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Archives of Microbiology

, Volume 188, Issue 1, pp 55–68 | Cite as

Degradation of aromatic compounds by Acinetobacter radioresistens S13: growth characteristics on single substrates and mixtures

  • Roberto MazzoliEmail author
  • Enrica Pessione
  • Maria G. Giuffrida
  • Paolo Fattori
  • Cristina Barello
  • Carlo Giunta
  • Nicholas D. Lindley
Original Paper

Abstract

Acinetobacter radioresistens S13 is able to grow on phenol or benzoate as the sole carbon and energy source: both these compounds are catabolized through the β-ketoadipate pathway. Genes encoding the catabolic enzymes for degradation of aromatic compounds are localized on A. radioresistens S13 chromosome and organized in, at least, two distinct sets, one for benzoate degradation and another for phenol catabolism. In the present study, the growth and biodegradation kinetics for benzoate and phenol, and an easily metabolized substrate (acetate) were established. Benzoate was degraded slower and supports a less rapid and efficient growth than either acetate or phenol. A combined transcript-proteomic analysis of some of the major catabolic genes and their products nonetheless has shown that benzoate induces the expression of both benzoate and phenol catabolic operons. This result was confirmed by the fact that benzoate-acclimatized bacteria were rapidly able to degrade phenol too. Finally, the growth and biodegradation kinetics for different mixtures of acetate, benzoate and phenol were determined. Results indicate that a hierarchy of substrate utilization, benzoate > acetate > phenol, occurred: benzoate was the preferred substrate, despite its lower growth and biodegradation parameters. Hypotheses explaining these unusual metabolic features of A. radioresistens S13 are discussed.

Keywords

Proteome Transcript analysis Ortho cleavage pathway Benzoate dioxygenase Phenol hydroxylase 

Abbreviations

AP

Alkaline phosphatase

PH

Phenol hydroxylase and its components (PHO oxygenase, PHR reductase, PHI intermediate)

BD

Benzoate dioxygenase and its components (BDR reductase, BDO oxygenase)

DHBDH

Dihydroxybenzoate dehydrogenase

C12O IsoA (gene catAA)

Catechol 1,2-dioxygenase isoenzyme A

C12O IsoB (gene catAB)

Catechol 1,2-dioxygenase isoenzyme B

MCI (gene catB)

Muconate cycloisomerase

MLI (gene catC)

Muconolactone isomerase

β-KT

β-ketoadipil-CoA thiolase

BenA

The gene encoding BDOα

MopN

The gene encoding PHOα

μ

Bacterial specific growth rate

qX

Substrate consumption rate

YX/S

Bacterial growth yield

Cmmol

Millimoles of carbon

Notes

Acknowledgments

We would like to thank Dr. Sergine Even for invaluable aid in the optimization of transcript techniques. This study received financial support from FIRB. Roberto Mazzoli received a European Union Marie Curie Training Site grant (HPMT-2000-00135) while travel expenses were possible due to financial support from the Franco-Italian Galileo bilateral support scheme.

Supplementary material

203_2007_223_MOESM1_ESM.ppt (155 kb)
ESM1 (PPT 155 KB)

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Copyright information

© Springer-Verlag 2007

Authors and Affiliations

  • Roberto Mazzoli
    • 1
    • 3
    Email author
  • Enrica Pessione
    • 1
  • Maria G. Giuffrida
    • 2
  • Paolo Fattori
    • 1
  • Cristina Barello
    • 2
  • Carlo Giunta
    • 1
  • Nicholas D. Lindley
    • 3
  1. 1.Dipartimento di Biologia Animale e dell’UomoUniversità di TorinoTorinoItaly
  2. 2.ISPA-CNRColleretto Giacosa (To)Italy
  3. 3.Laboratoire d’Ingénierie des Systèmes Biologiques et des Procédés, UMR CNRS/INRA/INSAInstitut National des Sciences AppliquéesToulouseFrance

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