Purification and degradation characteristics of Biphenyl degrading enzyme BphC from <i>Aquamicrobium</i> sp. SK-2

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  • SUGAWARA Hideto
    Division of Sustainable and Environmental Engineering, Muroran Institute of Technology
  • KOYAMA Daiki
    Division of Sustainable and Environmental Engineering, Muroran Institute of Technology
  • SAWADA Ken
    Division of Production Systems Engineering, Muroran Institute of technology
  • CHANG Young-Cheol
    Division of Sustainable and Environmental Engineering, Muroran Institute of Technology
  • KIKUCHI Shintaro
    Division of Sustainable and Environmental Engineering, Muroran Institute of Technology

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  • <i>Aquamicrobium</i> sp. SK-2 株由来 Biphenyl 分解酵素 BphC の精製と分解特性

Abstract

 In the present study, we purified the biphenyl-degrading enzyme 2, 3-dihydroxybiphenyl-1, 2-dioxygenase (BphC) from the bacteria Aquamicrobium sp. SK-2. The BphC was dimer and had molecular weight of 65 kDa. This enzyme showed activity at wide range of temperatures, and from a neutral to an alkali pH, it showed highest activity, at 30°C and pH 8, respectively. The BphC showed Km (12.0 μM) and Vmax(154 mM/min) values with the substrate 2, 3-dihydroxybiphenyl. This result indicated that the BphC had a relatively high affinity with the substrate 2, 3-dihydroxybiphenyl. We analyzed the N-terminal amino acid sequence of the purified enzyme. Sequencing results denoted that the enzyme BphC from SK-2 had high homology (92%) with the enzyme of Pseudomonas sp. KKS102. Based on these results we concluded that BphC was involved in the ring-opening reactions of 2, 3-dihydroxybiphenyl and catechol.

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