Proteomics and Metabolomics Analyses to Elucidate the Desulfurization Pathway of Chelatococcus sp

Autor: Mihir K. Chaudhuri, Pabitra Bhagowati, Naba K. Bordoloi, Ashis K. Mukherjee
Jazyk: angličtina
Rok vydání: 2016
Předmět:
0301 basic medicine
Proteomics
Fossil Fuels
Sulfur metabolism
lcsh:Medicine
Environmental pollution
Bacterial growth
Biochemistry
Mass Spectrometry
Analytical Chemistry
chemistry.chemical_compound
Database and Informatics Methods
Spectrum Analysis Techniques
lcsh:Science
Phylogeny
chemistry.chemical_classification
Air Pollutants
Multidisciplinary
Chromatographic Techniques
Lipids
Enzymes
Chemistry
Dibenzothiophene
Physical Sciences
Engineering and Technology
Sequence Analysis
Gasoline
Sulfur utilization
Signal Transduction
Research Article
Chemical Elements
030106 microbiology
Materials Science
Sequence Databases
Fuels
Research and Analysis Methods
Gas Chromatography-Mass Spectrometry
Catalysis
03 medical and health sciences
Diesel Fuel
Biosynthesis
Bacterial Proteins
Beijerinckiaceae
Flavin reductase
Metabolomics
Desulfurization
Molecular Biology Techniques
Sequencing Techniques
Molecular Biology
Materials by Attribute
lcsh:R
Biology and Life Sciences
Proteins
Energy and Power
030104 developmental biology
Enzyme
Biological Databases
chemistry
Enzymology
lcsh:Q
Oils
Sulfur
Zdroj: PLoS ONE, Vol 11, Iss 4, p e0153547 (2016)
PLoS ONE
ISSN: 1932-6203
Popis: Desulfurization of dibenzothiophene (DBT) and alkylated DBT derivatives present in transport fuel through specific cleavage of carbon-sulfur (C-S) bonds by a newly isolated bacterium Chelatococcus sp. is reported for the first time. Gas chromatography-mass spectrometry (GC-MS) analysis of the products of DBT degradation by Chelatococcus sp. showed the transient formation of 2-hydroxybiphenyl (2-HBP) which was subsequently converted to 2-methoxybiphenyl (2-MBP) by methylation at the hydroxyl group of 2-HBP. The relative ratio of 2-HBP and 2-MBP formed after 96 h of bacterial growth was determined at 4:1 suggesting partial conversion of 2-HBP or rapid degradation of 2-MBP. Nevertheless, the enzyme involved in this conversion process remains to be identified. This production of 2-MBP rather than 2-HBP from DBT desulfurization has a significant metabolic advantage for enhancing the growth and sulfur utilization from DBT by Chelatococcus sp. and it also reduces the environmental pollution by 2-HBP. Furthermore, desulfurization of DBT derivatives such as 4-M-DBT and 4, 6-DM-DBT by Chelatococcus sp. resulted in formation of 2-hydroxy-3-methyl-biphenyl and 2-hydroxy -3, 3/- dimethyl-biphenyl, respectively as end product. The GC and X-ray fluorescence studies revealed that Chelatococcus sp. after 24 h of treatment at 37°C reduced the total sulfur content of diesel fuel by 12% by per gram resting cells, without compromising the quality of fuel. The LC-MS/MS analysis of tryptic digested intracellular proteins of Chelatococcus sp. when grown in DBT demonstrated the biosynthesis of 4S pathway desulfurizing enzymes viz. monoxygenases (DszC, DszA), desulfinase (DszB), and an NADH-dependent flavin reductase (DszD). Besides, several other intracellular proteins of Chelatococcus sp. having diverse biological functions were also identified by LC-MS/MS analysis. Many of these enzymes are directly involved with desulfurization process whereas the other enzymes/proteins support growth of bacteria at an expense of DBT. These combined results suggest that Chelatococcus sp. prefers sulfur-specific extended 4S pathway for deep-desulphurization which may have an advantage for its intended future application as a promising biodesulfurizing agent.
Databáze: OpenAIRE
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