Molecular adaptation to high temperatures: pernisine from the archaeon Aeropyrum pernix K1

Authors

  • Kevin Hartman Biotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, 1000 Ljubljana, Slovenia
  • Miha Bahun Biotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, 1000 Ljubljana, Slovenia
  • Marko Šnajder Biotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, 1000 Ljubljana, Slovenia
  • Nataša Poklar Ulrih Biotechnical Faculty, University of Ljubljana, Jamnikarjeva 101, 1000 Ljubljana, Slovenia

Keywords:

expression systems, molecular adaptation, pernisine, thermally stable enzymes

Abstract

Pernisine is a subtilisin-like protease from the hyperthermophilic archaeon Aeropyrum pernix. Due to its high thermal stability and its activity in the presence of denaturants, pernisine represents a promising enzyme for use in various industrial applications. Another potentially applicable characteristic of this protease is its ability to degrade infectious prion aggregates. Production of pernisine in A. pernix does not provide sufficient yield for its commercial use, and alternative production strategies are hence needed. This review summarizes the biochemical and biophysical characteristics of pernisine and progress that has been made toward production of recombinant pernisine using Escherichia coli and Streptomyces rimosus as expression systems.

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Published

2020-02-27

How to Cite

Hartman, K., Bahun, M., Šnajder, M., & Poklar Ulrih, N. (2020). Molecular adaptation to high temperatures: pernisine from the archaeon Aeropyrum pernix K1. Biologia Serbica, 41(2). Retrieved from https://journal.pmf.uns.ac.rs/index.php/biologiaserbica/article/view/88

Issue

Vol. 41 No. 2 (2019): Biologia Serbica

Section

Review paper