Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Kinetic Properties of Manganese Peroxidase from the Mushroom Stereum ostrea and its Ability to Decolorize Dyes

  • Praveen, K. (Department of Microbiology, Sri Krishnadevaraya University) ;
  • Usha, K.Y. (Department of Microbiology, Sri Krishnadevaraya University) ;
  • Viswanath, Buddolla (Department of Virology, Sri Venkateswara University) ;
  • Reddy, B. Rajasekhar (Department of Microbiology, Sri Krishnadevaraya University)
  • Received : 2011.12.07
  • Accepted : 2012.06.26
  • Published : 2012.11.28
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Abstract

Manganese peroxidase (MnP) was isolated from the culture filtrate of the wood log mushroom Stereum ostrea (S. ostrea), grown on Koroljova medium, and then purified by ammonium sulfate [70% (w/v)] fractionation, DEAE-cellulose anion exchange chromatography, and Sephadex G-100 column chromatography, with an attainment of 88.6-fold purification and the recovery of 22.8% of initial activity. According to SDS-PAGE the molecular mass of the MnP was 40 kDa. The optimal pH and temperature were found to be 4.5 and $35^{\circ}C$, respectively. The enzyme was stable even after exposure to a pH range of 4.5 to 6.0, and at temperatures of up to $35^{\circ}C$ at a pH of 4.5 for 1h. The $K_m$ and $V_{max}$ values for the substrate phenol red were found to be $8{\mu}m$ and 111.14 U/mg of protein, respectively. The MnP also oxidized other substrates such as guaiacol, DMP, and veratryl alcohol. Sodium azide, EDTA, SDS, $Cu^{2+}$, and $Fe^{2+}$, at 1-5 mM, strongly inhibited enzyme activity, whereas $Ca^{2+}$ and $Zn^{2+}$ increased enzyme activity. The participation of the purified enzyme in the decolorization of dyes suggests that S. ostrea manganese peroxidase could be effectively employed in textile industries.

Keywords

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