Abstract
Pseudomonas is a widespread bacterial genus embracing a vast number of species. Various genosystematic methods are used to identify Pseudomonas and differentiate these bacteria from species of the same genus and species of other genera. Ability to degrade and produce a whole spectrum of compounds makes these species perspective in industrial applications. It also makes possible to use various media, including wastes, for cultivation of Pseudomonas. Pseudomonads may be applied in bioremediation, production of polymers and low-molecular-weight compounds, biocontrol. Recent studies open up new frontiers for further use of Pseudomonas in various areas.
Keywords
- Pseudomonas bacteria
- physiology
- taxonomy
- application
1. Introduction
Genus
Diversity of
2. Morphology and physiology of Pseudomonas bacteria
Some
Bacterial cells don’t produce prosthecae and aren’t surrounded by sheaths, but they can form biofilms that provide attachment of cells to the substrate and increase stability under adverse conditions [9].
Another important
Strains of
Members of the genus
The β-ketoadipate pathway is the most widespread
Genus
3. Taxonomy and identification of Pseudomonas bacteria
The genus
The identification of
In the 1960s studies on nucleic acid similarity have been started. DNA–DNA hybridization (DDH) has shown high degree of genomic heterogeneity among the species assigned to the genus [14, 22]. DDH is a universal technique that could offer truly genome-wide comparisons between organisms, but it demands large quantities of high-quality DNA (in comparison with PCR-based techniques). It makes DDH time-consuming and labour-intensive [23].
Evidence of the high level of conservatism among ribosomal RNA molecules [24, 25] allowed to divide this genus into five rRNA groups using rRNA–DNA hybridization [26]. Only rRNA group I that included the type species
Sequential development of molecular methods has emphasized the role of 16S rRNA in the identification and classification of bacteria, including
As a result of 16S rRNA sequencing by Moore et al., the genus
Although 16S rRNA gene sequencing is useful for classification and identification, it has some resolution problems at the genus and species level. These problematic groups include the family
Some conservative genes such as
Another recently introduced method for taxonomic investigations of bacteria is multilocus sequence typing/analysis (MLST/MLSA). MLSA is a molecular typing method that consists of sequencing 400-600 bp long fragments of some housekeeping genes, i.e., genes that are present in most bacteria. MLSA has two important advantages over 16S rRNA sequencing: 1) the higher variability of housekeeping genes as compared to the 16S rRNA sequence and increased length of the total analyzed sequence even allow differentiation of strains; 2) sequencing of some genes reduces the risk that horizontal gene transfer obscures the resulting phylogeny [44]. According to the recent MLSA research (16S rRNA,
In addition to sequencing of different genes it’s possible to use a number of other methods. Restriction fragment length polymorphism (RFLP) is related to the polymorphic nature of the locations of restriction enzyme sites within defined genetic regions. As a result of RFLP, restriction profile is revealed. RFLP procedure is simple in manipulation and it doesn’t require sequence information allowing to identify bacteria at species or subspecies level. On the other hand, it’s time consuming and requires large amounts of DNA. The method was applied to determine genomovars and biotypes of various
It’s possible to use polymerase chain reaction-reverse cross-blot hybridization (PCR-RCBH) in detection and identification studies. 16S-23S intergenic spacer region was amplified and used in hybridization assay with specific oligonucleotide probes to fluorescent pseudomonads and certain species of the genus. Positive reactions were observed if studied bacteria at least belonged to genus
Pulsed-field gel electrophoresis (PFGE) can be used for differentiation and identification of single strains [49, 50]. PFGE is often considered the “gold standard” of molecular typing methods. PFGE has the high discriminatory power, however, this method is time-consuming and labour-intensive, and some point mutations can change banding patterns, resulting in misleading results [51]. Enterobacterial repetitive intergenic consensus PCR (ERIC-PCR) is also an effective method for identification of
As mentioned above, some chemotaxonomic markers like pyoverdines also can be taxonomic tools for the identification of
Another possible tool for
There are many methods allowing to identify and classify the
4. Criteria for selection of Pseudomonas bacteria
As mentioned above, pseudomonads are able to degrade a broad spectrum of compounds. They are also characterized by an enormous biosynthesis capacity resulting in the production of a wide range of secondary metabolites and biopolymers. Ability to degrade and synthesize various substances is a vital technological merit of
5. Safety of Pseudomonas bacteria
Important feature of
Antibiotics used to treat
The outer membrane contains proteins (porins) which form water-filled channels for diffusion of hydrophilic molecules. Porins play an important physiological role in the transport of various compounds. β-lactams, aminoglycosides, tetracyclines, and some fluoroquinolones can pass through porin channels [64, 65]. The loss of these porin channels can decrease the susceptibility of
Porin OprD takes part in uptake of basic amino acids, small peptides and carbapenems (such as imipenem and meropenem) [69, 70]. Any substitution or deletion within external loop 2 and loop 3 of OprD results in changes of conformation and can cause imipenem resistance. Functional deletion of loop 2 at H729 induced partial resistance to imipenem and meropenem. Imipenam was found to bind to sites in loop 2 to block channel function. Deletion of loops 3 and 4 in OprD also results in failed expression. However, loop 3 is more likely to serve as a passage channel within OprD for imipenem, but not a direct binding site. Loop 1, loop 5, loop 6, loop 7, and loop 8 are not involved in the passage of imipenem, but either the deletion or amino acid substitutions of loop 5, loop 7, and loop 8 resulted in increased susceptibility to β-lactams, quinolones, chloramphenicol, carbapenems and tetracycline [71-76]. Amino acids including histidine, arginine, and lysine, its analogs, and peptides containing lysine can inhibit the penetration of imipenem in
Polycationic antibiotics, such as polymyxin B and aminoglycosides, and EDTA can pass through outer membrane without porins [78]. They displace divalent cations from lipopolysaccharide (LPS) molecules and destabilize the outer membrane increasing susceptibility to these antibiotics [79, 80]. Overexpression of OprH as a result of mutation or adaptation to low Mg2+ concentrations increases membrane resistance. OprH binds to LPS sites which are occupied by divalent cations and prevents access of polymyxin, gentamicin, and EDTA to these sites [78].
Besides porins,
Additionally,
Another mechanism of antibiotic resistance is modification of antibiotics such as aminoglycosides. Modifying enzymes phosphorylate (aminoglycoside phosphoryltransferase), acetylate (aminoglycoside acetyltransferase), or adenylate (aminoglycoside nucleotidyltransferase) these antibiotics. Aminoglycoside acetyltransferases (AAC) acetylate compounds such as gentamicin, tobramycin, netilmicin, and amikacin at the 1, 3, 6′, and 2′ amino groups. Aminoglycoside phosphoryltransferases (APH) inactivate kanamycin, neomycin, and streptomycin by modification of the 3′-OH of these antibiotics. Primary role of some phosphotransferases such as APH(3′)-IIb may be participation in metabolism, and resistance to aminoglycosides may be provided fortuitously. Aminoglycoside nucleotidyltransferases (ANT) modify aminoglycosides such as streptomycin and gentamicin. ANT(2")-I with AAC(6′) and AAC(3) are the most common enzymes providing for aminoglycoside resistance in
Antibiotic resistance can be provided by changes in targets. Mutations in genes
Biofilm-forming ability provides resistance to adverse conditions, like antibiotic tolerance in
Thereby
6. Waste as media for growth of Pseudomonas bacteria
As mentioned above,
Frying oil is produced in large quantities by the food industry and private households. The used cooking oil changes its composition and contains more than 30% of polar compounds depending on the variety of food, the type of frying and the number of cycles used. The utilization of these compounds is a growing problem, arousing expanding interest in the use of waste in microbial transformation [101]. Most of the tested
Biosurfactants are the surface-active compounds that find use in the cosmetic and food production, healthcare, pulp and paper processing, coal, ceramic, and metal industries. They also may be applied in cleaning of oil-contaminated tankers, oil spill removal, transportation and recovery of crude oil, and bioremediation of contaminated sites. Biosurfactants show advantages over chemical analogs owing to their low toxicity and biodegradable nature.
Similar experiments showed that waste motor lubricant oil and peanut oil cake [105], waste frying rice bran oil [106], distillery and whey wastes [107], waste frying coconut oil [108], olive oil mill wastewater [109] and molasses [110] can be used as cheap carbon sources for production of biosurfactants by
Glycerol, cassava wastewater, waste cooking oil and cassava wastewater with waste frying oils were evaluated as alternative low-cost carbon substrates for the production of rhamnolipids and polyhydroxyalkanoates (PHAs) by various
PHAs are composed of medium-chain length (R)-3-hydroxyfatty acids characterized by thermoplastic properties, biodegradability and biocompatibility. They make PHAs suitable for use in the packaging, medicine, pharmacy, agriculture and food industries [58]. Technical oleic acid and waste frying oil were shown to be suitable substrates for PHAs production by
Wastes can be used as media in melanin production. Melanins represent a group of macromolecules, synthesized in living organisms by oxidative polymerization of various phenolic substances in the process of adaption [116]. Melanins act as photoprotectants against UV and visible light, charge transport mediators, free-radical scavengers, antioxidants, metal ion balancers [117]. Melanins find applications in agriculture, medicine, cosmetic and pharmaceutical industries. Some bacteria are able to synthesize these compounds. Marine melanin producer
Another possible waste substrate as fermentation media is animal fleshing, the solid waste produced in large amounts by tanning industry. The studied
The potential use of keratinous and chitinous wastes, such as chicken-feathers and shrimp wastes for oil-remediation was shown. Cultures were grown in minimal media with crude oil, or oil supplemented with chicken-feathers or shrimp wastes. The presence of organic wastes, mainly keratinous ones, enhanced the oil-hydrocarbons removal to an extent of 90%. Keratinolytic bacteria were better enzyme producers than the chitinolytic ones, and oil removal in the presence of chicken-feathers was 3.8 times higher than with shrimp wastes, and almost twice, in comparison with oil-only added cultures [123].
Various combinations of agricultural wastes can be tested to promote
Toner waste black powder (TWBP) from copiers and printers is considered to be toxic for environment, and introduction of bacteria can alleviate the problem of TWBP disposal. It was stated that
Tobacco-related processes can release wastes saturated with water-soluble nicotine posing biological and ecological hazard.
7. Stress resistance of Pseudomonas bacteria
There are some ways that allow pseudomonads to resist to adverse conditions. The alternative sigma factors RpoS (σs) and RpoE (σ22; also referred to as AlgU or AlgT in fluorescent pseudomonads) are involved in bacterial survival under stress conditions. The sigma factor encoded by the
The sigma factor AlgU contributes to tolerance towards osmotic, oxidative, and heat stresses in the pathogens
Production of some compounds can provide bacterial resistance to adverse conditions. PHA-negative mutants were more sensitive to heat treatment than non-mutated cells. The similar effect was revealed in biofilms of PHA-negative mutants as compared to non-mutated strains [137]. PHA availability enhances the ATP and ppGpp levels, and ppGpp has been shown to induce expression of the
Study of
Organic solvents are extremely toxic to microbial cells, even at very low concentration. The cell membrane is the primary target for these compounds. Solvents penetrate into and disrupt the lipid bilayer of membrane. Concentration plays a crucial role in determining toxicity of organic solvents. Since Gram-negative bacteria have an additional outer membrane, and Gram-positive bacteria have a single cytoplasmic membrane, it was assumed that Gram-negative bacteria are better equipped to resist to organic solvents. Gram-negative bacteria including some strains of
As mentioned above, ability to form biofilm provides resistance to adverse conditions, like antibiotic exposure of
8. Application of Pseudomonas bacteria
Due to simple requirements of growth conditions and medium composition, capacity to produce and degrade a number of compounds,
Another possible application of
The textile industry makes extensive use of synthetic chemicals as dyes. A significant proportion of these dyes entering the surrounding media via wastewater is toxic to the environment and humans [159]. Dyes obstruct light penetration and oxygen transfer in water reservoirs. They retain stability and persistence in the environment for a long term [160]. Various physicochemical methods have been used for decolorization of dyes in wastewater, but these methods are distinguished by low efficiency, high cost, limited application scope, and production of recalcitrant wastes [161]. Application of bacteria can solve problems typical to physicochemical methods. It was shown that different
9. Conclusion
Genus
Vast potential of pseudomonads as biocontrol agents was demonstrated.
The recent technological advances in the area of genomics and proteomics are now beginning to lay out important avenue of research focused on the role of
References
- 1.
Shinoda S, Okamoto K. Formation and function of Vibrio parahemolyticus lateral flagella. Journal of Bacteriology 1977;129(3) 1266-1271. - 2.
Moore ERB, Tindall BJ, Martins Dos Santos VAP, Pieper DH, Ramos JL, Palleroni NJ. Nonmedical: Pseudomonas. In: Dworkin M, Falkow S, Rosenberg E., Schleifer KH, Stackebrandt E. (eds.) The Prokaryotes Volume 6: Proteobacteria: Gamma Subclass. Springer New York; 2006. p.646-703. DOI: 10.1007/0-387-30746-X_21. - 3.
Woods DE, Straus DC, Johanson WG, Berry VK, Bass JA. Role of pili in adherence of Pseudomonas aeruginosa to mammalian buccal epithelial-cells. Infection and Immunity 1980;29(3) 1146-1151. - 4.
Doig P, Todd T, Sastry PA, Lee KK, Hodges RS, Paranchych W, Irvin RT. Role of pili in adhesion of Pseudomonas aeruginosa to human respiratory epithelial-cells. Infection and Immunity 1988:56(6) 1641-1646. - 5.
Bradley DE. A function of Pseudomonas aeruginosa PAO polar pili: twitching motility. Can Journal of Bacteriology 1980;26(2) 146-154. DOI: 10.1139/m80-022. - 6.
Klausen M, Heydorn A, Ragas P, Lambertsen L, Aaes-Jørgensen A, Molin S, Tolker-Nielsen T. Biofilm formation by Pseudomonas aeruginosa wild type, flagella and type IV pili mutants. Molecular Microbiology 2003;48(6) 1511-1524. DOI: 10.1046/j.1365-2958.2003.03525.x. - 7.
O'Toole GA, Kolter R. Flagellar and twitching motility are necessary for Pseudomonas aeruginosa biofilm development. Molecular Microbiology 1998;30(2) 295-304. DOI: 10.1046/j.1365-2958.1998.01062.x. - 8.
Li CM, Brown I, Mansfield J, Stevens C, Boureau T, Romantschuk M, Taira S. The Hrp pilus of Pseudomonas syringae elongates from its tip and acts as a conduit for translocation of the effector protein HrpZ. The EMBO Journal 2002;21(8) 1909-1915. DOI: 10.1093/emboj/21.8.1909. - 9.
Ghafoor A, Hay ID, Rehm BH. Role of exopolysaccharides in Pseudomonas aeruginosa biofilm formation and architecture. Applied and Environmental Microbiology 2011;77(15) 5238-5246. DOI: 10.1128/AEM.00637-11. - 10.
Meyer JM, Abdallah MA. The fluorescent pigment of Pseudomonas fluorescens: biosynthesis, purification and physicochemical properties. Journal of General Microbiology 1978;107(2) 319-328. DOI: 10.1099/00221287-107-2-319. - 11.
Meyer JM, Hornsperger JM. Role of pyoverdine Pf, the iron binding fluorescent pigment of Pseudomonas fluorescens in iron transport. Journal of General Microbiology 1978;107(2) 329-331. DOI: 10.1099/00221287-107-2-329. - 12.
Takase H, Nitanai H, Hoshino K, Otani T. Impact of siderophore production on Pseudomonas aeruginosa infections in immunosuppressed mice. Infection and Immunity 2000;68(4) 1834-1839. DOI: 10.1128/IAI.68.4.1834-1839.2000. - 13.
Meyer JM, Geoffroy VA, Baida N, Gardan L, Izard D, Lemanceau P, Achouak W, Palleroni NJ. Siderophore typing, a powerful tool for the identification of fluorescent and nonfluorescent pseudomonads. Applied and Environmental Microbiology 2002;68(6) 2745-2753. DOI: 10.1128/AEM.68.6.2745-2753.2002. - 14.
Palleroni NJ. Pseudomonas. In: Brenner DJ, Krieg NR, Staley JT, Garrity GM. (eds.) Bergey’s Manual of Systematic Bacteriology, Volume Two the Proteobacteria Part B the Gammaproteobacteria. 2nd ed. Springer US; 2005. p.323-379. DOI: 10.1007/0-387-28022-7. - 15.
Blondel-Hill E, Henry DA, David P. Pseudomonas. In: Murray PR, Baron EJ, Jorgensen JH, Landry ML, Pfaller MA. (eds.) Manual of Clinical Microbiology. 9th ed. Washington, DC: ASM Press. 2007; p.734-748. - 16.
Wolterink AFWM., Jonker AB, Kengen SWM, Stams AJM. Pseudomonas chloritidismutans sp. nov., a non-denitrifying, chlorate-reducing bacterium. International Journal of Systematic and Evolutionary Microbiology 2002;52(Pt 6) 2183-2190. DOI: 10.1099/ijs.0.02102-0. - 17.
Lessie TG, Phibbs PV Jr. Alternative pathways of carbohydrate utilization in pseudomonads. Annual Review of Microbiology 1984;38: 359-388. DOI: 10.1146/annurev.mi.38.100184.002043. - 18.
Jiménez JI, Nogales J, García JL, Díaz E. A genomic view of the catabolism of aromatic compounds in Pseudomonas . In: Timmis KN. (ed.) Handbook of Hydrocarbon and Lipid Microbiology. Springer Berlin Heidelberg; 2010. p.1297-1325. DOI: 10.1007/978-3-540-77587-4_91. - 19.
Jiménez JI, Miñambres B, Garcı́a JL, Dı́az E. Genomic insights in the metabolism of aromatic compounds in Pseudomonas. In: Ramos JL. (ed.) Pseudomonas, Volume 3 Biosynthesis of Macromolecules and Molecular Metabolism. Springer US; 2004. p.425-462. DOI: 10.1007/978-1-4419-9088-4_15. - 20.
List of prokaryotic names with standing in nomenclature. http://www.bacterio.net (accessed 30 January 2015). - 21.
Stanier RY, Palleroni NJ, Doudoroff M. The aerobic pseudomonads: a taxonomic study. Journal of General Microbiology 1966;43(2) 159-271. DOI: 10.1099/00221287-43-2-159. - 22.
Palleroni NJ. The Pseudomonas story. Environmental Microbiology 2010;12(6) 1377-1383. DOI: 10.1111/j.1462-2920.2009.02041.x. - 23.
Goris J, Konstantinidis KT, Klappenbach JA, Coenye T, Vandamme P, Tiedje JM. DNA-DNA hybridization values and their relationship to whole-genome sequence similarities. International Journal of Systematic and Evolutionary Microbiology 2007;57(Pt 1) 81-91. DOI: 10.1099/ijs.0.64483-0. - 24.
Doi RH, Igarashi RT. Conservation of ribosomal and messenger ribonucleic acid cistrons in Bacillus species. Journal of Bacteriology 1965; 90(2) 384-390. - 25.
Dubnau D, Smith I, Porell P, Marmur J. Gene conservation in Bacillus species. I. Conserved genetic and nucleic acid base sequence homologies. Proceedings of the National Academy of Sciences of the United States of America 1965;54(2) 491-498. DOI: 10.2307/72742. - 26.
Palleroni NJ, Kunisawa R, Contopoulou R, Doudoroff M. Nucleic acid homologies in the genus Pseudomonas. International Journal of Systematic Bacteriology 1973;23(4) 333-339. DOI: 10.1099/00207713-23-4-333. - 27.
Yabuuchi E, Kosako Y, Oyaizu H, Yano I, Hotta H, Hashimoto Y, Ezaki T, Arakawa M. Proposal of Burkholderia gen. nov. and transfer of seven species of the genus Pseudomonas homology group II to the new genus, with the type species Burkholderia cepacia (Palleroni and Holmes 1981) comb. nov. Microbiology and Immunology 1992;36(12) 1251-1275. DOI: 10.1111/j.1348-0421.1992.tb02129.x. - 28.
Yabuuchi E, Kosako Y, Yano I, Hotta I, Nishiuchi Y. Transfer of two Burkholderia and an Alcaligenes species to Ralstonia gen. nov.: proposal of Ralstonia pickettii (Ralston, Palleroni and Doudoroff 1973) comb. nov., Ralstonia solanacearum (Smith 1896) comb. nov. and Ralstonia eutropha (Davis 1969) comb. nov. Microbiology and Immunology 1995;39(11) 897-904. DOI: 10.1111/j.1348-0421.1995.tb03275.x. - 29.
Willems A, Busse J, Goor M, Pot B, Falsen E, Jantzen E, Hoste B, Gillis M, Kersters K, Auling G, De Ley J. Hydrogenophaga, a new genus of hydrogen-oxidizing bacteria that includes Hydrogenophaga flava comb. nov. (formerly Pseudomonas flava), Hydrogenophaga palleroni (formerly Pseudomonas palleroni), Hydrogenophaga pseudoflava (formerly Pseudomonas pseudoflava and ‘‘Pseudomonas carboxydoflava’’), and Hydrogenophaga taeniospiralis (formerly Pseudomonas taeniospiralis). International Journal of Systematic Bacteriology 1989;39(3) 319-333. DOI: 10.1099/00207713-39-3-319. - 30.
Willems A, Falsen E, Pot B, Jantzen E, Hoste B, Vandamme P, Gillis M, Kersters K, De Ley J. Acidovorax, a new genus for Pseudomonas facilis, Pseudomonas delafieldii E. Falsen (EF) group 13, EF group 16, and several clinical isolates, with the species Acidovorax facilis comb. nov., Acidovorax delafieldeii comb. nov., and Acidovorax temperans sp. nov. International Journal of Systematic Bacteriology 1990;40(4) 384-398. DOI: 10.1099/00207713-40-4-384. - 31.
Tamaoka J, Ha D-M, Komagata K. Reclassification of Pseudomonas acidovorans den Dooren de Jong 1926 and Pseudomonas testosteroni Marcus and Talalay 1956 as Comamonas acidovorans comb. nov. and Comamonas testosterone comb. nov., with an emended description of the genus Comamonas. International Journal of Systematic Bacteriology 1987;37(1) 52-59. DOI: 10.1099/00207713-37-1-52. - 32.
Segers P, Vancanneyt M, Pot B, Torck U, Hoste B, Dewettinck D, Felsen E, Kersters K, De Vos P. Classification of Pseudomonas diminuta Leifson and Hugh 1954 and Pseudomonas vesicularis Büsing, Döll, and Freytag 1953 in Brevundimonas gen. nov. as Brevundimonas diminuta comb. nov. and Brevundimonas vesicularis comb. nov., respectively. International Journal of Systematic Bacteriology 1994;44(3) 499-510. DOI: 10.1099/00207713-44-3-499. - 33.
Palleroni NJ, Bradbury JF. Stenotrophomonas, a new bacterial genus for Xanthomonas maltophilia (Hugh 1980) Swings et al. 1983. International Journal of Systematic Bacteriology 1993;43(3) 606-609. DOI: 10.1099/00207713-43-3-606. - 34.
Patel JB. 16S rRNA gene sequencing for bacterial pathogen identification in the clinical laboratory. Molecular Diagnosis 2001;6(4) 313-321. DOI: 10.1007/BF03262067. - 35.
Moore ERB, Mau M, Arnscheidt A, Böttger EC, Hutson RA, Collins MD, van de Peer Y, De Wachter R, Timmis KN. The determination and comparison of the 16S rRNA gene sequences of species of the genus Pseudomonas (sensu stricto) and estimation of the natural intrageneric relationships. Systematic and Applied Microbiology 1996;19(4) 478-492. DOI: 10.1016/S0723-2020(96)80021-X. - 36.
Anzai Y, Kim H, Park JY, Wakabayashi H, Oyaizu H. Phylogenetic affiliation of the pseudomonads based on 16S rRNA sequence. International Journal of Systematic and Evolutionary Microbiology 2000;50(Pt 4) 1563-1589. DOI: 10.1099/00207713-50-4-1563. - 37.
Janda JM, Abbott SL. 16S rRNA gene sequencing for bacterial identification in the diagnostic laboratory: pluses, perils, and pitfalls. Journal of Clinical Microbiology 2007;45(9) 2761-2764. DOI: 10.1128/JCM.01228-07. - 38.
Yamamoto S, Harayama S. Phylogenetic relationships of Pseudomonas putida strains deduced from the nucleotide sequences of gyrB, rpoD and 16S rRNA genes. International Journal of Systematic Bacteriology 1998;48(Pt 3) 813-819. DOI: 10.1099/00207713-48-3-813. - 39.
Yamamoto S, Kasai H, Arnold DL, Jackson RW, Vivian A, Harayama S. Phylogeny of the genus Pseudomonas: intrageneric structure reconstructed from the nucleotide sequences of gyrB and rpoD genes. Microbiology 2000;146 (Pt 10) 2385-2394. - 40.
De Vos D, Bouton C, Sarniguet A, De Vos P, Vauterin M, Cornelis P. Sequence diversity of the oprI gene, coding for major outer membrane lipoprotein I, among rRNA group I pseudomonads. Journal of Bacteriology 1998;180(24) 6551-6556. - 41.
Ait Tayeb L, Ageron E, Grimont F, Grimont PAD. Molecular phylogeny of the genus Pseudomonas based on rpoB sequences and application for the identification of isolates. Research in Microbiology 2005;156(5-6) 763-773. DOI: 10.1016/j.resmic.2005.02.009. - 42.
Hilario E, Buckley TR, Young JM. Improved resolution on the phylogenetic relationships among Pseudomonas by the combined analysis of atp D, car A, rec A and 16S rDNA. Antonie Van Leeuwenhoek. 2004;86(1) 51-64. DOI: 10.1023/B:ANTO.0000024910.57117.16. - 43.
Bodilis J, Barray S. Molecular evolution of the major outer-membrane protein gene (oprF) of Pseudomonas. Microbiology 2006;152(Pt 4) 1075-1088. DOI: 10.1099/mic.0.28656-0. - 44.
Vinatzer BA, Bull CT. The impact of genomic approaches on our understanding of diversity and taxonomy of plant pathogenic bacteria. In: Jackson RW. (ed.) Plant Pathogenic Bacteria: Genomics and Molecular Biology. Horizon Scientific Press; 2009. p.37-61. - 45.
Mulet M, Lalucat J, García-Valdés E. DNA sequence-based analysis of the Pseudomonas species. Environmental Microbiology 2010;12(6) 1513-1530. DOI: 10.1111/j.1462-2920.2010.02181.x. - 46.
Guasp C, Moore ER, Lalucat J, Bennasar A. Utility of internally transcribed 16S-23S rDNA spacer regions for the definition of Pseudomonas stutzeri genomovars and other Pseudomonas species. International Journal of Systematic and Evolutionary Microbiology 2000;50(Pt 4) 1629-1639. DOI: 10.1099/00207713-50-4-1629. - 47.
Scarpellini M, Franzetti L, Galli A. Development of PCR assay to identify Pseudomonas fluorescens and its biotype. FEMS Microbiology Letters 2004;236(2) 257-260. DOI: 10.1111/j.1574-6968.2004.tb09655.x. - 48.
Jaturapahu T., Puttinaowarat S., Somsiri T. Detection and identification of Pseudomonas Spp. by polymerase chain reaction-reverse cross-blot hybridization (PCR-RCBH) with 16S-23S ribosomal RNA intergenic spacer probes. In: Walker P, Lester R, Bondad-Reantaso MG. (eds.) Diseases in Asian Aquaculture: Proceedings of the Fifth symposium on Diseases in Asian Aquaculture, 24-28 November 2002, Queensland, Australia. Fish Health Section, Asian Fisheries Society, Manila, Philippines. 2005. p.447-456. - 49.
Geider K. Differentiation and identification of Pseudomonas syringae pathovars by PCR- and PFGE-Analyses. In: Rudolph K, Burr TJ, Mansfield JW, Stead D, Vivian A, von Kietzell J. (eds.) Developments in Plant Pathology, Volume 9: Pseudomonas syringae Pathovars and Related Pathogens. Springer Netherlands; 1997. p.459-464. DOI: 10.1007/978-94-011-5472-7_82. - 50.
Spencker FB, Haupt S, Claros MC, Walter S, Lietz T, Schille R, Rodloff AC. Epidemiologic characterization of Pseudomonas aeruginosa in patients with cystic fibrosis. Clinical Microbiology and Infection 2000;6(11) 600-607. DOI: 10.1046/j.1469-0691.2000.00171.x. - 51.
Fothergill JL, White J, Foweraker JE, Walshaw MJ, Ledson MJ, Mahenthiralingam E, Winstanley C. Impact of Pseudomonas aeruginosa genomic instability on the application of typing methods for chronic cystic fibrosis infections. Journal of Clinical Microbiology 2010;48(6) 2053-2059. DOI: 10.1128/JCM.00019-10. - 52.
Wolska K, Szweda P. A comparative evaluation of PCR ribotyping and ERIC PCR for determining the diversity of clinical Pseudomonas aeruginosa isolates. Polish Journal of Microbiology 2008;57(2) 157-163. - 53.
Syrmis MW, O'Carroll MR, Sloots TP, Coulter C, Wainwright CE, Bell SC, Nissen MD. Rapid genotyping of Pseudomonas aeruginosa isolates harboured by adult and paediatric patients with cystic fibrosis using repetitive-element-based PCR assays. Journal of Medical Microbiology 2004;53(Pt 11): 1089-1096. DOI: 10.1099/jmm.0.45611-0. - 54.
Han MM, Mu LZ, Liu XP, Zhao J, Liu XF, Liu H. ERIC-PCR genotyping of Pseudomonas aeruginosa isolates from haemorrhagic pneumonia cases in mink. Veterinary Record Open 2014;1(1): e000043. DOI: 10.1136/vropen-2014-000043. - 55.
Meyer JM. Siderotyping and bacterial taxonomy: a siderophore bank for a rapid identification at the species level of fluorescent and non-fluorescent Pseudomonas. In: Varma A, Chincholkar SB. (eds.) Soil Biology, Microbial Siderophores, Volume 12. Springer Berlin Heidelberg; 2007. p.43-66. DOI: 10.1007/978-3-540-71160-5_2. - 56.
Meyer JM, Gruffaz C, Raharinosy V, Bezverbnaya I, Schäfer M, Budzikiewicz H. Siderotyping of fluorescent Pseudomonas: molecular mass determination by mass spectrometry as a powerful pyoverdine siderotyping method. Biometals 2008;21(3) 259-271. DOI: 10.1007/s10534-007-9115-6. - 57.
Tourkya B, Boubellouta T, Dufour E, Leriche F. Fluorescence spectroscopy as a promising tool for a polyphasic approach to pseudomonad taxonomy. Current Microbiology 2009;58(1) 39-46. DOI: 10.1007/s00284-008-9263-0. - 58.
Rehm BHA. Biotechnological relevance of Pseudomonads. In: Rehm BHA. (ed.) Pseudomonas: Model Organism, Pathogen, Cell Factory. Wiley-Blackwell; 2008. p.377-395. DOI: 10.1002/9783527622009.ch14. - 59.
OECD. Section 2 – Pseudomonas. In: Safety Assessment of Transgenic Organisms, Volume 2: OECD Consensus Documents. OECD Publishing; 2006. p.312-393. DOI: 10.1787/9789264095403-10-en. - 60.
Choi JY, Sifri CD, Goumnerov BC, Rahme LG, Ausubel FM, Calderwood SB. Identification of virulence genes in a pathogenic strain of Pseudomonas aeruginosa by representational difference analysis. Journal of Bacteriology 2002;184(4): 952-961. DOI: 10.1128/jb.184.4.952-961.2002. - 61.
Lambert PA. Mechanisms of antibiotic resistance in Pseudomonas aeruginosa. Journal of the Royal Society of Medicine 2002;95(Suppl 41) 22-26. - 62.
Scott MG, Yan H, Hancock REW. Biological properties of structurally related α-helical cationic antimicrobial peptides. Infection and Immunity 1999;67(4) 2005-2009. - 63.
Huang H, Hancock REW. The role of specific surface loop regions in determining the function of the imipenem-specific pore protein OprD of Pseudomonas aeruginosa. Journal of Bacteriology 1996;178(11) 3085-3090. - 64.
Nikaido H. Outer membrane barrier as a mechanism of antimicrobial resistance. Antimicrobial Agents and Chemotherapy 1989;33(11): 1831-1836. DOI: 10.1128/AAC.33.11.1831. - 65.
Yoshimura F, Nikaido H. Diffusion of beta-lactam antibiotics through the porin channels of Escherichia coli K-12. Antimicrobial Agents and Chemotherapy 1985;27(1) 84-92. DOI: 10.1128/AAC.27.1.84. - 66.
Hancock REW, Brinkman FS. Function of pseudomonas porins in uptake and efflux. Annual Review of Microbiology 2002;56 17-38. DOI: 10.1146/annurev.micro.56.012302.160310. - 67.
Brinkman FS, Bains M, Hancock RE. The amino terminus of Pseudomonas aeruginosa outer membrane protein OprF forms channels in lipid bilayer membranes: correlation with a three-dimensional model. Journal of Bacteriology 2000;182(18) 5251-5255. DOI: 10.1128/JB.182.18.5251-5255.2000. - 68.
Bratu S, Landman D, Gupta J, Quale J. Role of AmpD, OprF and penicillin-binding proteins in beta-lactam resistance in clinical isolates of Pseudomonas aeruginosa. Journal of Medical Microbiology 2007;56(6) 809-814. DOI: 10.1099/jmm.0.47019-0. - 69.
Trias J, Nikaido H. Outer membrane protein D2 catalyzes facilitated diffusion of carbapenems and penems through the outer membrane of Pseudomonas aeruginosa. Antimicrobial Agents and Chemotherapy 1990;34(1) 52-57. DOI: 10.1128/AAC.34.1.52. - 70.
Trias J, Nikaido H. Protein D2 channel of the Pseudomonas aeruginosa outer membrane has a binding site for basic amino acids and peptides. Journal of Biological Chemistry 1990;265(26) 15680-15684. - 71.
Ochs MM, Bains M, Hancock REW. Role of putative loops 2 and 3 in imipenem passage through the specific porin OprD of Pseudomonas aeruginosa. Antimicrobial Agents and Chemotherapy 2000;44(7) 1983-1985. DOI: 10.1128/AAC.44.7.1983-1985.2000. - 72.
Huang H, Jeanteur D, Pattus F, Hancock REW. Membrane topology and site specific mutagenesis of Pseudomonas aeruginosa porin OprD. Molecular Microbiology 1995;16(5) 931–941. DOI: 10.1111/j.1365-2958.1995.tb02319.x. - 73.
Huang H, Hancock RW. The role of specific surface loop regions in determining the function of the imipenem-specific pore protein OprD of Pseudomonas aeruginosa. Journal of Bacteriology 1996;178(11) 3085-3090. - 74.
Pirnay JP, De Vos D, Mossialos D, Vanderkelen A, Cornelis P, Zizi M. Analysis of the Pseudomonas aeruginosa oprD gene from clinical and environmental isolates. Environmental Microbiology 2002;4(12) 872-882. DOI: 10.1046/j.1462-2920.2002.00281.x. - 75.
Chevalier S, Bodilis J, Jaouen T, Barray S, Feuilloley MGJ, Orange N. Sequence diversity of the OprD protein of environmental Pseudomonas strains. Environmental Microbiology 2007;9(3) 824-835. DOI: 10.1111/j.1462-2920.2006.01191.x. - 76.
Epp SF, Köhler T, Plésiat P, Michéa-Hamzehpour M, Frey J, Pechère JC. C-terminal region of Pseudomonas aeruginosa outer membrane porin OprD modulates susceptibility to meropenem. Antimicrobial Agents and Chemotherapy 2001;45(6) 1780-1787. DOI: 10.1128/AAC.45.6.1780-1787.2001. - 77.
Muramatsu H, Horii T, Morita M, Hashimoto H, Kanno T, Maekawa M. Effect of basic amino acids on susceptibility to carbapenems in clinical Pseudomonas aeruginosa isolates. International Journal of Medical Microbiology 2003;293(2-3) 191-197. DOI: 10.1078/1438-4221-00256. - 78.
Young ML, Bains M, Bell A, Hancock RE. Role of Pseudomonas aeruginosa outer membrane protein OprH in polymyxin and gentamicin resistance: isolation of an OprH-deficient mutant by gene replacement techniques. Antimicrobial Agents and Chemotherapy 1992;36(11) 2566-2568. DOI: 10.1128/AAC.36.11.2566. - 79.
Hancock RE, Chan L. Outer membranes of environmental isolates of Pseudomonas aeruginosa. Journal of Clinical Microbiology 1988;26(11) 2423-2424. - 80.
M Vaara. Agents that increase the permeability of the outer membrane. Microbiological Reviews 1992;56(3) 395-411. - 81.
Van Bambeke R, Balzi E, Tulkens PM. Antibiotic efflux pumps. Biochemical Pharmacology 2000;60(4) 457-470. DOI: 10.1016/S0006-2952(00)00291-4. - 82.
Stover CK, Pham XQ, Erwin AL, Mizoguchi SD, Warrener P, Hickey MJ, Brinkman FS, Hufnagle WO, Kowalik DJ, Lagrou M, Garber RL, Goltry L, Tolentino E, Westbrock-Wadman S, Yuan Y, Brody LL, Coulter SN, Folger KR, Kas A, Larbig K, Lim R, Smith K, Spencer D, Wong GK, Wu Z, Paulsen IT, Reizer J, Saier MH, Hancock RE, Lory S, Olson MV. Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen. Nature 2000;406(6799) 959-964. DOI: 10.1038/35023079. - 83.
Lister PD, Wolter DJ, Hanson ND. Antibacterial-resistant Pseudomonas aeruginosa: clinical impact and complex regulation of chromosomally encoded resistance mechanisms. Clinical Microbiology Reviews 2009;22(4) 582-610. DOI: 10.1128/CMR.00040-09. - 84.
Livermore DM, Woodford N. The beta-lactamase threat in Enterobacteriaceae, Pseudomonas and Acinetobacter. Trends in Microbiology 2006;14(9) 413-420. DOI: 10.1016/j.tim.2006.07.008. - 85.
Poole K. Aminoglycoside resistance in Pseudomonas aeruginosa. Antimicrobial Agents and Chemotherapy 2005;49(2) 479-487. DOI: 10.1128/AAC.49.2.479-487.2005. - 86.
Yonezawa M, Takahata M, Matsubara N, Watanabe Y, Narita H. DNA gyrase gyrA mutations in quinolone-resistant clinical isolates of Pseudomonas aeruginosa. Antimicrobial Agents and Chemotherapy 1995;39(9) 1970-1972. DOI: 10.1128/AAC.39.9.1970. - 87.
Higgins PG, Fluit AC, Milatovic D, Verhoef J, Schmitz FJ. Mutations in GyrA, ParC, MexR and NfxB in clinical isolates of Pseudomonas aeruginosa. The International Journal of Antimicrobial Agents 2003;21(5) 409-413. DOI: 10.1016/S0924-8579(03)00009-8. - 88.
Salma R, Dabboussi F, Kassaa I, Khudary R, Hamze M. gyrA and parC mutations in quinolone-resistant clinical isolates of Pseudomonas aeruginosa from Nini Hospital in north Lebanon. Journal of Infection and Chemotherapy 2013;19(1) 77-81. DOI: 10.1007/s10156-012-0455-y. - 89.
Flemming HC, Wingender J. Relevance of microbial extracellular polymeric substances (EPSs)-Part I: Structural and ecological aspects. Water Science and Technology 2001;43(6) 1-8. - 90.
Sutherland IW. Exopolysaccharides in biofilms, flocs and related structures. Water Science and Technology 2001;43(6) 77-86. - 91.
Whitchurch CB, Tolker-Nielsen T, Ragas PC, Mattick JS. Extracellular DNA required for bacterial biofilm formation. Science 2002;295(5559) 1487. DOI: 10.1126/science.295.5559.1487. - 92.
Toyofuku M, Roschitzki B, Riedel K, Eberl L. Identification of proteins associated with the Pseudomonas aeruginosa biofilm extracellular matrix. Journal of Proteome Research 2012;11(10) 4906-4915. DOI: 10.1021/pr300395j. - 93.
Ghafoor A, Hay ID, Rehm BH. Role of exopolysaccharides in Pseudomonas aeruginosa biofilm formation and architecture. Applied and Environmental Microbiology 2011;77(15) 5238-5246. DOI: 10.1128/AEM.00637-11. - 94.
Borriello G, Werner E, Roe F, Kim AM, Ehrlich GD, Stewart PS. Oxygen limitation contributes to antibiotic tolerance of Pseudomonas aeruginosa in biofilms. Antimicrobial Agents and Chemotherapy 2004;48(7) 2659-2664. DOI: 10.1128/AAC.48.7.2659-2664.2004. - 95.
Brown MRW, Allison DG, Gilbert P. Resistance of bacterial biofilms to antibiotics: a growth-rate related effect? Journal of Antimicrobial Chemotherapy 1988;22(6) 777-783. DOI: 10.1093/jac/22.6.777. - 96.
Hoyle BD, Alcantara J, Costerton JW. Pseudomonas aeruginosa biofilm as a diffusion barrier to piperacillin. Antimicrobial Agents and Chemotherapy 1992;36(9) 2054-2056. DOI: 10.1128/AAC.36.9.2054. - 97.
Shigeta M, Tanaka G, Komatsuzawa H, Sugai M, Suginaka H, Usui T. Permeation of antimicrobial agents through Pseudomonas aeruginosa biofilms: a simple method. Chemotherapy 1997;43(5) 340-345. - 98.
Alipour M, Suntres ZE, Omri A. Importance of DNase and alginate lyase for enhancing free and liposome encapsulated aminoglycoside activity against Pseudomonas aeruginosa. Journal of Antimicrobial Chemotherapy 2009;64(2) 317-325. DOI: 10.1093/jac/dkp165. - 99.
Pamp SJ, Gjermansen M, Johansen HK, Tolker-Nielsen T. Tolerance to the antimicrobial peptide colistin in Pseudomonas aeruginosa biofilms is linked to metabolically active cells, and depends on the pmr and mexAB-oprM genes. Molecular Microbiology 2008;68(1) 223-240. DOI: 10.1111/j.1365-2958.2008.06152.x. - 100.
Banin E, Brady KM, Greenberg EP. Chelator-induced dispersal and killing of Pseudomonas aeruginosa cells in a biofilm. Applied and Environmental Microbiology 2006;72(3) 2064-2069. DOI: 10.1128/AEM.72.3.2064-2069.2006. - 101.
Kock JLF, Botha A, Blerh J, Nigam S. Used cooking oil: science tackles a potential health hazard. South African Journal of Science 1996;92(11-12) 513–514. - 102.
Haba E, Espuny MJ, Busquets M, Manresa A. Screening and production of rhamnolipids by Pseudomonas aeruginosa 47T2 NCIB 40044 from waste frying oils. Journal of Applied Microbiology 2000;88(3) 379-387. DOI: 10.1046/j.1365-2672.2000.00961.x. - 103.
Makkar RS, Cameotra SS. An update on the use of unconventional substrates for biosurfactant production and their new applications. Applied Microbiology and Biotechnology 2002;58(4) 428-434. DOI: 10.1007/s00253-001-0924-1. - 104.
Nitschke M, Costa SG, Haddad R, Gonçalves LA, Eberlin MN, Contiero J. Oil wastes as unconventional substrates for rhamnolipid biosurfactant production by Pseudomonas aeruginosa LBI. Biotechnology Progress 2005;21(5) 1562-1566. DOI: 10.1021/bp050198x. - 105.
Thavasi R, Subramanyam Nambaru VRM, Jayalakshmi S, Balasubramanian T, Banat IM. Biosurfactant production by Pseudomonas aeruginosa from renewable resources. Indian Journal of Microbiology 2011;51(1) 30-36. DOI: 10.1007/s12088-011-0076-7. - 106.
Venkatesh NM, Vedaraman N. Remediation of soil contaminated with copper using rhamnolipids produced from Pseudomonas aeruginosa MTCC 2297 using waste frying rice bran oil. Annals of Microbiology 2012;62(1) 85-91. DOI: 10.1007/s13213-011-0230-9. - 107.
Babu PS, Vaidya AN, Bal AS, Kapur R, Juwarkar A, Khanna P. Kinetics of biosurfactant production by Pseudomonas aeruginosa strain BS2 from industrial wastes. Biotechnology Letters 1996;18(3) 263-268. DOI: 10.1007/BF00142942. - 108.
George S, Jayachandran K. Production and characterization of rhamnolipid biosurfactant from waste frying coconut oil using a novel Pseudomonas aeruginosa D. Journal of Applied Microbiology 2013;114(2) 373-383. DOI: 10.1111/jam.12069. - 109.
Colak AK, Kahraman H. The use of raw cheese whey and olive oil mill wastewater for rhamnolipid production by recombinant Pseudomonas aeruginosa. Environmental and Experimental Biology 2013;11(3) 125-130. - 110.
Rashedi H, Assadi MM, Bonakdarpour B, Jamshidi E. Environmental importance of rhamnolipid production from molasses as a carbon source. Internation Journal of Environmental Science and Technology 2005;2(1) 59-62. DOI: 10.1007/BF03325858. - 111.
Costa SG, Lépine F, Milot S, Déziel E, Nitschke M, Contiero J. Cassava wastewater as a substrate for the simultaneous production of rhamnolipids and polyhydroxyalkanoates by Pseudomonas aeruginosa. Journal of Industrial Microbiology and Biotechnology 2009;36(8) 1063-1072. DOI: 10.1007/s10295-009-0590-3. - 112.
Fernández D, Rodríguez E, Bassas M, Viñas M, Solanas AM, Llorens J, Marqués AM, Manresa A. Agro-industrial oily wastes as substrates for PHA production by the new strain Pseudomonas aeruginosa NCIB 40045: Effect of culture conditions. Biochemical Engineering Journal 2005;26(2) 159-167. DOI: 10.1016/j.bej.2005.04.022. - 113.
Phukon P, Phukan MM, Phukan S, Konwa BK. Polyhydroxyalkanoate production by indigenously isolated Pseudomonas aeruginosa using glycerol by-product of KCDL biodiesel as an inexpensive carbon source. Annals of Microbiology 2014;64(4) 1567-1574. DOI 10.1007/s13213-014-0800-8. - 114.
Füchtenbusch B, Wullbrandt D, Steinbüchel A. Production of polyhydroxyalkanoic acids by Ralstonia eutropha and Pseudomonas oleovorans from an oil remaining from biotechnological rhamnose production. Applied Microbiology and Biotechnology 2000;53(2) 167-172. DOI: 10.1007/s002530050004. - 115.
Ribera RG, Monteoliva-Sanchez M, Ramos-Cormenzana A. Production of polyhydroxyalkanoates by Pseudomonas putida KT2442 harboring pSK2665 in wastewater from olive oil mills (alpechín). Electronic Journal of Biotechnology 2001;4(2) 116-119. - 116.
Sajjan S, Purification and physiochemical characterization of melanin pigment from Klebsiella sp. GSK. Journal of Microbiology and Biotechnology 2010;20(11) 1513-1520. - 117.
Geng J, Yuan P, Shao C, Yu SB, Zhou B, Zhou P, Chen XD. Bacterial melanin interacts with double-stranded DNA with high affinity and may inhibit cell metabolism in vivo. Archives of Microbiology 2010;192(5) 321-329. DOI: 10.1007/s00203-010-0560-1. - 118.
Tarangini K, Mishra S. Production, characterization and analysis of melanin from isolated marine Pseudomonas sp. using vegetable waste. Research Journal of Engineering Sciences 2013;2(5) 40-46. - 119.
Dayanandan A, Kanagaraj J, Sounderraj L, Govindaraju R., Rajkumar GS. Application of an alkaline protease in leather processing: an ecofriendly approach. Journal of Cleaner Production 2003;11(5) 533-536. DOI: 10.1016/S0959-6526(02)00056-2. - 120.
Kumar AG, Swarnalatha S, Sairam B, Sekaran G. Production of alkaline protease by Pseudomonas aeruginosa using proteinaceous solid waste generated from leather manufacturing industries. Bioresource Technology 2008;99(6) 1939-1944. DOI: 10.1016/j.biortech.2007.03.025. - 121.
Jellouli K, Bayoudh A, Manni L, Agrebi R, Nasri M. Purification, biochemical and molecular characterization of a metalloprotease from Pseudomonas aeruginosa MN7 grown on shrimp wastes. Applied Microbiology and Biotechnology 2008;79(6) 989-999. DOI: 10.1007/s00253-008-1517-z. - 122.
Wang SL, Chen SJ, Wang CL. Purification and characterization of chitinases and chitosanases from a new species strain Pseudomonas sp. TKU015 using shrimp shells as a substrate. Carbohydrate Research 2008;19;343(7) 1171-1179. DOI: 10.1016/j.carres.2008.03.018. - 123.
Cervantes-González E, Rojas-Avelizapa NG, Cruz-Camarillo R, García-Mena J, Rojas-Avelizapa LI. Oil-removal enhancement in media with keratinous or chitinous wastes by hydrocarbon-degrading bacteria isolated from oil-polluted soils. Environmental Technology 2008;29(2) 171-182. DOI: 10.1080/09593330802028659. - 124.
Poorni KE, Manikandan A, Geethanjali S, Percy PK. Production of Pseudomonas fluorescence from agricultural wastes and its application in the preservation of selected vegetables. Advances in Applied Science Research 2011;2(2) 156-160. - 125.
Sepperumal U, Selvanayagam S, Markandan M. Utilization of toner waste black powder for bacterial growth. Journal of Microbiology and Biotechnology Research 2014;4(1) 28-30. - 126.
Zhong W, Zhu C, Shu M, Sun K, Zhao L, Wanga C, Ye Z, Chen J. Degradation of nicotine in tobacco waste extract by newly isolated Pseudomonas sp. ZUTSKD. Bioresource Technology 2010;101(18) 6935-6941. DOI: 10.1016/j.biortech.2010.03.142. - 127.
Jørgensen F, Bally M, Chapon-Herve V, Michel G, Lazdunski A, Williams P, Stewart GS. RpoS-dependent stress tolerance in Pseudomonas aeruginosa. Microbiology 1999;145(Pt 4) 835-844. DOI: 10.1099/13500872-145-4-835. - 128.
Murakami K, Ono T, Viducic D, Kayama S, Mori M, Hirota K, Nemoto K, Miyake Y. Role for rpoS gene of Pseudomonas aeruginosa in antibiotic tolerance. FEMS Microbiology Letters 2005;242(1) 161-167. DOI: 10.1016/j.femsle.2004.11.005. - 129.
Martin DW, Schurr MJ, Yu H, Deretic V. Analysis of promoters controlled by the putative sigma factor AlgU regulating conversion to mucoidy in Pseudomonas aeruginosa: relationship to σE and stress response. Journal of Bacteriology 1994;176(21) 6688-6696. - 130.
Keith LMW, Bender CL. AlgT (σ22) controls alginate production and tolerance to environmental stress in Pseudomonas syringae. Journal of Bacteriology 1999;181(23) 7176-7184. - 131.
Schurr MJ, Deretic V. Microbial pathogenesis in cystic fibrosis: co-ordinate regulation of heat-shock response and conversion to mucoidy in Pseudomonas aeruginosa. Molecular Microbiology 1997;24(2) 411-420. DOI: 10.1046/j.1365-2958.1997.3411711.x. - 132.
Schurr MJ, Yu H, Boucher JC, Hibler NS, Deretic V. Multiple promoters and induction by heat shock of the gene encoding the alternative sigma factor AlgU (σE) which controls mucoidy in cystic fibrosis isolates of Pseudomonas aeruginosa. Journal of Bacteriology 1995;177(19) 5670-5679. - 133.
Yu H, Schurr MJ, Deretic V. Functional equivalence of Escherichia coli σE and Pseudomonas aeruginosa AlgU: E. coli rpoE restores mucoidy and reduces sensitivity to reactive oxygen intermediates in algU mutants of P. aeruginosa. Journal of Bacteriology 1995;177(11) 3259-3268. - 134.
Schnider-Keel U, Lejbølle KB, Baehler E, Haas D, Keel C. The sigma factor AlgU (AlgT) controls exopolysaccharide production and tolerance towards desiccation and osmotic stress in the biocontrol agent Pseudomonas fluorescens CHA0. Applied and Environmental Microbiology 2001;67(12) 5683-5693. DOI: 10.1128/AEM.67.12.5683-5693.2001. - 135.
Govan J, Deretic V. Microbial pathogenesis in cystic fibrosis: mucoid Pseudomonas aeruginosa and Burkholderia cepacia. Microbiological Reviews 1996;60(3) 539-574. - 136.
Mathee K, McPherson CJ, Ohman DE. Posttranslational control of the algT (algU)-encoded sigma22 for expression of the alginate regulon in Pseudomonas aeruginosa and localization of its antagonist proteins MucA and MucB (AlgN). Journal of Bacteriology 1997;179(11) 3711-3720. - 137.
Pham TH, Webb JS, Rehm BHA. The role of polyhydroxyalkanoate biosynthesis by Pseudomonas aeruginosa in rhamnolipid and alginate production as well as stress tolerance and biofilm formation. Microbiology 2004;150(10) 3405-3413. DOI: 10.1099/mic.0.27357-0. - 138.
Gentry DR, Hernandez VJ, Nguyen LH, Jensen DB, Cashel M. Synthesis of the stationary-phase sigma factor σs is positively regulated by ppGpp. Journal of Bacteriology 1993;175(24) 7982-7989. - 139.
Rangeshwaran R, Ashwitha K, Sivakumar G, Jalali SK. Analysis of proteins expressed by an abiotic stress tolerant Pseudomonas putida (NBAII-RPF9) isolate under saline and high temperature conditions. Current Microbiology 2013;67(6) 659-667. DOI: 10.1007/s00284-013-0416-4. - 140.
Aspedon A, Palmer K, Whiteley M. Microarray analysis of the osmotic stress response in Pseudomonas aeruginosa. Journal of Bacteriology 2006;188(7) 2721-2725. DOI: 10.1128/JB.188.7.2721-2725.2006. - 141.
Frank DW. The exoenzyme S regulon of Pseudomonas aeruginosa. Molecular Microbiology 1997;26(4) 621-629. DOI: 10.1046/j.1365-2958.1997.6251991.x. - 142.
Hueck CJ. Type III protein secretion systems in bacterial pathogens of animals and plants. Microbiology and Molecular Biology Reviews 1998;62(2) 379-433. - 143.
D'Souza-Ault MR, Smith LT, Smith GM. Roles of N-acetylglutaminylglutamine amide and glycine betaine in adaptation of Pseudomonas aeruginosa to osmotic stress. Applied and Environmental Microbiology 1993;59(2) 473-478. - 144.
Sardessai Y, Bhosle S. Tolerance of bacteria to organic solvents. Research in Microbiology 2002;153(5) 263-268. DOI: 10.1016/S0923-2508(02)01319-0. - 145.
Teitzel GM, Parsek MR. Heavy metal resistance of biofilm and planktonic Pseudomonas aeruginosa. Applied and Environmental Microbiology 2003;69(4) 2313-2320. DOI: 10.1128/AEM.69.4.2313-2320.2003. - 146.
Boopathy NR, Indhuja D, Srinivasan K, Uthirappan M, Gupta R, Ramudu KN, Chellan R. Statistical medium optimization of an alkaline protease from Pseudomonas aeruginosa MTCC 10501, its characterization and application in leather processing. Indian Journal of Experimental Biology 2013;51(4) 336-342. - 147.
Kojima Y, Sakuradani E, Shimizu S. Different specificities of two types of Pseudomonas lipases for C20 fatty acids with a Δ5 unsaturated double bond and their application for selective concentration of fatty acids. Journal of Bioscience and Bioengineering 2006;101(6) 490-500. DOI: 10.1263/jbb.101.496. - 148.
Cheirsilp B, Jeamjounkhaw P, Kittikun AH. Optimizing an alginate immobilized lipase for monoacylglycerol production by the glycerolysis reaction. Journal of Molecular Catalysis B: Enzymatic 2009;59(1-3) 206-211. DOI: 10.1016/j.molcatb.2009.03.001. - 149.
Zhang A, Gao R, Diao N, Xie G, Gao G, Cao S. Cloning, expression and characterization of an organic solvent tolerant lipase from Pseudomonas fluorescens JCM5963. Journal of Molecular Catalysis B: Enzymatic 2009;56(2-3) 78-84. DOI: 10.1016/j.molcatb.2008.06.021. - 150.
Priya K, Chadha A. Synthesis of hydrocinnamic esters by Pseudomonas cepacia lipase. Enzyme and Microbial Technology 2003;32(3-4) 885-890. DOI: 10.1016/S0141-0229(02)00340-X. - 151.
Li Q, Yan Y. Production of biodiesel catalyzed by immobilized Pseudomonas cepacia lipase from Sapium sebiferum oil in micro-aqueous phase. Applied Energy 2008;87(10) 3148-3154. DOI: 03/13/201510.1016/j.apenergy.2010.02.032. - 152.
Vandana P, Peter JK. Application of partially purified laccases from Pseudomonas fluorescens on dye decolourization. International Journal of Advanced Technology in Engineering and Science 2014;2(8) 317-327. - 153.
Kumar V, Singh S, Manhas A, Singh J, Singla S, Kaur P, Data S, Negi P, Kalia A. Bioremediation of petroleum hydrocarbon by using Pseudomonas species isolated from petroleum contaminated soil. Oriental Journal of Chemistry 2014;30(4) 1771-1776. - 154.
Sathiya-Moorthi P, Deecaraman M, Kalaichelvan PT. Bioremediation of automobile oil effluent by Pseudomonas sp. Advanced Biotech 2008;31 34-37. - 155.
Roy AS, Yenn R, Singh AK, Boruah HPD, Saikia N, Deka M. Bioremediation of crude oil contaminated tea plantation soil using two Pseudomonas aeruginosa strains AS 03 and NA 108. African Journal of Biotechnology 2013;12(19) 2600-2610. DOI: 10.5897/AJB12.170 - 156.
Baltazar M, Gracioso L, Avanzi I, Veiga M, Gimenes L, Nascimento C, Perpetuo E. Bioremediation potential of Pseudomonas aeruginosa and Enterobacter cloacae isolated from a copper-contaminated area. BMC Proceedings 2014;8(Suppl 4) P188. DOI: 10.1186/1753-6561-8-S4-P188. - 157.
Ali Khan MW, Ahmad M. Detoxification and bioremediation potential of a Pseudomonas fluorescens isolate against the major Indian water pollutants. Journal of Environmental Science and Health, Part A: Toxic/Hazardous Substances and Environmental Engineering 2006;41(4) 659-674. DOI: 10.1080/10934520600575051. - 158.
Singh R, Bishnoi NR, Kirrolia A. Evaluation of Pseudomonas aeruginosa an innovative bioremediation tool in multi metals ions from simulated system using multi response methodology. Bioresource Technology 2013;138 222-234. DOI: 10.1016/j.biortech.2013.03.100. - 159.
Moorthi PS, Selvam SP, Sasikalaveni A, Murugesan K, Kalaichelvan PT. Decolorization of textile dyes and their effluents using white rot fungi. African Journal of Biotechnology 2007;6(4) 424-429. - 160.
Silveira E, Marques PP, Silva SS, Lima-Filho JL, Porto ALF, Tambourgi EB. Selection of Pseudomonas for industrial textile dyes decolourization. International Biodeterioration and Biodegradation 2009;63(2) 230-235. DOI: 10.1016/j.ibiod.2008.09.007. - 161.
Daneshvar N, Ayazloo M, Khataee AR, Pourhassan M. Biological decolorization of dye solution containing Malachite Green by microalgae Cosmarium sp. Bioresource Technology 2007;98(6) 1176-1182. DOI: 10.1016/j.biortech.2006.05.025. - 162.
Shah MP, Patel KA, Nair SS, Darji AM. Microbial decolourization of methyl orange dye by Pseudomonas spp. OA Biotechnology 2013;2(1) 10. - 163.
Joe J, Kothari RK, Raval CM, Kothari CR, Akbari VG, Singh SP. Decolorization of textile dye Remazol Black B by Pseudomonas aeruginosa CR-25 isolated from the common effluent treatment plant. Journal of Bioremediation and Biodegradation 2011;2 118. DOI: 10.4172/2155-6199.1000118. - 164.
Wu J, Jung BG, Kim KS, Lee YC, Sung NC. Isolation and characterization of Pseudomonas otitidis WL-13 and its capacity to decolorize triphenylmethane dyes. Journal of Environmental Sciences 2009;21(7) 960-964. DOI: 10.1016/S1001-0742(08)62368-2. - 165.
Chen JP, Lin YS. Decolorization of azo dye by immobilized Pseudomonas luteola entrapped in alginate–silicate sol–gel beads. Process Biochemistry 2007;42(6) 934-942. DOI: 10.1016/j.procbio.2007.03.001. - 166.
Işik M, Sponza DT. Effect of oxygen on decolorization of azo dyes by Escherichia coli and Pseudomonas sp. and fate of aromatic amines. Process Biochemistry 2003;38(8) 1183-1192. DOI: 10.1016/S0032-9592(02)00282-0. - 167.
Chang JS, Chou C, Lin YC, Lin PJ, Ho JY, Hu TL. Kinetic characteristics of bacterial azo-dye decolorization by Pseudomonas luteola. Water Research 2001;35(12) 2841-2850. DOI: 10.1016/S0043-1354(00)00581-9. - 168.
Voisard C, Keel C, Haas D, Dèfago G. Cyanide production by Pseudomonas fluorescens helps suppress black root rot of tobacco under gnotobiotic conditions. The EMBO Journal 1989 Feb;8(2) 351-358. - 169.
Nandakumar R, Babu S, Viswanathan R, Raguchander T, Samiyappan R. Induction of systemic resistance in rice against sheath blight disease by Pseudomonas fluorescens. Soil Biology and Biochemistry 2001;33(4-5) 603-612. DOI: 10.1016/S0038-0717(00)00202-9. - 170.
Samavat S, Heydari A, Zamanizadeh HR, Rezaee S, Aliabadi AA. Application of new bioformulations of Pseudomonas aureofaciens for biocontrol of cotton seedling damping-off. Journal of Plant Protection Research 2014;54(4) 334-339. DOI: 10.2478/jppr-2014-0050. - 171.
Khan MR, Haque Z. Soil application of Pseudomonas fluorescens and Trichoderma harzianum reduces root-knot nematode, Meloidogyne incognita, on tobacco. Phytopathologia Mediterranea 2011;50(2) 257-266. DOI: 10.14601/Phytopathol_Mediterr-9252. - 172.
Vanitha S, Ramjegathesh R. Bio control potential of Pseudomonas fluorescens against coleus root rot disease. Journal of Plant Pathology and Microbiology 2014;5(1) 1-4. DOI: 10.4172/2157-7471.1000216. - 173.
Heil M, Bostock RM. Induced systemic resistance (ISR) against pathogens in the context of induced plant defences. Annals of Botany 2002:89(5) 503-512. DOI: 10.1093/aob/mcf076.