The unique cold-adapted extracellular subtilase from psychrophilic yeast Leucosporidium antarcticum

Marzena Pazgier, Marianna Turkiewicz*, Halina Kalinowska, Stanislaw Bielecki

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

The extracellular subtilase synthesized by a strain of L. antarcticum isolated from the Admiralty Bay waters (depth of 200m) was purified to homogeneity by means of 3-step column chromatography and characterized. The enzyme appeared to be kinetically and thermodynamically adapted to cold (Topt 25°C, poor thermostability, high catalytic efficiency at 5-25°C, low values of ΔG*, ΔH*, ΔS* and Ea). The sequence of 35 N-terminal amino acid residues of the L. antarcticum proteinase shows 31 and 37% homology with that of proteinase K and A. oligospora subtilase, respectively, thus indicating that the L. antarcticum serine proteinase belongs to the subfamily C clan SB. It is the first psychrophilic yeast subtilase in this subfamily.

Original languageEnglish
Pages (from-to)39-42
Number of pages4
JournalJournal of Molecular Catalysis B: Enzymatic
Volume21
Issue number1-2
DOIs
StatePublished - 2 Jan 2003
Externally publishedYes

Keywords

  • Leucosporidium antarcticum
  • Subtilase
  • Yeast

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