, Volume 7, Issue 6, pp 435–442

A cold-adapted extracellular serine proteinase of the yeast Leucosporidium antarcticum

  • Marianna Turkiewicz
  • Marzena Pazgier
  • Halina Kalinowska
  • Stanisław Bielecki
Original Paper


An extracellular serine proteinase, lap2, from the psychrophilic antarctic yeast Leucosporidium antarcticum 171 was purified to homogeneity and characterized. The enzyme is a glycoprotein with a molecular mass of 34.4 kDa and an isoelectric point of pH 5.62. The proteinase is halotolerant, and its activity and stability are dependent neither on Ca2+ nor on other metal ions. Lap2 is a true psychrophilic enzyme because of low optimal temperature (25°C), poor thermal stability, relatively small values of free energy, enthalpy and entropy of activation, and high catalytic efficiency at 0–25°C. The 35 N-terminal amino acid residues of lap2 have homology with subtilases of the proteinase K subfamily (clan SB, family S8, subfamily C). The proteinase lap2 is the first psychrophilic subtilase in this family.


Antarctic Leucosporidium antarcticum Psychrophile Subtilisin-like 


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Copyright information

© Springer-Verlag 2003

Authors and Affiliations

  • Marianna Turkiewicz
    • 1
  • Marzena Pazgier
    • 1
  • Halina Kalinowska
    • 1
  • Stanisław Bielecki
    • 1
  1. 1.Institute of Technical BiochemistryTechnical University of ŁódźŁódźPoland

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