An efficient method for the expression and reconstitution of thermostable Mn/Fe superoxide dismutase from Aeropyrum pernix K1

Hee Jin Lee; Hye Won Kwon; Jong Uk Koh; Dong Kuk Lee; Ja Young Moon; Kwang Hoon Kong

doi:10.4014/jmb.0911.11008

An efficient method for the expression and reconstitution of thermostable Mn/Fe superoxide dismutase from Aeropyrum pernix K1

Hee Jin Lee, Hye Won Kwon, Jong Uk Koh, Dong Kuk Lee, Ja Young Moon, Kwang Hoon Kong

Dept. of Fine Chemistry

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

9 Scopus citations

Abstract

The gene APE0743 encoding the superoxide dismutase (ApSOD) of a hyperthermophilic archaeon Aeropyrum pernix K1 was cloned and overexpressed as a GST fusion protein at a high level in Escherichia coli. The expressed protein was simply purified by the process of glutathione affinity chromatography and thrombin treatment. The ApSOD was a homodimer of 25 kDa subunits and a cambialistic SOD, which was active with either Fe(II) or Mn(II) as a cofactor. The ApSOD was highly stable against high temperature. This thermostable ApSOD is expected to be applicable as a useful biocatalyst for medicine and bioindustrial processes.

Original language	English
Pages (from-to)	727-731
Number of pages	5
Journal	Journal of Microbiology and Biotechnology
Volume	20
Issue number	4
DOIs	https://doi.org/10.4014/jmb.0911.11008
State	Published - Apr 2010

Keywords

Aeropyrum pernix
APE0743
GST tag
Reconstitution
Superoxide dismutase
Thermostable enzyme

Access to Document

10.4014/jmb.0911.11008

Cite this

@article{2057f37be0214d8597f106fca7535004,

title = "An efficient method for the expression and reconstitution of thermostable Mn/Fe superoxide dismutase from Aeropyrum pernix K1",

abstract = "The gene APE0743 encoding the superoxide dismutase (ApSOD) of a hyperthermophilic archaeon Aeropyrum pernix K1 was cloned and overexpressed as a GST fusion protein at a high level in Escherichia coli. The expressed protein was simply purified by the process of glutathione affinity chromatography and thrombin treatment. The ApSOD was a homodimer of 25 kDa subunits and a cambialistic SOD, which was active with either Fe(II) or Mn(II) as a cofactor. The ApSOD was highly stable against high temperature. This thermostable ApSOD is expected to be applicable as a useful biocatalyst for medicine and bioindustrial processes.",

keywords = "Aeropyrum pernix, APE0743, GST tag, Reconstitution, Superoxide dismutase, Thermostable enzyme",

author = "Lee, \{Hee Jin\} and Kwon, \{Hye Won\} and Koh, \{Jong Uk\} and Lee, \{Dong Kuk\} and Moon, \{Ja Young\} and Kong, \{Kwang Hoon\}",

year = "2010",

month = apr,

doi = "10.4014/jmb.0911.11008",

language = "English",

volume = "20",

pages = "727--731",

journal = "Journal of Microbiology and Biotechnology",

issn = "1017-7825",

number = "4",

}

TY - JOUR

T1 - An efficient method for the expression and reconstitution of thermostable Mn/Fe superoxide dismutase from Aeropyrum pernix K1

AU - Lee, Hee Jin

AU - Kwon, Hye Won

AU - Koh, Jong Uk

AU - Lee, Dong Kuk

AU - Moon, Ja Young

AU - Kong, Kwang Hoon

PY - 2010/4

Y1 - 2010/4

N2 - The gene APE0743 encoding the superoxide dismutase (ApSOD) of a hyperthermophilic archaeon Aeropyrum pernix K1 was cloned and overexpressed as a GST fusion protein at a high level in Escherichia coli. The expressed protein was simply purified by the process of glutathione affinity chromatography and thrombin treatment. The ApSOD was a homodimer of 25 kDa subunits and a cambialistic SOD, which was active with either Fe(II) or Mn(II) as a cofactor. The ApSOD was highly stable against high temperature. This thermostable ApSOD is expected to be applicable as a useful biocatalyst for medicine and bioindustrial processes.

AB - The gene APE0743 encoding the superoxide dismutase (ApSOD) of a hyperthermophilic archaeon Aeropyrum pernix K1 was cloned and overexpressed as a GST fusion protein at a high level in Escherichia coli. The expressed protein was simply purified by the process of glutathione affinity chromatography and thrombin treatment. The ApSOD was a homodimer of 25 kDa subunits and a cambialistic SOD, which was active with either Fe(II) or Mn(II) as a cofactor. The ApSOD was highly stable against high temperature. This thermostable ApSOD is expected to be applicable as a useful biocatalyst for medicine and bioindustrial processes.

KW - Aeropyrum pernix

KW - APE0743

KW - GST tag

KW - Reconstitution

KW - Superoxide dismutase

KW - Thermostable enzyme

UR - https://www.scopus.com/pages/publications/77954980176

U2 - 10.4014/jmb.0911.11008

DO - 10.4014/jmb.0911.11008

M3 - Article

C2 - 20467245

AN - SCOPUS:77954980176

SN - 1017-7825

VL - 20

SP - 727

EP - 731

JO - Journal of Microbiology and Biotechnology

JF - Journal of Microbiology and Biotechnology

IS - 4

ER -

An efficient method for the expression and reconstitution of thermostable Mn/Fe superoxide dismutase from Aeropyrum pernix K1

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this