TY - JOUR
T1 - The unique cold-adapted extracellular subtilase from psychrophilic yeast Leucosporidium antarcticum
AU - Pazgier, Marzena
AU - Turkiewicz, Marianna
AU - Kalinowska, Halina
AU - Bielecki, Stanislaw
N1 - Funding Information:
The studies were partially supported by funding from the Polish Committee of Scientific Researches (Grant no. 3 PO4B 02622).
PY - 2003/1/2
Y1 - 2003/1/2
N2 - 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.
AB - 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.
KW - Leucosporidium antarcticum
KW - Subtilase
KW - Yeast
UR - http://www.scopus.com/inward/record.url?scp=0037413449&partnerID=8YFLogxK
U2 - 10.1016/S1381-1177(02)00134-0
DO - 10.1016/S1381-1177(02)00134-0
M3 - Article
AN - SCOPUS:0037413449
SN - 1381-1177
VL - 21
SP - 39
EP - 42
JO - Journal of Molecular Catalysis B: Enzymatic
JF - Journal of Molecular Catalysis B: Enzymatic
IS - 1-2
ER -