ArticlePloS one2017
Overexpression and characterization of two types of nitrile hydratases from Rhodococcus rhodochrous J1.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 23 citations in OpenAlex.
- Biodegradation of Neonicotinoid Insecticides Thiacloprid and Thiamethoxam by Microorganisms: Metabolic Process, Metabolic Enzymes and Toxicity Assessments of their Metabolites.Current microbiology · 2025Review
- Nitrile hydratase as a promising biocatalyst: recent advances and future prospects.Biotechnology letters · 2024Review
- Merging enzymes with chemocatalysis for amide bond synthesis.Nature communications · 2022Article
- Response surface methodology: An effective optimization strategy for enhanced production of nitrile hydratase (NHase) byHeliyon · 2020Article
- Recent Advances and Promises in Nitrile Hydratase: From Mechanism to Industrial Applications.Frontiers in bioengineering and biotechnology · 2020Review
- Efficient Overproduction of Active Nitrile Hydratase by Coupling Expression Induction and Enzyme MaturationFrontiers in bioengineering and biotechnology · 2020Article
- Advances in cloning, structural and bioremediation aspects of nitrile hydratases.Molecular biology reports · 2019Review
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nitrile hydratase (NHase) from Rhodococcus rhodochrous J1 is widely used for industrial production of acrylamide and nicotinamide. However, the two types of NHases (L-NHase and H-NHase) from R. rhodochrous J1 were only slightly expressed in E. coli by routine methods, which limits the comprehensive and systematic characterization of the enzyme properties. We successfully expressed the two types of recombinant NHases in E. coli by codon-optimization, engineering of Ribosome Binding Site (RBS) and spacer sequences. The specific activity of the purified L-NHase and H-NHase were 400 U/mg and 234 U/mg, respectively. The molecular mass of L-NHase and H-NHase was identified to be 94 kDa and 504 kDa, respectively, indicating that the quaternary structure of the two types of NHases was the same as those in R. rhodochrous J1. H-NHase exhibited higher substrate and product tolerance than L-NHase. Moreover, higher activity and shorter culture time were achieved in recombinant E. coli, and the whole cell catalyst of recombinant E. coli harboring H-NHase has equivalent efficiency in tolerance to the high-concentration product relative to that in R. rhodochrous J1. These results indicate that biotransformation of nitrile by R. rhodochrous J1 represents a potential alternative to NHase-producing E. coli.
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