Transformation of triclosan by a novel cold-adapted laccase from Botrytissp. FQ

Yuanyuan Shi, Deyang Kong, Jiayang Liu, Junhe Lu, Xiaoming Yin, Quansuo Zhou

PDF(1276 KB)
PDF(1276 KB)
Front. Environ. Sci. Eng. ›› 2017, Vol. 11 ›› Issue (3) : 6. DOI: 10.1007/s11783-017-0927-5
RESEARCH ARTICLE
RESEARCH ARTICLE

Transformation of triclosan by a novel cold-adapted laccase from Botrytissp. FQ

Author information +
History +

Highlights

A cold-adapt laccase excreted by a fungi from rotten tomato was characterized.

The laccase can effectively transform triclosan to form polymerized products.

The reaction rate is first order to the concentrations of both laccase and triclosan.

The reaction was inhibited by humic acid.

Abstract

This work investigated the transformation of triclosan (TCS) by laccase produced by a pathogen isolated from rotten tomato. The pathogen was characterized asBotrytis sp. FQ, belonging to subphylum Deuteromycotina. The laccase exhibited cold-adaptation with relatively high activity at 20°C. The laccase could effectively transform TCS. Approximately 62% TCS could be removed at dose of 1.0 unit·mL1 in 120 min. The reaction rate appeared to be pseudo-first-order to the concentration of the substrate, suggesting the laccase activity remained stable during the reaction. Transformation products of TCS were analyzed by mass spectrometry and it was revealed that TCS dimers were formed via radical coupling pathways. During this process, laccase catalyzed oxidation of TCS to form a radical intermediate is the rate limiting step. However, this step can be reversed by humic acid. Overall, the laccase showed great potential in the treatment of phenolic contaminants. Since laccase is widely presented in natural environment, this study also revealed an important pathway involved in the transformation of phenolic contaminants in the environment.

Graphical abstract

Keywords

Laccase / Botrytis cinerea / Triclosan / Transformation / Kinetics

Cite this article

Download citation ▾
Yuanyuan Shi, Deyang Kong, Jiayang Liu, Junhe Lu, Xiaoming Yin, Quansuo Zhou. Transformation of triclosan by a novel cold-adapted laccase from Botrytissp. FQ. Front. Environ. Sci. Eng., 2017, 11(3): 6 https://doi.org/10.1007/s11783-017-0927-5

References

[1]
Gujjala L K S ,  Bandyopadhyay T K ,  Banerjee R . Kinetic modelling of laccase mediated delignification of Lantana camara. Bioresource Technology, 2016, 212: 47–54
CrossRef Pubmed Google scholar
[2]
Nguyen L N, Hai  F I, Dosseto  A, Richardson C ,  Price W E ,  Nghiem L D . Continuous adsorption and biotransformation of micropollutants by granular activated carbon-bound laccase in a packed-bed enzyme reactor. Bioresource Technology, 2016, 210: 108–116
CrossRef Pubmed Google scholar
[3]
Mao L, Huang  Q, Luo Q ,  Lu J, Yang  X, Gao S . Ligninase-mediated removal of 17b-estradiol from water in the presence of natural organic matter: efficiency and pathways. Chemosphere, 2010, 80(4): 469–473
CrossRef Pubmed Google scholar
[4]
Mao L, Lu  J, Habteselassie M ,  Luo Q, Gao  S, Cabrera M ,  Huang Q . Ligninase-mediated removal of natural and synthetic estrogens from water: II. Reactions of 17b-estradiol. Environmental Science & Technology, 2010, 44(7): 2599–2604nbsp;doi:10.1021/es903058k
Pubmed
[5]
Litthauer D, van Vuuren  M J, van Tonder  A, Wolfaardt F W . Purification and kinetics of a thermostable laccase from Pycnoporus sanguineus (SCC 108). Enzyme and Microbial Technology, 2007, 40(4): 563568
CrossRef Google scholar
[6]
Liu J Y, Cai  Y J, Liao  X R, Huang  Q G, Hao  Z H, Hu  M M, Zhang  D B, Li  Z L. Efficiency of laccase production in a 65-liter air-lift reactor for potential green industrial and environmental application. Journal of Cleaner Production, 2013, 39(1): 154160
[7]
Wang Z X, Cai  Y J, Liao  X R, Tao  G J, Li  Y Y, Zhang  F, Zhang D B . Purification and characterization of two thermostable laccases with high cold adapted characteristics from Pycnoporus sp. SYBC-L1. Process Biochemistry, 2010, 45(10): 17201729
CrossRef Google scholar
[8]
Buth J M, Steen  P O, Sueper  C, Blumentritt D ,  Vikesland P J ,  Arnold W A ,  McNeill K . Dioxin photoproducts of triclosan and its chlorinated derivatives in sediment cores. Environmental Science & Technology, 2010, 44(12): 4545–4551
CrossRef Pubmed Google scholar
[9]
Halden R U. On the need and speed of regulating triclosan and triclocarban in the United States. Environmental Science & Technology, 2014, 48(7): 3603–3611
CrossRef Pubmed Google scholar
[10]
Dann A B, Hontela  A. Triclosan: environmental exposure, toxicity and mechanisms of action. Journal of Applied Toxicology, 2011, 31(4): 285–311
CrossRef Pubmed Google scholar
[11]
Fiss E M, Rule  K L, Vikesland  P J. Formation of chloroform and other chlorinated byproducts by chlorination of triclosan-containing antibacterial products. Environmental Science & Technology, 2007, 41(7): 2387–2394
CrossRef Pubmed Google scholar
[12]
Fiss E M, Rule  K L, Vikesland  P J. Formation of chloroform and other chlorinated byproducts by chlorination of triclosan-containing products. Environmental Science & Technology, 2008, 42(3): 976976
CrossRef Pubmed Google scholar
[13]
Latch D E, Packer  J L, Stender  B L, VanOverbeke  J, Arnold W A ,  McNeill K . Aqueous photochemistry of triclosan: formation of 2,4-dichlorophenol, 2,8-dichlorodibenzo-p-dioxin, and oligomerization products. Environmental Toxicology and Chemistry, 2005, 24(3): 517–525
CrossRef Pubmed Google scholar
[14]
Zhang H, Huang  C H. Oxidative transformation of triclosan and chlorophene by manganese oxides. Environmental Science & Technology, 2003, 37(11): 2421–2430
CrossRef Pubmed Google scholar
[15]
Li J, Peng  J, Zhang Y ,  Ji Y, Shi  H, Mao L ,  Gao S. Removal of triclosan via peroxidases-mediated reactions in water: reaction kinetics, products and detoxification. Journal of Hazardous Materials, 2016, 310: 152–160
CrossRef Pubmed Google scholar
[16]
Diwaniyan S, Kharb  D, Raghukumar C ,  Kuhad R . Decolorization of synthetic dyes and textile effluents by basidiomycetous fungi. Water, Air, and Soil Pollution, 2010, 210(1–4): 409419
[17]
Tien M, Kirk  T K. Lignin peroxidase of Phanerochaete chrysosporium. Methods in Enzymology, 1988, 161: 238249
CrossRef Google scholar
[18]
Camarero S, Ibarra  D, Martínez M J ,  Martínez A T . Lignin-derived compounds as efficient laccase mediators for decolorization of different types of recalcitrant dyes. Applied and Environmental Microbiology, 2005, 71(4): 1775–1784
CrossRef Pubmed Google scholar
[19]
Yu H, Sutton  J C. Morphological development and interactions of Gliocladium roseum and Botrytis cinerea in raspberry. Canadian Journal of Plant Pathology-Revue Canadienne De Phytopathologie, 1997, 19(3): 237246
CrossRef Google scholar
[20]
Morgan W M. The effect of night temperature and glasshouse ventilation on the incidence of Botrytis cinerea in a late-planted tomato crop. Crop Protection (Guildford, Surrey), 1984, 3(2): 243251
CrossRef Google scholar
[21]
Swadling I R, Jeffries  P. Antagonistic properties of two bacterial biocontrol agents of grey mould disease. Biocontrol Science and Technology, 1998, 8(3): 439448
CrossRef Google scholar
[22]
Amerine M A. The search for good wine. Science, 1966, 154(3757): 1621–1628
CrossRef Pubmed Google scholar
[23]
Zouari N, Romette  J L, Thomas  D. Purification and properties of two laccase isoenzymes produced by Botrytis cinerea. Applied Biochemistry and Biotechnology, 1987, 15(3): 213225
CrossRef Google scholar
[24]
Baldrian P. Fungal laccases—Occurrence and properties. FEMS Microbiology Reviews, 2006, 30(2): 215–242 PMID:16472305 doi:10.1111/j.1574-4976.2005.00010.x
[25]
Kim Y, Yeo  S, Kim M K ,  Choi H T . Removal of estrogenic activity from endocrine-disrupting chemicals by purified laccase of Phlebia tremellosa. FEMS Microbiology Letters, 2008, 284(2): 172–175
CrossRef Pubmed Google scholar
[26]
Wang Z, Cai  Y, Liao X ,  Zhang F ,  Zhang D ,  Li Z. Production and characterization of a novel laccase with cold adaptation and high thermal stability from an isolated fungus. Applied Biochemistry and Biotechnology, 2010, 162(1): 280–294nbsp;doi:10.1007/s12010-009-8801-y
Pubmed
[27]
Auriol M, Filali-Meknassi  Y, Adams C D ,  Tyagi R D . Natural and synthetic hormone removal using the horseradish peroxidase enzyme: temperature and pH effects. Water Research, 2006, 40(15): 2847–2856
CrossRef Pubmed Google scholar
[28]
Lu J, Huang  Q, Mao L . Removal of acetaminophen using enzyme-mediated oxidative coupling processes: I. Reaction rates and pathways. Environmental Science & Technology, 2009, 43(18): 7062–7067
CrossRef Pubmed Google scholar
[29]
Murray C A, Parsons  S A. Removal of NOM from drinking water: Fenton’s and photo-Fenton’s processes. Chemosphere, 2004, 54(7): 1017–1023
CrossRef Pubmed Google scholar

Acknowledgements

The work was supported by the National Natural Science Foundation of China (Grant No. 51503074), the Fundamental Research Funds for Central Universities (KYZ201626) and the priority Academic Program Development (PAPD) of Jiangsu Higher Education Institute. We would like to thank Kang Wu (SEM laboratory, Jiangnan University, Wuxi, China) for his assistance in SEM observation.

RIGHTS & PERMISSIONS

2017 Higher Education Press and Springer–Verlag Berlin Heidelberg
AI Summary AI Mindmap
PDF(1276 KB)

Accesses

Citations

Detail

Sections
Recommended

/