Biotransformation of petroleum asphaltenes and high molecular weight polycyclic aromatic hydrocarbons by Neosartorya fischeri

Environ Sci Pollut Res Int. 2016 Jun;23(11):10773-10784. doi: 10.1007/s11356-016-6277-1. Epub 2016 Feb 19.

Abstract

Neosartorya fischeri, an Aspergillaceae fungus, was evaluated in its capacity to transform high molecular weight polycyclic aromatics hydrocarbons (HMW-PAHs) and the recalcitrant fraction of petroleum, the asphaltenes. N. fischeri was able to grow in these compounds as sole carbon source. Coronene, benzo(g,h,i)perylene, and indeno(1,2,3-c,d)pyrene, together with the asphaltenes, were assayed for fungal biotransformation. The transformation of the asphaltenes and HMW-PAHs was confirmed by reverse-phase high-performance liquid chromatography (HPLC), nano-LC mass spectrometry, and IR spectrometry. The formation of hydroxy and ketones groups on the PAH molecules suggest a biotransformation mediated by monooxygenases such as cytochrome P450 system (CYP). A comparative microarray with the complete genome from N. fischeri showed three CYP monooxygenases and one flavin monooxygenase genes upregulated. These findings, together with the internalization of aromatic substrates into fungal cells and the microsomal transformation of HMW-PAHs, strongly support the role of CYPs in the oxidation of these recalcitrant compounds.

Keywords: Asphaltenes; Biotransformation; Cytochrome P450; Neosartorya fischeri; Polycyclic aromatic hydrocarbons.

MeSH terms

  • Biotransformation
  • Chromatography, High Pressure Liquid
  • Cytochrome P-450 Enzyme System / genetics
  • Cytochrome P-450 Enzyme System / metabolism
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism
  • Genome, Fungal
  • Microarray Analysis
  • Molecular Weight
  • Neosartorya / metabolism*
  • Oxidation-Reduction
  • Petroleum*
  • Polycyclic Aromatic Hydrocarbons / chemistry
  • Polycyclic Aromatic Hydrocarbons / metabolism*

Substances

  • Fungal Proteins
  • Petroleum
  • Polycyclic Aromatic Hydrocarbons
  • Cytochrome P-450 Enzyme System