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

Marianna Turkiewicz; Marzena Pazgier; Halina Kalinowska; Stanisław Bielecki

doi:10.1007/s00792-003-0340-9

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

Marianna Turkiewicz^*, Marzena Pazgier, Halina Kalinowska, Stanisław Bielecki

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

74 Scopus citations

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.

Original language	English
Pages (from-to)	435-442
Number of pages	8
Journal	Extremophiles
Volume	7
Issue number	6
DOIs	https://doi.org/10.1007/s00792-003-0340-9
State	Published - 2003
Externally published	Yes

Keywords

Antarctic
Leucosporidium antarcticum
Psychrophile
Subtilisin-like

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10.1007/s00792-003-0340-9

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title = "A cold-adapted extracellular serine proteinase of the yeast Leucosporidium antarcticum",

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.",

keywords = "Antarctic, Leucosporidium antarcticum, Psychrophile, Subtilisin-like",

author = "Marianna Turkiewicz and Marzena Pazgier and Halina Kalinowska and Stanis{\l}aw Bielecki",

note = "Funding Information: Acknowledgment This work was supported by funding from the Polish Committee of Scientific Researches (grant number 3P04B 026 22).",

year = "2003",

doi = "10.1007/s00792-003-0340-9",

language = "English",

volume = "7",

pages = "435--442",

journal = "Extremophiles",

issn = "1431-0651",

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T1 - A cold-adapted extracellular serine proteinase of the yeast Leucosporidium antarcticum

AU - Turkiewicz, Marianna

AU - Pazgier, Marzena

AU - Kalinowska, Halina

AU - Bielecki, Stanisław

N1 - Funding Information: Acknowledgment This work was supported by funding from the Polish Committee of Scientific Researches (grant number 3P04B 026 22).

PY - 2003

Y1 - 2003

N2 - 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.

AB - 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.

KW - Antarctic

KW - Leucosporidium antarcticum

KW - Psychrophile

KW - Subtilisin-like

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DO - 10.1007/s00792-003-0340-9

M3 - Article

C2 - 12845553

AN - SCOPUS:4544247637

SN - 1431-0651

VL - 7

SP - 435

EP - 442

JO - Extremophiles

JF - Extremophiles

IS - 6

ER -

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

Abstract

Keywords

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