Media containing aromatic compounds induce peculiar proteins inAcinetobacter radioresistens, as revealed by proteome analysis
| Autor: | Amedeo Conti, Roberto Mazzoli, Cristina Barello, Enrica Pessione, Carlo Giunta, Giuseppina Dellavalle, Maria Gabriella Giuffrida |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Muconic acid
Proteome Metabolite Clinical Biochemistry Dehydrogenase Biochemistry Analytical Chemistry chemistry.chemical_compound Bacterial Proteins Dioxygenase Acinetobacter radioresistens Phenol Electrophoresis Gel Two-Dimensional Proteoma chemistry.chemical_classification Acinetobacter biology Membrane biology.organism_classification Culture Media Enzyme chemistry Energy source Bioremediation Aromatici |
| Zdroj: | Electrophoresis (Weinh., Print) 9 (2001): 1705–1711. info:cnr-pdr/source/autori:Giuffrida M.G.1, Pessione E.2, Mazzoli R.2, Dellavalle G.1, Barello C.1, Conti A.1, Giunta C.2/titolo:Media containing aromatic compounds induce peculiar proteins in Acinetobacter radioresistens as revealed by Proteome analysis/doi:/rivista:Electrophoresis (Weinh., Print)/anno:2001/pagina_da:1705/pagina_a:1711/intervallo_pagine:1705–1711/volume:9 |
| ISSN: | 1522-2683 0173-0835 |
| Popis: | An Acinetobacter radioresistens strain able to grow on phenol or benzoate as sole carbon and energy source through the beta-ketoadipate pathway was isolated in our laboratories. In previous research, we found a different expression of catechol-1,2-dioxygenase isoenzymes (C-1,2-O) depending on the growth substrate (phenol or benzoate). In the present study, we used proteome techniques to extend our investigation to other enzymes involved in the aromatic degradation pathway. Since the first nontoxic metabolite in this route is cis,cis-muconic acid, we focused our attention on the enzymes leading to this compound, chiefly phenol hydroxylase (PH), benzoate dioxygenase (BD), cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase (D) and C-1,2-O. In particular, the A. radioresistens proteome was monitored under different growth substrate conditions, using acetate, benzoate, or phenol as sole carbon source. We compared the protein maps by software image analysis and detected marked differences, suggesting the inducibility of most enzymes. This research also sought to evaluate the conditions allowing the best expression of enzymes to be used in immobilized systems suitable for bioremediation. The experimental data indicate that benzoate is the best carbon source to gain the highest amount of C-1,2-O and D, while phenol is the best growth substrate to obtain PH. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text