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

Marzena Pazgier; Marianna Turkiewicz; Halina Kalinowska; Stanislaw Bielecki

doi:10.1016/S1381-1177(02)00134-0

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 journal › Article › peer-review

15 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 (T_opt 25°C, poor thermostability, high catalytic efficiency at 5-25°C, low values of ΔG^*, ΔH^*, ΔS^* 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.

Original language	English
Pages (from-to)	39-42
Number of pages	4
Journal	Journal of Molecular Catalysis B: Enzymatic
Volume	21
Issue number	1-2
DOIs	https://doi.org/10.1016/S1381-1177(02)00134-0
State	Published - 2 Jan 2003
Externally published	Yes

Keywords

Leucosporidium antarcticum
Subtilase
Yeast

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10.1016/S1381-1177(02)00134-0

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title = "The unique cold-adapted extracellular subtilase from psychrophilic yeast Leucosporidium antarcticum",

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.",

keywords = "Leucosporidium antarcticum, Subtilase, Yeast",

author = "Marzena Pazgier and Marianna Turkiewicz and Halina Kalinowska and Stanislaw Bielecki",

note = "Funding Information: The studies were partially supported by funding from the Polish Committee of Scientific Researches (Grant no. 3 PO4B 02622).",

year = "2003",

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doi = "10.1016/S1381-1177(02)00134-0",

language = "English",

volume = "21",

pages = "39--42",

journal = "Journal of Molecular Catalysis B: Enzymatic",

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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 - https://www.scopus.com/pages/publications/0037413449

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 -

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

Abstract

Keywords

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