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

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Abstract

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.

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Acknowledgment

This work was supported by funding from the Polish Committee of Scientific Researches (grant number 3P04B 026 22 ).

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Authors and Affiliations

  1. Institute of Technical Biochemistry, Technical University of Łódź, ul. Stefanowskiego 4/10, 90-924, Łódź, Poland

    Marianna Turkiewicz, Marzena Pazgier, Halina Kalinowska & Stanisław Bielecki

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  1. Marianna Turkiewicz
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  2. Marzena Pazgier
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  3. Halina Kalinowska
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  4. Stanisław Bielecki
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Correspondence to Marianna Turkiewicz.

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Communicated by K. Horikoshi

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Turkiewicz, M., Pazgier, M., Kalinowska, H. et al. A cold-adapted extracellular serine proteinase of the yeast Leucosporidium antarcticum . Extremophiles 7, 435–442 (2003). https://doi.org/10.1007/s00792-003-0340-9

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