Skip to main content

Advertisement

SpringerLink
Log in

A New Alkaliphilic Cold-Active Esterase from the Psychrophilic Marine Bacterium Rhodococcus sp.: Functional and Structural Studies and Biotechnological Potential

  • Published:
Applied Biochemistry and Biotechnology Aims and scope Submit manuscript

Abstract

The special features of cold-adapted lipolytic biocatalysts have made their use possible in several industrial applications. In fact, cold-active enzymes are known to be able to catalyze reactions at low temperatures, avoiding side reactions taking place at higher temperatures and preserving the integrity of products. A lipolytic gene was isolated from the Arctic marine bacterium Rhodococcus sp. AW25M09 and expressed in Escherichia coli as inclusion bodies. The recombinant enzyme (hereafter called RhLip) showed interesting cold-active esterase activity. The refolded purified enzyme displayed optimal activity at 30 °C and was cold-active with retention of 50 % activity at 10 °C. It is worth noting that the optimal pH was 11, and the low relative activity below pH 10 revealed that RhLip was an alkaliphilic esterase. The enzyme was active toward short-chain p-nitrophenyl esters (C2–C6), displaying optimal activity with the butyrate (C4) ester. In addition, the enzyme revealed a good organic solvent and salt tolerance. These features make this an interesting enzyme for exploitation in some industrial applications.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6
Fig. 7
Fig. 8

Similar content being viewed by others

References

  1. Rhee, S. K., Liu, X., Wu, L., Chong, S. C., Wan, X., & Zhou, J. (2004). Applied and Environmental Microbiology, 70, 4303–4317.

    Article  CAS  Google Scholar 

  2. Gupta, R., Gupta, N., & Rathi, P. (2004). Applied Microbiology and Biotechnology, 64, 763–781.

    Article  CAS  Google Scholar 

  3. Aurilia, V., Parracino, A., & D’Auria, S. (2008). Microbial carbohydrate esterases in cold adapted environments. Gene, 410, 234–240.

    Article  CAS  Google Scholar 

  4. Paredes, D. I., Watters, K., Pitman, D. J., Bystroff, C., & Dordick, J. S. (2011). BMC Structural Biology, 11, 42.

    Article  CAS  Google Scholar 

  5. Cavicchioli, R., Charlton, T., Ertan, H., Mohd Omar, S., Siddiqui, K. S., & Williams, T. J. (2011). Microbial Biotechnology, 4, 449–460.

    Article  CAS  Google Scholar 

  6. Jeon, J. H., Kim, J. T., Kang, S. G., Lee, J. H., & Kim, S. J. (2009). Marine Biotechnology (NY), 11, 307–316.

    Article  CAS  Google Scholar 

  7. de Pascale, D., De Santi, C., Fu, J., & Landfald, B. (2012). Marine Genomics, 8, 15–22.

    Article  Google Scholar 

  8. Hjerde, E., Pierechod, M. M., Williamson, A. K., et al. (2013). Genome Announcements, 7(1). e0005513.

  9. Rutherford, K., Parkhill, J., Crook, J., Horsnell, T., Rice, P., Rajandream, M. A., et al. (2000). Bioinformatics, 16, 944–945.

    Article  CAS  Google Scholar 

  10. Laemmli, U. K. (1970). Nature, 227, 680–685.

    Article  CAS  Google Scholar 

  11. Thompson, J. D., Higgins, D. G., & Gibson, T. J. (1994). Nucleic Acids Research, 22, 4673–4680.

    Article  CAS  Google Scholar 

  12. Sali, A., & Blundell, T. L. (1993). Journal of Molecular Biology, 234, 779–815.

    Article  CAS  Google Scholar 

  13. Laskowski, R. A. (2001). Nucleic Acids Research, 29, 221–222.

    Article  CAS  Google Scholar 

  14. Laskowski, R. A., MacArthur, M., Moss, D. S., & Thornton, J. M. (1993). Journal Applied Crystallography, 26, 283–291.

    Article  CAS  Google Scholar 

  15. Vriend, G. (1990). Journal of Molecular Graphics, 8(29), 52–56.

    Article  CAS  Google Scholar 

  16. Cavallo, L., Kleinjung, J., & Fraternali, F. (2003). Nucleic Acids Research, 31, 3364–3366.

    Article  CAS  Google Scholar 

  17. Hess, B., Kutzner, C., van der Spoel, D., & Lindhal, E. (2008). Journal of Chemical Theory and Computation, 4, 435–447.

    Article  CAS  Google Scholar 

  18. Kademi, A., Ait-Abdelkader, N., Fakhreddine, L., & Baratti, J. (2000). Applied Microbiology and Biotechnology, 54, 173–179.

    Article  CAS  Google Scholar 

  19. Park, H. J., Jeon, J. H., Kang, S. G., Lee, J. H., Lee, S. A., & Kim, H. K. (2007). Protein Expression and Purification, 52, 340–347.

    Article  CAS  Google Scholar 

  20. Hu, X. P., Heath, C., Taylor, M. P., Tuffin, M., & Cowan, D. (2012). Extremophiles : Life Under Extreme Conditions, 16, 79–86.

    Article  CAS  Google Scholar 

  21. Kim, Y. H., Kwon, E. J., Kim, S. K., Jeong, Y. S., Kim, J., Yun, H. D., et al. (2010). Biochemical and Biophysical Research Communications, 393, 45–49.

    Article  CAS  Google Scholar 

  22. De Santi, C., Tutino, M. L., Mandrich, L., Giuliani, M., Parrilli, E., Del Vecchio, P., et al. (2010). Biochimie, 92, 949–957.

    Article  CAS  Google Scholar 

  23. Wang, Q., Hou, Y., Ding, Y., & Yan, P. (2012). Molecular Biology Reports, 39, 9233–9238.

    Article  CAS  Google Scholar 

  24. Mandrich, L., De Santi, C., de Pascale, D., & Manco, G. (2012). Journal of Molecular Catalysis B Enzymatic, 83, 46–52.

    Article  CAS  Google Scholar 

  25. Peters, K. S. (2007). Chemical Reviews, 107, 859–873.

    Article  CAS  Google Scholar 

  26. Gandolfi, R., Marinelli, F., Lazzarini, A., & Molinari, F. (2000). Journal of Applied Microbiology, 89, 870–875.

    Article  CAS  Google Scholar 

  27. Morimoto, K., Furuta, E., Hashimoto, H., & Inouye, K. (2006). Journal of Biochemistry, 139, 1065–1071.

    Article  CAS  Google Scholar 

  28. Egorova, K., & Antranikian, G. (2005). Current Opinion in Microbiology, 8, 649–655.

    Article  CAS  Google Scholar 

Download references

Acknowledgments

This work was supported by P.N.R.A. (Italian National Antarctic Research Programme) 2009–2011. We also thank the Yggdrasil application grants 2011–2012 and 2012–2013, funded by the National Research Council of Norway, for supporting the research activities of Dr. Concetta De Santi.

Author information

Authors and Affiliations

  1. Institute of Protein Biochemistry, National Research Council, Via P. Castellino, 111, 80131, Naples, Italy

    Concetta De Santi, Pietro Tedesco, Luca Ambrosino & Donatella de Pascale

  2. NorStruct, Department of Chemistry, Faculty of Science and Technology, University of Tromsø, Tromsø, Norway

    Bjørn Altermark & Nils-Peder Willassen

Authors
  1. Concetta De Santi
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Pietro Tedesco
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Luca Ambrosino
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Bjørn Altermark
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Nils-Peder Willassen
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Donatella de Pascale
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Donatella de Pascale.

Additional information

Concetta De Santi and Pietro Tedesco contributed equally to this work.

Rights and permissions

Reprints and permissions

About this article

Cite this article

De Santi, C., Tedesco, P., Ambrosino, L. et al. A New Alkaliphilic Cold-Active Esterase from the Psychrophilic Marine Bacterium Rhodococcus sp.: Functional and Structural Studies and Biotechnological Potential. Appl Biochem Biotechnol 172, 3054–3068 (2014). https://doi.org/10.1007/s12010-013-0713-1

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s12010-013-0713-1

Keywords

Search

Navigation