Abstract
Nitrile hydratase (NHase, EC 4.2.1.84) is one type of metalloenzyme participating in the biotransformation of nitriles into amides. Given its catalytic specificity in amide production and eco-friendliness, NHase has overwhelmed its chemical counterpart during the past few decades. However, unclear catalytic mechanism, low thermostablity, and narrow substrate specificity limit the further application of NHase. During the past few years, numerous studies on the theoretical and industrial aspects of NHase have advanced the development of this green catalyst. This review critically focuses on NHase research from recent years, including the natural distribution, gene types, posttranslational modifications, expression, proposed catalytic mechanism, biochemical properties, and potential applications of NHase. The developments of NHase described here are not only useful for further application of NHase, but also beneficial for the development of the fields of biocatalysis and biotransformation.
Highlights
Nitriles (RCN) are generally toxic, carcinogenic, mutagenic, and widespread organic compounds, that are primarily found in nature as cyanogenic glycosides, cyanolipids, β-cyanoalanine, and mandelonitrile (Legras et al, 1990)
Nitrile hydratase (NHase) from Rhodococcus pyridinivorans NIT-36 was found to be able to produce lactamide, an industrially important lactic amide which is widely used in the cosmetic industry, with high catalytic activity (Singh et al, 2019). 2,6-Difluorobenzamide, an important intermediate in pesticide industries, could be synthesized by NHase from A. manganoxydans ATCC BAA-1229 with a final concentration equals to 314 g/L through a simple batch process (Yang et al, 2019b)
Researchers from all over the world have dedicated themselves to the development of NHase with the aim of advancing NHase research into a new era
Summary
Nitriles (RCN) are generally toxic, carcinogenic, mutagenic, and widespread organic compounds, that are primarily found in nature as cyanogenic glycosides, cyanolipids, β-cyanoalanine, and mandelonitrile (Legras et al, 1990). The iron or cobalt ion at the active site helps to improve the hydration process of substrate; on the other hand, the metal ions could aid in the NHase folding (Banerjee et al, 2002). Rhodococcus erythropolis is the main organism producing Fe-type NHase, and NHases coordinated with iron ion at the active site are discovered in organisms such as P. chlororaphis, P. putida or Bacillus sp.
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