Bioremediation of Simulated Textile Effluent by an Efficient Bio-catalyst Purified from a Novel Pseudomonas fluorescence LiP-RL5

Page: [128 - 139] Pages: 12

  • * (Excluding Mailing and Handling)

Abstract

Background: Microbial degradation of highly stable textile dyes, using lignin peroxidase, is an eco-friendly, less expensive and much advantageous in comparison to the chemical method.

Objective: Biodegradation potential of lignin peroxidase (LiP), from Pseudomonas fluorescens LiP-RL5, was enhanced after optimization and purification so as to use it as a potential bioresource for the treatment of textile effluent.

Methods: LiP producing bacterial isolate was primarily screened by methylene blue assay followed by LiP assay. The standard protocol was used for purification of lignin peroxidase and purified LiP was finally used for degradation of textile dyes.

Results: 57 bacterial isolates were screened for lignin peroxidase activity. Isolate LiP-RL5 showed maximum activity (19.8 ±0.33 %) in terms of methylene blue reduction in comparison to others. Biochemical and molecular characterization of LiP-RL5 showed 99 % similarity with P. fluorescens. Lignin peroxidase activity was increased by 50 % after optimization of cultural conditions. Maximum enhancement in the activity was achieved when peptone was used as a nitrogen source. LiP from P. fluorescens LiP-RL5 was further purified up to 2 folds. SDS-PAGE analysis revealed a single protein band of approximately 40 kDa. Enzyme also showed high catalytic efficiency with Km= 6.94 mM and Vmax= 78.74 μmol/ml/min. Purified enzyme was able to decolorize the simulated textile effluent up to 45.05 ±0.28 % after 40 minutes.

Conclusion: High catalytic efficiency of purified LiP from P. fluorescens LiP-RL5 suggests its utility as a potential candidate for biodegradation of toxic dyes in the industrial effluent, which could be successfully utilized for wastewater treatment at commercial level.

Keywords: Bioremediation, P. fluorescens, lignin peroxidase, methylene blue, decolorization, textile effluent.

Graphical Abstract

[1]
Bridge G, Watson S. The Blackwell City Reader. John Wiley & Sons 2010; pp. 75-6.
[2]
Brinzila CI, Ciobanu R, Brillas E. Effect of experimental parameters on crystal violet mineralization by electro-fenton process. Environ Eng Manag J 2011; 1: 11.
[3]
Azizi A, Moghaddam MRA, Arami M. Application of wood waste for removal of reactive blue 19 from aqueous solutions: optimization through response surface methodology. Environ Eng Manag J 2012; 11: 795-804.
[http://dx.doi.org/10.30638/eemj.2012.102]
[4]
Zucca P, Rescigno A, Pintus M, Rinaldi AC, Sanjust E. Degradation of textile dyes using immobilized lignin peroxidase-like metalloporphines under mild experimental conditions. Chem Cent J 2012; 6(1): 161.
[http://dx.doi.org/10.1186/1752-153X-6-161] [PMID: 23256784]
[5]
Shah V, Garg N, Madamwar D. Exopolysaccharides production by a marine Cyanobacterium cyanothece sp. and its application in dye removal by its gelation phenomenon. Appl Biochem Biotechnol 1999; 82: 81-90.
[http://dx.doi.org/10.1385/ABAB:82:2:81]
[6]
Verma P, Madamwar D. Decolorization of synthetic textile dyes by lignin peroxidase of Phanerochaete chrysosporium. Folia Microbiol (Praha) 2002; 47(3): 283-6.
[http://dx.doi.org/10.1007/BF02817653] [PMID: 12094739]
[7]
Da Silva CG, Faria JL. Photochemical and photocatalytic degradation of an azo dye in aqueous solution by UV irradiation. J Photochem Photobiol Chem 2003; 155: 133-43.
[http://dx.doi.org/10.1016/S1010-6030(02)00374-X]
[8]
Ecker J, Fülöp L. Lignin peroxidase ligand access channel dysfunction in the presence of atrazine. Sci Rep 2018; 8(1): 5989.
[http://dx.doi.org/10.1038/s41598-018-24478-w] [PMID: 29662099]
[9]
Katoon N, Jamal A, Ali MI. Lignin peroxidase isoenzyme: A novel approach to biodegrade the toxic synthetic polymer waste. Environ Technol 2019; 40(11): 1366-75.
[http://dx.doi.org/10.1080/09593330.2017.1422550] [PMID: 29291675]
[10]
Kalyani DC, Patil PS, Jadhav JP, Govindwar SP. Biodegradation of reactive textile dye Red BLI by an isolated bacterium Pseudomonas sp. SUK1. Bioresour Technol 2008; 99(11): 4635-41.
[http://dx.doi.org/10.1016/j.biortech.2007.06.058] [PMID: 17765541]
[11]
Alam MZ, Mansor MF, Jalal KC. Optimization of lignin peroxidase production and stability by Phanerochaete chrysosporium using sewage-treatment-plant sludge as substrate in a stirred-tank bioreactor. J Ind Microbiol Biotechnol 2009; 36(5): 757-64.
[http://dx.doi.org/10.1007/s10295-009-0548-5] [PMID: 19259713]
[12]
Patil SR. Production and purification of lignin peroxidase from Bacillus megaterium and its application in bioremidation. J Microbiol 2014; 2: 22-8.
[13]
Sasidhara R, Thirunalasundar T. Lignolytic and lignocellulosic enzymes of Ganoderma lucidum in 999liquid medium. Eur J Exp Biol 2014; 4: 375-9.
[14]
Yang C, Yue F, Cui Y, et al. Biodegradation of lignin by Pseudomonas sp. Q18 and the characterization of a novel bacterial DyP-type peroxidase. J Ind Microbiol Biotechnol 2018; 45(10): 913-27.
[http://dx.doi.org/10.1007/s10295-018-2064-y] [PMID: 30051274]
[15]
Shamseldin A, Ahmed AA. Isolation and identification of newly effective bacterial strains exhibiting great ability of lignin and Rice straw biodegradation. Int J Curr Microbiol Appl Sci 2015; 4: 1039-49.
[16]
Singh P, Jain P, Verma R, Jagdish RS. Characterization of lignin peroxidase from Paecilomy species for depolarization of paper and pulp mill effluent. J Sci Ind Res (India) 2016; 75: 500-5.
[17]
Falade AO, Nwodo UU, Iweriebor BC, Green E, Mabinya LV, Okoh AI. Lignin peroxidase functionalities and prospective applications. MicrobiologyOpen 2017; 6(1)
[http://dx.doi.org/10.1002/mbo3.394] [PMID: 27605423]
[18]
Catcheside DE, Ralph JP. Biological processing of coal. Appl Microbiol Biotechnol 1999; 53: 16-24.
[http://dx.doi.org/10.1007/s002530051482]
[19]
Salvachúa D, Prieto A, Mattinen ML, et al. Versatile peroxidase as a valuable tool for generating new biomolecules by homogeneous and heterogeneous cross-linking. Enzyme Microb Technol 2013; 52(6-7): 303-11.
[http://dx.doi.org/10.1016/j.enzmictec.2013.03.010] [PMID: 23608497]
[20]
Magalhaes DB. Carvalho MEAde, Bon E, Neto JSA, Kling SH. Colorimetric assay for lignin peroxidase activity determination using methylene blue as substrate. Biotechnol Tech 1996; 10: 273-6.
[http://dx.doi.org/10.1007/BF00184028]
[21]
Sharma JM, Yadava M, Singh NP, Yadav KD. Purification and characterization of Lignin Peroxidase from Pycnoporus sanguineus MTCC- 1371. Appl Biochem Microbiol 2011; 47: 532-53.
[http://dx.doi.org/10.1134/S0003683811050139]
[22]
Saratale RG, Saratele DG, Chang JS, Govindwar SP. Bacterial decolorization and degradation of azo dyes: A review. Journal of Taiwan Institute Chemical Engneers 2011; 42: 138-57.
[http://dx.doi.org/10.1016/j.jtice.2010.06.006]
[23]
Kersten P, Cullen D. Copper radical oxidases and related extracellular oxidoreductases of wood-decay Agaricomycetes. Fungal Genet Biol 2014; 72: 124-30.
[http://dx.doi.org/10.1016/j.fgb.2014.05.011] [PMID: 24915038]
[24]
Abraham KG. Extraction of lignin peroxidase enzyme from bacteria isolated from the mangrove wood. Indian Journal of Research 2016; 5: 7-9.
[25]
Crawford DL, Muralidhara R. Bacterial extracellular lignin peroxidase United States Patent 5200338 2004.
[26]
Loncar N, Draskovi N, Bozi N, et al. Catalysts 2019; 9: 463.
[http://dx.doi.org/10.3390/catal9050463]
[27]
Sasikumar V, Priya V, Shiv CS, Sathish DS. Isolation and preliminary screening of lignin degrading microbes. Journal of Academic & Industrial Research 2014; 3: 291-4.
[28]
Bansal N, Kanwar SS. Peroxidase(s) in environment protection. ScientificWorldJournal 2013.2013714639
[http://dx.doi.org/10.1155/2013/714639] [PMID: 24453894]
[29]
Woo HL, Hazen TC, Simmons BA, DeAngelis KM. Enzyme activities of aerobic lignocellulolytic bacteria isolated from wet tropical forest soils. Syst Appl Microbiol 2014; 37(1): 60-7.
[http://dx.doi.org/10.1016/j.syapm.2013.10.001] [PMID: 24238986]
[30]
Yadav M, Singh SK, Yadav KS, Singh KD. Purification of lignin peroxidase from Hexagona tenuis MTCC-1119 and its kinetic properties in aqueous medium containing miscible organic solvent. Indian J Chem 2010; 49: 487-98.
[31]
Yadav M, Yadav HS. Applications of ligninolytic enzymes to pollutants, wastewater, dyes, soil, coal, paper and polymers. Environ Chem Lett 2015; 13: 309-18.
[http://dx.doi.org/10.1007/s10311-015-0516-4]
[32]
Mikiashivili N, Wasser SP, Nevo E, Elisashivili V. Effect of carbon and nitrogen sources on Pleurotus ostreatus ligninlytic enzyme activity. World J Microbiol Biotechnol 2006; 22: 999-1002.
[http://dx.doi.org/10.1007/s11274-006-9132-6]
[33]
Gottschalk LM, Macedo JM, Bon EP. Lignin peroxidase production by Streptomyces viridosporus T7A: use of corn oil as a carbon source. Appl Biochem Biotechnol 1999; 77-79: 771-8.
[http://dx.doi.org/10.1385/ABAB:79:1-3:771] [PMID: 15304696]
[34]
Kheiralla ZH, Badr El-Din MS, Saad MA, Douaa HA. Optimization of cultural conditions for lignin peroxidase production by Phanerochaete chrysosporium and Pleurotus ostreatus Academic Journal of Biotechnology 2013; 1087.
[35]
Bandounas L, Wierckx NJ, de Winde JH, Ruijssenaars HJ. Isolation and characterization of novel bacterial strains exhibiting ligninolytic potential. BMC Biotechnol 2011; 11: 94.
[http://dx.doi.org/10.1186/1472-6750-11-94] [PMID: 21995752]
[36]
Rodríguez Couto S, Toca Herrera JL. Industrial and biotechnological applications of laccases: a review. Biotechnol Adv 2006; 24(5): 500-13.
[http://dx.doi.org/10.1016/j.biotechadv.2006.04.003] [PMID: 16716556]
[37]
Sivakami V, Ramachandran B, Srivathsan J, Kesavaperumal G, Smily B, Kumar DM. Production and optimization of laccase and lignin peroxidase by newly isolated Pleurotus ostreatus LIG 19. Journal of Microbiology & Biotechnology Research 2012; 2: 875-81.
[38]
Tuncer G, Tekkaya C, Sungur S, Cakiroglu J, Ertepinar H, Kaplowitz M. Assessing pre-service teachers’ environmental literacy in Turkey as a mean to develop teacher education programs. Int J Educ Dev 2009; 29: 426-36.
[http://dx.doi.org/10.1016/j.ijedudev.2008.10.003]
[39]
Hariharan S, Nambisan P. Optimization of lignin peroxidase, and lac production from Ganoderma lucidum under solid state fermentation of pineapple leaf. Bioresource 2013; 8: 250-71.
[40]
Osma JF, Toca-Herrera JL, Rodriguez-couto S. Biodegradation of a simulated textile effluent by immobilised-coated laccase in laboratory-scale reactors. Appl Catal A Gen 2010; 373: 147-53.
[http://dx.doi.org/10.1016/j.apcata.2009.11.009]