Open AccessCharacterization of the Medium- and Long-Chain n-Alkanes Degrading Pseudomonas aeruginosa Strain SJTD-1 and Its Alkane Hydroxylase Genes
Author(s) -
Huan Liu,
Jing Xu,
Rubing Liang,
Jianhua Liu
Publication year - 2014
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0105506
Subject(s) - octadecane , alkane , hexadecane , monooxygenase , pseudomonas aeruginosa , tetradecane , pseudomonas , bacteria , biology , gene , microbiology and biotechnology , biochemistry , strain (injury) , pseudomonadaceae , pristane , thermophile , pseudomonadales , enzyme , chemistry , hydrocarbon , stereochemistry , genetics , organic chemistry , cytochrome p450 , catalysis , anatomy
A gram-negative aliphatic hydrocarbon-degrading bacterium SJTD-1 isolated from oil-contaminated soil was identified as Pseudomonas aeruginosa by comparative analyses of the 16S rRNA sequence, phenotype, and physiological features. SJTD-1 could efficiently mineralize medium- and long-chain n- alkanes (C 12 -C 30 ) as its sole carbon source within seven days, showing the most optimal growth on n -hexadecane, followed by n -octadecane, and n -eicosane. In 36 h, 500 mg/L of tetradecane, hexadecane, and octadecane were transformed completely; and 2 g/L n -hexadecane was degraded to undetectable levels within 72 h. Two putative alkane-degrading genes (gene 3623 and gene 4712) were characterized and our results indicated that their gene products were rate-limiting enzymes involved in the synergetic catabolism of C 12 –C 16 alkanes. On the basis of bioinformatics and transcriptional analysis, two P450 monooxygenases, along with a putative AlmA-like oxygenase, were examined. Genetically defective mutants lacking the characteristic alkane hydroxylase failed to degrade n -octadecane, thereby suggesting a different catalytic mechanism for the microbial transformation of alkanes with chain lengths over C 18 .