Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Purification and Characterization of 2,4-Dichlorophenol Oxidizing Peroxidase from Streptomyces sp. AD001

  • Jeon, Jeong-Ho (Department of biological Science/BK21 Graduate program in Environmental and Biological Engineering, MyongJu University) ;
  • Yun-Jon Han (Department of biological Science/BK21 Graduate program in Environmental and Biological Engineering, MyongJu University) ;
  • Tae-Gu kang (Department of biological Science/BK21 Graduate program in Environmental and Biological Engineering, MyongJu University) ;
  • Eung-Soo Kim (Department of Biotechnology, Inha University) ;
  • Soon-Kwang Hong (Department of biological Science/BK21 Graduate program in Environmental and Biological Engineering, MyongJu University) ;
  • Byeong-Chul Jeong (Department of biological Science/BK21 Graduate program in Environmental and Biological Engineering, MyongJu University)
  • Published : 2002.12.01
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Abstract

Streptomyces sp. AD001 is a Gram-positive soil actinomycetes secreting an uncharacterized 2,4-dichlorophenol (DCP) oxidizing enzyme, whose activity is similar to the previously known Actinomycetes lignin-peroxidase (ALiP). This extracellular peroxidase was purified from Streptomyces sp. AD001 as a single protein band on an SDS-PACE by ammonium sulfate fractionation, Q-sepharose, concanavalin A, and Bio-Gel HTP column chromatographies. The molecular mass of the purified peroxidase was determined by SDS-PAGE to be 45.2 kDa, and 49.7 kDa with MALDI-TOF-MS, respectively. The highest level of peroxidase activity was observed at pH 7.5 and $30^{\circ}C$. The amino terminal sequence of the purified peroxidase (G-E-P-E-E-G-N-V-D-G-T-L) showed no significant homologies to my known proteins, suggesting that Streptomyces sp. AD001 may secrete a novel kind of bacterial peroxidase Initial rate kinetic data of the 2,4-DCP oxidation were best modeled with a random-binding bireactant system.

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