Ligninase-mediated removal of natural and synthetic estrogens from water: I. Reaction behaviors

Environmental Science and Technology

Volumn 43, Issue 2, 2009, Pages 374-379

  Mao, Liang ^a,b   Huang, Qingguo ^b   Lu, Junhe ^b   Gao, Shixiang ^a  

^a NANJING UNIVERSITY   (China)

^b UNIVERSITY OF GEORGIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHRYSOSPORIUM; ENZYMATIC METHODS; EXTRA-CELLULAR ENZYMES; LIGNIN PEROXIDASE; LIGNINASE; MOLECULAR CHARACTERISTICS; NATURAL ENVIRONMENTS; NATURAL ORGANIC MATTERS; PHANEROCHAETE CHRYSOSPORIUM; REACTION BEHAVIORS; REACTION EFFICIENCIES; REACTION PRODUCTS; SECONDARY METABOLITES; VERATRYL ALCOHOLS; WHITE ROT FUNGUS;

BINDING ENERGY; BINDING SITES; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; METABOLITES; PORPHYRINS;

ENZYMES;

ESTROGEN; HEME; LIGNIN PEROXIDASE; NATURAL ORGANIC MATTER; NATURAL PRODUCT; VERATRYL ALCOHOL; BENZYL ALCOHOL DERIVATIVE; ESTRADIOL; ESTRADIOL DERIVATIVE; ORGANIC COMPOUND; OXYGENASE; PEROXIDASE; WATER;

ENZYME ACTIVITY; ESTROGENIC COMPOUND; EXPERIMENTAL STUDY; FUNGUS; LIGNIN; MASS SPECTROMETRY; WATER TREATMENT;

ARTICLE; BINDING SITE; CHEMICAL REACTION; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME SUBSTRATE; NONHUMAN; PH MEASUREMENT; PHANEROCHAETE; BIOCATALYSIS; BIOREMEDIATION; CHEMISTRY; ISOLATION AND PURIFICATION; KINETICS; METABOLISM; PH; TIME;

FUNGI; PHANEROCHAETE CHRYSOSPORIUM;

BENZYL ALCOHOLS; BINDING SITES; BIOCATALYSIS; BIODEGRADATION, ENVIRONMENTAL; ESTRADIOL; ESTRADIOL CONGENERS; ESTROGENS; HYDROGEN-ION CONCENTRATION; KINETICS; ORGANIC CHEMICALS; OXYGENASES; PEROXIDASES; TIME FACTORS; WATER;

EID: 62749134999     PISSN: 0013936X     EISSN: 15205851     Source Type: Journal    
DOI: 10.1021/es801791v     Document Type: Article

References (32)

1. Colosi, L. M.; Huang, Q.; Weber, W. J. Quantitative structure-activity relationship based quantification of the impacts of enzyme-substrate binding on rates of peroxidase-mediated reactions of estrogenic phenolic chemicals. J. Am. Chem. Soc.2006, 128, 4041-4047.
2. Purdom, C. E.; Hardiman, P. A; Bye, V. J.; Eno, N.C.; Tyler, C. R.; Sumpter, J. P. Estrogenic effects of effluents from sewage treatment works. Chem. Ecol.1994, 8, 275-285.
3. Fan, Z. S.; Casey, F. X. M.; Hakk, H.; Larsen, G. L. Persistence and fate of 17β-estradiol and testosterone in agricultural soils. Chemosphere2007, 67, 886-895.
4. Suzuki, K.; Hirai, H.; Murata, H.; Nishida, T. Removal of estrogenic activities of 17β-estradiol and ethinylestradlol by ligninolytic enzymes from white rot fungi. Water Res.2003, 37, 1972-1975.
5. Auriol, M.; Filali-Meknassi, Y.; Tyagi, R. D.; Adams, C. D. Oxidation of natural and synthetic hormones by the horseradish peroxidase enzyme in wastewater. Chemosphere2007, 68, 1830-1837.
6. Kolpin, D. W.; Furlong, E. T.; Meyer, M. T.; Thurman, E. M.; Zaugg, S. D.; Barber, L. B.; Buxton, H. T. Pharmaceuticals, hormones, and other organic wastewater contaminants in U.S. streams, 1999-2000: a national reconnaissance. Environ. Sci. Technol.2002, 36, 1202-1211.
7. Huang, Q.; Weber, W. J. Transformation and removal of bisphenol A from aqueous phase via peroxidase-mediated oxidative coupling reactions: efficacy, products, and pathways. Environ. Sci. Technol.2005, 39, 6029-6036.
8. Auriol, M.; Filali-Meknassi, Y.; Adams, C. D.; Tyagi, R. D. Laccasecatalyzed conversion ofnatural and synthetic hormones from a municipal wastewater. Water Res.2007, 41, 3281-3288.
9. Nicell, J. A.; Wagner, M. Enzyme treatment of waters and waste. In Chemical Degradation Methods for Wastes and Pollutants: Environmental and Industrial Applications, Tarr, M. A. , Ed.; Marcel Dekker Inc.: New York, NY,2003, pp 423-475.
10. Huang, Q.; Weber, W. Peroxidase-catalyzed coupling of phenol in the presence of model inorganic and organic solid phases. Environ. Sci. Technol.2004, 38, 5238-5245.
11. Colosi, L. M.; Burllngame, D. J.; Huang, Q.; Weber, W. J., Jr. Peroxidase-meidated removal of a polychlorinated biphenyl using natural organic matter as the sole cosubstrate. Environ. Sci. Technol.2007, 41, 891-896.
12. Shah, M. M.; Barr, D. P.; Chung, N.; Aust, S. D. Use of white rot fungi in the degradation of environmental chemicals. Toxicol. Letr.1992, 64/65, 493-501.
13. Tien, M.; Kirk, T. K. Lignin peroxidase of Phanerochaete chrysosporium. Methods Enzymol.1988, 161, 238-249.
14. Poulos, T. L.; Edwards, S. L.; Wariishi, H.; Gold, M. H. Crystallographic refinement of lignin peroxidase at 2 Å. J. Mol. Biol.1993, 268, 4429-4440.
15. Barr, D. P.; Aust, S. D. Conversion of lignin peroxidase compound III to active enzyme by cation radicals. Arch. Biochem. Biophys.1994, 312, 511-515.
16. Gelpke, M. D. S.; Lee, J.; Gold, M. H. Lignin peroxidase oxidation of veratryl alcohol: effects of the mutants H82A, Q222A, W171A, and F267L. Biochemistry2002, 41, 3498-3506.
17. Ward, G.; Hadar, Y.; Dosoretz, C. G. Inactivation of lingnin peroxidase during oxidation of the highly reactive substrate ferulic acid. Enzyme Micro. Tech.2001, 29, 34-41.
18. Nie, G.; Aust, S. D. Spectral changes of lignin peroxidase during reversible Inactivation. Biochemistry1997, 36, 5113-5119.
19. Banci, L.; Ciofl-Baffoni, S.; Tien, M. Lignin and Mn peroxidasecatalyzed oxidation ofphenolic lignin olgomers. Biochemistry1999, 38, 3205-3210.
20. Khindaria, A.; Nie, G.; Aust, S. D. Detection and characterization of the lignin peroxidase compound II-veratryl alcohol cation radical complex, Biochemistry1997, 36, 14181-14185.
21. Khindaria, A.; Yamazaki, I.; Aust, S. D. Veratryl alcohol oxidation by lignin peroxidase, Biochemistry1995, 34, 16860-16869.
22. DuP. LoewG. H. In Plant Peroxidase: Biochemistry and Physiology, University of Geneva: Switzerland, 1993;pp 2730.
23. Doyle, W. A.; Blodig, W.; Veitch, N. C.; Piontek, K.; Smith, A. T. Two substrate interaction site in lignin peroxidase revealed by site-directed mutagenesis, Biochemistry1998, 37, 15097-15105.
24. Cholnowski, T.; Blodig, W.; Winterhalter, K. H.; Piontek, K. The crystal structure of lignin peroxidase at 1.70 Å resolution reveals a hydroxyl group on the Cβ of Tryptophan 171: a novel radical site formed during the redox cycle. J. Mol. Biol.1999, 286, 809-827.
25. Mester, T.; Amber-Balay, K.; Ciofl-Baffoni, S.; Banci, L.; Jones, A. D.; Tien, M. Oxidation of a tetrameric nonphenolic lignin model compound by lignin peroxidase. J. Biol. Chem.2001, 22, 22985-22990.
26. Sheng, D.; Gold, M. H. Irreversible oxidation of Ferricytochrome c by lignin peroxidase, Biochemistry1994, 37, 2029-2036.
27. Mauro, J. M.; Finzel, L. A.; Hazzard, J. T.; Meyer, T. E.; Tollin, G.; Cusanovich, M. A.; Kraut, J. Tryptophan-191 → phenylalanine, a proximal-side mutation in yeast cytochrome cperoxidase that strongly affects the kinetics of ferrocytochrome c oxidation. Biochemistry1988, 27, 6243-6256.
28. Wariishi, H.; Huang, J.; Dunford, H. B.; Gold, M. H. Reactions of lignin peroxidase compounds I and II with veratryl alcohol. Transient-state kinetic characterization. J. Biol. Chem.1991, 266, 20694-20699.
29. Cabana, H.; Jones, J. P.; Agathos, S. N. Elimination of endocrine disrupting chemicals using white rot fungi and their lignin modifying enzymes: A review. Eng. Life. Sci.2007, 7, 429-456.
30. Koduri, R. S.; Tien, M. Kinetic analysis of Lignin Peroxidase: explanation for the mediation phenomenon by veratryl alcohol. Biochemistry1994, 33, 4225-1230.
31. Wariishi, H.; Gold, M. H. Lignin peroxidase compound III: formation, inactivation, and conversion to the native enzyme. FEBS Lett. 4 1989, 243, 165-168.
32. Wariishi, H.; Gold, M. H. Lignin peroxidase compound III: mechanism of formation and decomposition. J. Biol. Chem.1990, 265, 2070-2077.