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Cloning, expression, and characterization of a novel nitrilase, PaCNit, from Pannonibacter carbonis Q4.6

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Abstract

Objective

Identification of a heavy metal ion-stimulated nitrilase with broad-spectrum substrate specificity.

Results

A novel nitrilase, PaCNit, was identified from Pannonibacter carbonis Q4.6 and its enzymatic properties were investigated. The maximum activity of PaCNit was observed at 65 °C and pH 7.0. PaCNit showed broad substrate specificity towards aliphatic, aromatic, and heterocyclic nitriles, and was tolerant to different organic solvents. Remarkably, PaCNit activity was highly stimulated by metal ions, particularly by Ag+ and Hg2+.

Conclusion

PaCNit nitrilase has a broad range of substrate specificity and can be activated by heavy metal ions. This specific characteristic makes it have a great potential for industrial application.

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Acknowledgements

The authors are grateful for the financial support of National Natural Science Foundation of China (Nos. 21473256, 31400005), the Key Research Project of Shandong Province (No. 2017GGX40114) and the Fundamental Research Funds for the Central Universities of China (Nos. 17CX05013, 18CX05015A).

Supporting information

Supplementary Fig. 1—Sequence alignment of PaCNit with other nitrilases.

Supplementary Fig. 2—SDS-PAGE analysis of the purified nitrilase.

Supplementary Table 1—Effects of surfactants and organic solvents on the activity of the recombinant nitrilase.

Supplementary Table 2—Substrate specificity of the recombinant nitrilase.

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Correspondence to Lijun Xi or Jianguo Liu.

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Liu, D., Xi, L., Han, D. et al. Cloning, expression, and characterization of a novel nitrilase, PaCNit, from Pannonibacter carbonis Q4.6. Biotechnol Lett 41, 583–589 (2019). https://doi.org/10.1007/s10529-019-02661-x

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  • DOI: https://doi.org/10.1007/s10529-019-02661-x

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