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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 .

Overexpression and characterization of two types of nitrile hydratases from Rhodococcus rhodochrous J1