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

• Published in: Journal of molecular catalysis. B, Enzymatic Vol. 21; no. 1; pp. 39 - 42
• Main Authors: Pazgier, Marzena, Turkiewicz, Marianna, Kalinowska, Halina, Bielecki, Stanislaw
• Format: Journal Article Conference Proceeding
• Language: English
• Published: Amsterdam Elsevier B.V 02.01.2003; Elsevier Science
• Subjects: Biological and medical sciences; Biology of microorganisms of confirmed or potential industrial interest; Biotechnology; Fundamental and applied biological sciences. Psychology; Leucosporidium antarcticum; Miscellaneous; Mission oriented research; Subtilase; Yeast; Subtilase; Leucosporidium antarcticum; Yeast; Fungi; Peptidases; Purification; Enzyme; Psychrophily; Basidiomycetes; Hydrolases; Leucosporidium; Physicochemical properties; Thallophyta
• ISSN: 1381-1177; 1873-3158
• DOI: 10.1016/S1381-1177(02)00134-0

The extracellular subtilase synthesized by a strain of L. antarcticum isolated from the Admiralty Bay waters (depth of 200 m) was purified to homogeneity by means of 3-step column chromatography and characterized. The enzyme appeared to be kinetically and thermodynamically adapted to cold ( T opt 25 °C, poor thermostability, high catalytic efficiency at 5–25 °C, low values of Δ G ∗, Δ H ∗, Δ S ∗ and E a). 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.