To main content

Ralstonia sp U2 naphthalene dioxygenase and Comamonas sp JS765 nitrobenzene dioxygenase show differences in activity towards methylated naphthalenes

Ralstonia sp U2 naphthalene dioxygenase and Comamonas sp JS765 nitrobenzene dioxygenase show differences in activity towards methylated naphthalenes

Category
Journal publication
Abstract
Methylsubstituted naphthalenes constitute a significant part of light gas oil fractions (LGO). These are toxic compounds with low fuel value, and can potentially be enzymatically modified to increase the fuel value and at the same time reduce toxicity. The first step in the biodegradation of naphthalene involves dioxygenation of the aromatic ring catalysed by naphthalene dioxygenase (NDO). Here we show that recombinantly produced NDO from Ralstonia sp. U2 and the related nitrobenzene dioxygenase (NBDO) from Comamonas sp. JS765 can use several mono-, di-, tri-, and tetramethylated naphthalenes as substrates. For the majority of the substrates both enzymes catalyse the formation of a mixture of mono- and dioxygenated products, and it is only dioxygenated products that are likely to be processed further, leading to ring cleavage. In some cases, like for 1-methylnaphthalene, NDO mainly generates the monooxygenated form, while with NBDO, the dioxygenated form dominates. In other cases, as for 1,4-dimethylnaphthalene, the monooxygenated product dominates with NDO, whereas NBDO generates similar amounts of both forms. Presumably, the best future strategy for bioconversion of methylated naphthalenes in LGO is to develop engineered enzyme that are optimised with respect to the specific composition of naphthalene derivatives found in a given product.
Language
English
Author(s)
Affiliation
  • Norwegian University of Science and Technology
  • SINTEF Industry / Biotechnology and Nanomedicine
  • Diverse norske bedrifter og organisasjoner
Year
2012
Published in
Journal of Bioscience and Bioengineering
ISSN
1389-1723
Volume
113
Issue
2
Page(s)
173 - 178