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Cited by 138Enzyme-mediated dye degradationEnzyme Production and CharacterizationTannin, Tannase and Anticancer Activities

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Purification, biochemical characterization and dye decolorization capacity of an alkali-resistant and metal-tolerant laccase from Trametes pubescens

Si, Jing, Peng, Feng, Cui, Baokai·2013·Bioresource Technology
DOI 10.1016/j.biortech.2012.10.085
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Abstract

Extracellular laccase (Tplac) from Trametes pubescens was purified to homogeneity by a three-step method, which resulted in a high specific activity of 18.543 Umg(-1), 16.016-fold greater than that of crude enzyme at the same level. Tplac is a monomeric protein that has a molecular mass of 68 kDa. The enzyme demonstrated high activity toward 1.0mM ABTS at an optimum pH of 5.0 and temperature of 50 °C, and under these conditions, the catalytic efficiency (k(cat)/K(m)) is 8.34 s(-1) μM(-1). Tplac is highly stable and resistant under alkaline conditions, with pH values ranging from 7.0 to 10.0. Interestingly, above 88% of initial enzyme activity was maintained in the presence of metal ions at 25.0mM, leading to an increase in substrate affinity, which indicated that the laccase is highly metal-tolerant. These unusual properties demonstrated that the new fungal laccase Tplac has potentials for the specific industrial or environmental applications.

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Research works printed but not linked: 30

  1. Arora, 2010, Ligninolytic fungal laccases and their biotechnological applications, Appl. Biochem. Biotechnol., 160, 1760, 10.1007/s12010-009-8676-y · DOI
  2. Asgher, 2008, Recent developments in biodegradation of industrial pollutants by white rot fungi and their enzyme system, Biodegradation, 19, 771, 10.1007/s10532-008-9185-3 · DOI
  3. Bradford, 1976, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein–dye binding, Anal. Biochem., 72, 248, 10.1016/0003-2697(76)90527-3 · DOI · Paper page
  4. Claus, 2004, Laccases: structure, reactions, distribution, Micron, 35, 93, 10.1016/j.micron.2003.10.029 · DOI
  5. Duggleby, 1979, Experimental designs for estimating the kinetic parameters for enzyme-catalysed reactions, J. Theor. Biol., 81, 671, 10.1016/0022-5193(79)90276-5 · DOI
  6. Eisenman, 2007, Cryptococcus neoformans laccase catalyses melanin synthesis from both d- and l-DOPA, Microbiology, 153, 3954, 10.1099/mic.0.2007/011049-0 · DOI
  7. Enayatizamir, 2011, Biodegradation pathway and detoxification of the diazo dye Reactive Black 5 by Phanerochaete chrysosporium, Bioresour. Technol., 102, 10359, 10.1016/j.biortech.2011.08.130 · DOI
  8. Fang, 2012, A new marine bacterial laccase with chloride-enhancing, alkaline-dependent activity and dye decolorization ability, Bioresour. Technol., 111, 36, 10.1016/j.biortech.2012.01.172 · DOI
  9. Frasconi, 2010, Kinetic and biochemical properties of high and low redox potential laccases from fungal and plant origin, Biochim. Biophys. Acta, 1804, 899, 10.1016/j.bbapap.2009.12.018 · DOI
  10. Gomi, 2011, Degradation of the synthetic dye amaranth by the fungus Bjerkandera adusta Dec 1: inference of the degradation pathway from an analysis of decolorized products, Biodegradation, 22, 1239, 10.1007/s10532-011-9478-9 · DOI
  11. Guo, 2011, Production, purification and characterization of a thermostable laccase from a tropical white-rot fungus, World J. Microbiol. Biotechnol., 27, 731, 10.1007/s11274-010-0502-8 · DOI
  12. Johannes, 2000, Laccase activity tests and laccase inhibitors, J. Biotechnol., 78, 193, 10.1016/S0168-1656(00)00208-X · DOI
  13. Jonstrup, 2011, Sequential anaerobic-aerobic treatment of azo dyes: decolourisation and amine degradability, Desalination, 280, 339, 10.1016/j.desal.2011.07.022 · DOI
  14. Kalpana, 2011, Bioremediation of the heavy metal complex dye Isolan Dark Blue 2SGL-01 by white rot fungus Irpex lacteus, J. Hazard. Mater., 198, 198, 10.1016/j.jhazmat.2011.10.030 · DOI
  15. Kalyani, 2008, Biodegradation of reactive textile dye Red BL1 by an isolated bacterium Pseudomonas sp. SUK1, Bioresour. Technol., 99, 4635, 10.1016/j.biortech.2007.06.058 · DOI
  16. Kalyani, 2012, Characterization of a novel laccase from the isolated Coltricia perennis and its application to detoxification of biomass, Process Biochem., 47, 671, 10.1016/j.procbio.2012.01.013 · DOI
  17. Kim, 2012, Decolorization of Remazol Brilliant Blue R by a purified laccase of Polyporus brumalis, Appl. Biochem. Biotechnol., 166, 159, 10.1007/s12010-011-9412-y · DOI
  18. Litthauer, 2007, Purification and kinetics of a thermostable laccase from Pycnoporus sanguineus (SCC 108), Enzyme Microb. Technol., 40, 563, 10.1016/j.enzmictec.2006.05.011 · DOI
  19. Lorenzo, 2005, Inhibition of laccase activity from Trametes versicolor by heavy metals and organic compounds, Chemosphere, 60, 1124, 10.1016/j.chemosphere.2004.12.051 · DOI
  20. Mendonça, 2008, Evaluation of the white-rot fungi Ganoderma australe and Ceriporiopsis subvermispora in biotechnological applications, J. Ind. Microbiol. Biotechnol., 35, 1323, 10.1007/s10295-008-0414-x · DOI
  21. Murugesan, 2009, Effect of metal ions on reactive dye decolorization by laccase from Ganoderma lucidum, J. Hazard. Mater., 168, 523, 10.1016/j.jhazmat.2009.02.075 · DOI
  22. Roriz, 2009, Application of response surface methodological approach to optimise Reactive Black 5 decolouration by crude laccase from Trametes pubescens, J. Hazard. Mater., 169, 691, 10.1016/j.jhazmat.2009.03.150 · DOI
  23. Sadhasivam, 2008, Production, purification and characterization of mid-redox potential laccase from a newly isolated Trichoderma harzianum WL1, Process Biochem., 43, 736, 10.1016/j.procbio.2008.02.017 · DOI
  24. Shevchenko, 1996, Linking genome and proteome by mass spectrometry: large-scale identification of yeast proteins from two dimensional gels, Proc. Natl. Acad. Sci. USA, 93, 14440, 10.1073/pnas.93.25.14440 · DOI
  25. Shin, 2000, Purification and characterization of a new member of the laccase family from the white-rot basidiomycete Coriolus hirsutus, Arch. Biochem. Biophys., 384, 109, 10.1006/abbi.2000.2083 · DOI
  26. Thurston, 1994, The structure and function of fungal laccase, Microbiology, 140, 19, 10.1099/13500872-140-1-19 · DOI · Paper page
  27. Xiao, 2012, Biodecolorization of Naphthol Green B dye by Shewanella oneidensis MR-1 under anaerobic conditions, Bioresour. Technol., 110, 86, 10.1016/j.biortech.2012.01.099 · DOI
  28. Zhang, 2009, Purification and characterization of a thermostable laccase with unique oxidative characteristics from Trametes hirsuta, Biotechnol. Lett., 31, 837, 10.1007/s10529-009-9945-0 · DOI
  29. Zhu, 2011, Production of a thermostable metal-tolerant laccase from Trametes versicolor and its application in dye decolorization, Biotechnol. Bioprocess Eng., 16, 1027, 10.1007/s12257-011-0129-0 · DOI
  30. Zou, 2012, Purification and characterization of a novel laccase from the edible mushroom Hericium coralloides, J. Microbiol., 50, 72, 10.1007/s12275-012-1372-6 · DOI

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Metadata

Authors
Si, J., Peng, F., & Cui, B.
Affiliations
Beijing Forestry University (CN)
ORCID
Venue
Bioresource Technology
Publisher
Elsevier BV
Published
2013-01
Volume
128
Pages
49-57
ISSN
0960-8524 (ISSN-L)
DOI
10.1016/j.biortech.2012.10.085
OpenAlex
W1988614666
Cited by
138
References
0
Citations by year
2026: 3 · 2025: 7 · 2024: 12 · 2023: 11 · 2022: 6 · 2021: 15 · 2020: 10 · 2019: 17 · 2018: 14 · 2017: 12 · 2016: 8 · 2015: 6 · 2014: 12 · 2013: 5
FWCI
8.41
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Bioresource Technology (publishedVersion)
  • PubMed (publishedVersion)
Funders
Program for New Century Excellent Talents in University
Topics
  • Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Enzyme-mediated dye degradation
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
  • Physical Sciences › Chemistry › Organic Chemistry › Tannin, Tannase and Anticancer Activities
Keywords
laccase, Trametes pubescens, fungal extracellular enzymes, enzyme purification, alkali resistance, metal tolerance, dye decolorization, ABTS, enzyme kinetics, enzyme stability, monomeric protein, industrial biocatalysis
MeSH terms
Alkalies, Color, Coloring Agents, Enzyme Stability, Metals, Water Pollutants, Chemical, Water Purification, Laccase, Trametes, Wastewater

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