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Advances in cloning, structural and bioremediation aspects of nitrile hydratases

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Abstract

Nitrile hydratase (NHase) is a prominent enzyme in many microorganisms for its nitrile metabolism. The potentiality in the bioconversion of nitriles to its high-value amides has been extensively used in industries for the production of acrylamide and nicotinamide which are essential chemicals. Enzymologists are still considering NHases for its potential biotechnological applications including biotransformations and bioremediations. But most of the nitrile hydratases have limitations like the low expression, low thermostability and enantioselectivity. Though considerable data has been generated in the area of gene configuration, crystal structure, kinetic mechanism and photoreactivity of NHases, there is a need for constant improvement to develop a robust biocatalyst for bioremediation of toxic nitriles. With these considerations, in the present review, we report advances with the main focus to structure, catalytic mechanism, cloning strategy, gene expression, bioinformatic tools, metagenomics, thermostability and current bioremediation applications of NHases.

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Acknowledgements

We thank profusely Mr Vinay Kumar Rao, Temasek life sciences laboratory, Singapore for manuscript preparation. Our thanks are to Drs Govindappa M, Rajeswari N and Mahesh S, Department of Biotechnology, DSCE, Bengaluru for technical assistance and financial assistance from Karnataka Innovation and Technology Society (K-Tech), Govt. of Karnataka, India.

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  1. Department of Biotechnology, Dayananda Sagar College of Engineering Affiliated to Visveswaraya Technological University, Bengaluru, India

    K. Supreetha, H. S. Anil & S. Kiran

  2. Pesticide Residue and Food Quality Analysis Laboratory, University of Agricultural Sciences, Raichur, Karnataka, India

    Saroja Narsing Rao & D. Srividya

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Supreetha, K., Rao, S.N., Srividya, D. et al. Advances in cloning, structural and bioremediation aspects of nitrile hydratases. Mol Biol Rep 46, 4661–4673 (2019). https://doi.org/10.1007/s11033-019-04811-w

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