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Niu-Chang-Chih · 2007 · Research Support, Non U.S. Gov'T

Medium relevance

A highly stable cambialistic-superoxide dismutase from Antrodia camphorata: expression in yeast and enzyme properties.

Antrodia camphorata

Immune supportSkin & hydration
SpeciesNiu-Chang-Chih
JournalJournal of biotechnology
Year2007

Key points

  • A cDNA encoding a putative superoxide dismutase (SOD) was identified in expressed sequence tags of Antrodia camphorata, a medicinal mushroom found only in Taiwan
  • The deduced protein was aligned with Mn-SODs and Fe-SODs from other organisms, this SOD showed greater homology to Mn-SOD. Functional A. camphorata SOD protein was overexpressed in yeast and purified
  • The purified enzyme showed two active forms on a 12.5% native PAGE, a dimer and a monomer
  • The dimeric protein's half-life of deactivation at 80 degrees C was 7 min, and its thermal inactivation rate constant K(d) was 9.87 x 10(-2)min(-1)
  • The enzyme was stable in a broad pH range from 5-11; in the presence of 0.4M imidazole and 2% SDS. The atomic absorption spectrometric assay showed that 1.0 atom of manganese/iron (9:1) was present in each SOD subunit
  • The SOD also documents its future utility in developing anti-inflammatory agent and in the treatment of chronic diseases

From the paper

Abstract

A cDNA encoding a putative superoxide dismutase (SOD) was identified in expressed sequence tags of Antrodia camphorata, a medicinal mushroom found only in Taiwan. The deduced protein was aligned with Mn-SODs and Fe-SODs from other organisms, this SOD showed greater homology to Mn-SOD. Functional A. camphorata SOD protein was overexpressed in yeast and purified. The purified enzyme showed two active forms on a 12.5% native PAGE, a dimer and a monomer. The dimeric protein's half-life of deactivation at 80 degrees C was 7 min, and its thermal inactivation rate constant K(d) was 9.87 x 10(-2)min(-1). The enzyme was stable in a broad pH range from 5-11; in the presence of 0.4M imidazole and 2% SDS. The atomic absorption spectrometric assay showed that 1.0 atom of manganese/iron (9:1) was present in each SOD subunit. The high stability of the enzyme make it better suited than other cambialistic-SODs for use in cosmetics. The SOD also documents its future utility in developing anti-inflammatory agent and in the treatment of chronic diseases.

Citation

Liau YJ, Wen L, Shaw JF, Lin CT (2007). A highly stable cambialistic-superoxide dismutase from Antrodia camphorata: expression in yeast and enzyme properties. Journal of biotechnology https://doi.org/10.1016/j.jbiotec.2007.05.021 PMID: 17604867

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