes 969 base pairs, which encodes a putative polypeptide of 322 amino acid residues. The molecular weight of the purified native nitrilase was about 560 kDa determined by size exclusion chromatography. This nitrilase showed one single band on SDS-PAGE with a molecular weight of 40 kDa. This suggested that the native nitrilase consisted of 14 subunits with identical size. The optimal pH and temperature of the purified enzyme were 7.0 and 40 °C, respectively. The kinetic parameters V max and K m toward 3-cyanopyridine were 77.5 μmol min(-1) mg(-1) and 73.1 mmol/l, respectively. The enzyme can easily convert aliphatic nitrile and aromatic nitriles to their corresponding acids. Furthermore, this enzyme demonstrated regioselectivity in hydrolysis of aliphatic dinitriles. This specific characteristic makes this nitrilase have a great potential for commercial production of various cyanocarboxylic acids by hydrolyzing readily available dinitriles.
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