The dual functions of biphenyl-degrading ability of Pseudomonas sp. KKS102: Energy acquisition and substrate detoxification

Mina Delawary, Yoshiyuki Ohtsubo, Akinori Ohta

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

The bph operon of Pseudomonas sp. KKS102 is constituted of 11 bph genes which encode enzymes for biphenyl assimilation. Growth of a mutant in which a large part of the bph operon was deleted was inhibited by biphenyl in a concentration-dependent manner. We constructed a series of bph operon deletion mutants and tested for their biphenyl sensitivity. Growth inhibition by biphenyl was more prominent with the mutants defective in bphA1, bphB, bphC, and bphD, which were clustered in the bph operon and working in the early stage of the biphenyl degradation. The mutant defective in bphE, which was working at the late stage and forming a different cluster from the early stage genes, was not much inhibited by biphenyl. These indicate that biphenyl is detoxified by enzymes which function in the early stage of biphenyl assimilation and thus detoxification of substrates as well as energy acquisition could have played an important role in the evolution of the KKS102 bph operon.

Original languageEnglish
Pages (from-to)1970-1975
Number of pages6
JournalBioscience, Biotechnology and Biochemistry
Volume67
Issue number9
DOIs
Publication statusPublished - 2003 Sep

Keywords

  • Biphenyl
  • Detoxification
  • Growth inhibition
  • Pseudomonas sp. KKS102

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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