Abstract
A strict aerobic Acinetobacter baumannii YNWH 226, isolated from an activated sludge reactor treating textile wastewater, was able to grow on Congo red as the sole carbon source under aerobic conditions. The decolorization and TOC reduction efficiency were 99.1 and 93.72%, respectively. The effects of the Congo red concentration were studied. The environmental factors (i.e., pH, temperature and agitation speed) on the biodegradation of Congo red in aqueous phase were studied and evaluated using response surface methodology. The results indicated that when the Congo red concentration was 100 mg/L, the optimal decolorization conditions were as follows: 37°C, pH 7.0 and 180 rpm. The single A. baumannii YNWH 226 was able to form aromatic amines by reductive breakage of the azo bond and then oxidize them into non-toxic metabolites.
Similar content being viewed by others
References
Van der Zee, F. P., I. A. E. Bisschops, V. G. Blanchard, R. H. M. Bouwman, G. Lettinga, and J. A. Field (2003) The contribution of biotic and abiotic processes during azo dye reduction in anaerobic sludge. Water Res. 37: 3098–3109.
Elisangela, F., Z. Andrea, D. G. Fabio, R. de Menezes Cristiano, D. L. Regina, and C. P. Artur (2009) Biodegradation of textile azo dyes by a facultative Staphylococcus arlettae strain VN-11 using a sequential microaerophilic/aerobic process. Internat. Biodeter. Biodegrad. 63: 280–288.
Amar, T., K. Dayanand, J. Jyoti and G. Sanjay (2008) Kinetics and mechanism of Reactive red 141 degradation by a bacterial isolate Rhizobium radiobacter MTCC 8161. Acta Chim. Sloven ica. 55: 320–329.
Saratale, R. G., G. D. Saratale, J. S. Chang, and S. P. Govindwar (2011) Bacterial decolorization and degradation of azo dyes: A review. J. Taiwan Institute Chem. Eng. 42: 138–157.
Ayed, L., A. Mahdhi, A. Cheref, and A. Bakhrouf (2011) Decolorization and degradation of azo dye Methyl Red by an isolated Sphingomonas paucimobilis: Biotoxicity and metabolites characterization. Desalinat. 274: 272–277.
Zu, L., G. Li, J. An, J. Li, and T. An (2013) Kinetic optimization of biodegradation and debromination of 2,4,6-tribromophenol using response surface methodology. Internat. Biodeter. Biodegrad. 76: 18–23.
Bhattacharya, S. S. and R. Banerjee (2008) Laccase mediated biodegradation of 2,4-dichlorophenol using response surface methodology. Chemosphere 73: 81–85.
Ghosal, D., A. Dutta, J. Chakraborty, S. Basu, and T. K. Dutta (2013) Characterization of the metabolic pathway involved in assimilation of acenaphthene in Acinetobacter sp. strain AGATW. Res. Microbiol. 164: 155–163.
Lade, H. S., T. R. Waghmode, A. A. Kadam, and S. P. Govindwar (2012) Enhanced biodegradation and detoxification of disperse azo dye Rubine GFL and textile industry effluent by defined fungalbacterial consortium. Internat. Biodeter. Biodegrad. 72: 94–107.
Fernando, E., T. Keshavarz, and G. Kyazze (2012) Enhanced biodecolourisation of acid orange 7 by Shewanella oneidensis through co-metabolism in a microbial fuel cell. Internat. Biodeter. Biodegrad. 72: 1–9.
Selvam, K., K. Swaminathan, and K.-S. Chae (2003) Decolourization of azo dyes and a dye industry effluent by a white rot fungus Thelephora sp.. Bioresour. Technol. 88: 115–119.
McMullan, G., C. Meehan, A. Conneely, N. Kirby, T. Robinson, P. Nigam, I. M. Banat, R. Marchant, and W. F. Smyth (2001) Microbial decolourisation and degradation of textile dyes. Appl. Microbiol. Biotechnol. 56: 81–87.
Lin, J., X. Zhang, Z. Li, and L. Lei (2010) Biodegradation of Reactive blue 13 in a two-stage anaerobic/aerobic fluidized beds system with a Pseudomonas sp. isolate. Bioresour. Technol. 101: 34–40.
Sarayu, K. and S. Sandhya (2009) Aerobic biodegradation pathway for remazol orange by Pseudomonas aeruginosa. Appl. Biochem. Biotechnol. 160: 1241–1253.
Valli Nachiyar, C. and G. Suseela Rajakumar (2005) Purification and characterization of an oxygen insensitive azoreductase from Pseudomonas aeruginosa. Enz. Microbial. Technol. 36: 503–509.
Ooi, T., T. Shibata, R. Sato, H. Ohno, S. Kinoshita, T. L. Thuoc, and S. Taguchi (2007) An azoreductase, aerobic NADH-dependent flavoprotein discovered from Bacillus sp.: Functional expression and enzymatic characterization. Appl. Microbiol. Biotechnol. 75: 377–386.
Chen, H., R.-F. Wang, and C. E. Cerniglia (2004) Molecular cloning, overexpression, purification, and characterization of an aerobic FMN-dependent azoreductase from Enterococcus faecalis. Protein Exp. Purif. 34: 302–310.
Nakanishi, M. (2001) Putative ACP phosphodiesterase gene (acpD) encodes an azoreductase. J. Biol. Chem. 276: 46394–46399.
Azadeh, T., I. Mina, and H. Kerdari (2013) Adsorption kinetics, thermodynamic studies, and high performance of CdO cauliflower- like nanostructure on the removal of Congo red from aqueous solution. J. Nanostruct. Chem. 1: 1–8.
Guz, N., E. Kocak, and N. Kilincer (2013) Molecular phylogeny of Trissolcus species (Hymenoptera: Scelionidae). Biochem. Syst. Ecol. 48: 85–91.
Saitou, N. and M. Nei (1987) The neighbor joining method a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4: 406–425.
Midolo, P. D., J. Turnidge, J. R. Lambert and J. M. Bell (1995) Validation of a Modified Kirby-Bauer disk diffusion method for metronidazole susceptibility testing of helicobacter pylori. Diagnostic Microbiol. Infect. Disease 21: 135–140.
Chen, B. Y. (2002) Understanding decolorization characteristics of reactive azo dyes by Pseudomonas. Proc. Biochem. 38: 437–446.
Box, G. E. P. and D. W. Behnken (1960) Some new three level designs for the study of quantitative variables. Technomet. 2: 455–475.
Hinkelmann, K. and O. Kempthorne (2007) Design and analysis of experiments. 2nd ed., pp. 29–58. John Wiley & Sons, Inc., Hoboken, NJ, USA.
Kim, J., K. J. Cho, G. Han, C. Lee, and S. Hwang (2013) Effects of temperature and pH on the biokinetic properties of thiocyanate biodegradation under autotrophic conditions. Water Res. 47: 251–258.
Smith, M. G., T. A. Gianoulis, S. Pukatzki, J. J. Mekalanos, L. N. Ornston, M. Gerstein, and M. Snyder (2007) New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis. Genes & Development. 21: 601–614.
Rainey, F. A., E. Lang, and E. Stackebrandt (1994) The phylogenetic structure of the genus Acinetobacter. FEMS Microbilol. 124: 349–354.
Paterson, D. L. (2006) The epidemiological profile of infections with Multidrug-Resistant Pseudomonas aeruginosa and Acinetobacter Species. Clinical Infectious Diseases. 43: 43–48.
Fournier, P. E. and H. Richet (2006) The epidemiology and control of Acinetobacter baumannii in health care facilities. Clin. Infect. Diseases 42: 692–699.
Giamarellou, H., A. Antoniadou, and K. Kanellakopoulou (2008) Acinetobacter baumannii: A universal threat to public health? Internat. J. Antimicrob. Agents. 32: 106–119.
Cao, Y., Y. Hu, J. Sun, and B. Hou (2010) Explore various cosubstrates for simultaneous electricity generation and Congo red degradation in air-cathode single-chamber microbial fuel cell. Bioelectrochem. 79: 71–76.
Chang, J., C. Chou, Y. Lin, P. Lin, J. Ho and T. L. Hu (2001) Kinetic characteristics of bacterial azo-dye decolorization by Pseudomonas luteola. Water Res. 35: 2841–2850.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Ning, Xa., Yang, C., Wang, Y. et al. Decolorization and biodegradation of the azo dye Congo red by an isolated Acinetobacter baumannii YNWH 226. Biotechnol Bioproc E 19, 687–695 (2014). https://doi.org/10.1007/s12257-013-0729-y
Received:
Revised:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s12257-013-0729-y