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Cloning and Heterologous Expression of Phytase Gene from Pantoea sp. 3.5.1

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Abstract

Phytases (myo-inositol hexakisphosphate phosphohydrolase) catalyzes the stepwise hydrolysis of phosphate groups from phytic acid (myo-inositol hexakisphosphate) or its salt phytate. These enzymes could be potentially used for the stereospecific and efficient production of different myo-inositol phosphate isomers with therapeutic features. In the present study, we cloned the 1728 bp open reading frame encoding Pantoea sp. 3.5.1 phytase into the expression vector pET28a. The recombinant Escherichia coli BL21 pLysS pET28a/agpP strain expressing Pantoea sp. 3.5.1 AgpP phytase was obtained.

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References

  1. Suzuki, U., Yoshimura, K., Takaishi, M. (1907). Über ein enzym ‘Phytase’ das anhydro-oxy-methylen diphosphorsaure’ spalter. Tokyo Imperial University College of Agriculture Bulletin, 7, 503–512.

    Google Scholar 

  2. Hayakawa, T., Suzuki, K., Miura, H., Ohno, T., Igaue, I. (1990). Myo-inositol polyphosphate Intermediates in the dephosphorylation of phytic acid by acid phosphatase with phytase activity from rice bran. Agricultural and Biological Chemistry, 54(2), 279–286.

    Google Scholar 

  3. Thomas, M. P., Mills, S. J., Potter, B. V. L. (2016). The “other” inositols and their phosphates: synthesis, biology, and medicine (with recent advances in myo-inositol chemistry). Angewandte Chemie International Edition, 55, 1614–1650. doi:10.1002/anie.201502227.

    Article  Google Scholar 

  4. Irvine, R. F., & Schell, M. J. (2001). Back in the water: the return of the inositol phosphates. Nature Reviews, 1, 327–338. doi:10.1038/35073015.

    Article  Google Scholar 

  5. Haefner, S., Knietsch, A., Scholten, E., Braun, J., Lohscheidt, M., Zelder, O. (2005). Biotechnological production and applications of phytases. Applied Microbiology and Biotechnology, 68, 588–597. doi:10.1007/s00253-005-0005-y.

    Article  Google Scholar 

  6. Dvorakova, J., Kopecky, J., Havlicek, V., Kren, V. (2000). Formation of myo-inositol phosphates by Aspergillus niger 3-phytase. Folia Microbiologica, 45(2), 128–132.

    Article  Google Scholar 

  7. Siren M (1986a) Stabilized pharmaceutical and biological material composition. Pat. SE 003, 165.

  8. Siren M (1986b) New myo-inositol triphosphoric acid isomer. Pat. SW 052, 950.

  9. Suleimanova, A. D., Beinhauer, A., Valeeva, L. R., Chastukhina, I. B., Balaban, N. P., Shakirov, E. V., et al. (2015). Novel glucose-1-phosphatase with high phytase activity and unusual metal ion activation from soil bacterium Pantoea sp. strain 3.5.1. Applied and Environmental Microbiology, 81, 6790–6799. doi:10.1128/AEM.01384-15.

    Article  Google Scholar 

  10. Sambrook, J., & Russell, D. W. (2001). Molecular cloning: a laboratory manual. USA: Cold Spring Harbor Laboratory Press.

    Google Scholar 

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Acknowledgments

This work was supported by the Russian Foundation for Basic Research (project no. 16-34-60191) and by the subsidy allocated to Kazan Federal University for the state assignment in the sphere of scientific activities (project no. 14–83 0211/02.11.10083.001). The work is performed according to the Russian Government Program of Competitive Growth of Kazan Federal University.

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Correspondence to Aliya D. Suleimanova.

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Suleimanova, A.D., Chastukhina, I.B., Valeeva, L.R. et al. Cloning and Heterologous Expression of Phytase Gene from Pantoea sp. 3.5.1. BioNanoSci. 6, 338–340 (2016). https://doi.org/10.1007/s12668-016-0227-8

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  • DOI: https://doi.org/10.1007/s12668-016-0227-8

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