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Purification, biochemical characterization and dye decolorization capacity of an alkali-resistant and metal-tolerant laccase from Trametes pubescens
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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“In the three works, it was identified that in azo dyes, the first step in the discolouration is the splitting of the bond -N=N-, which results in obtaining two asymmetric intermediate products (Figure 4), [289,290,291].”
From A Brief History of Colour, the Environmental Impact of Synthetic Dyes and Removal by Using Laccases (2021) · cites this paper as [291]
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Cited by
Sorted by citations
A Brief History of Colour, the Environmental Impact of Synthetic Dyes and Removal by Using Laccases
Ardila-Leal, L. D., Poutou-Piñales, R. A., Pedroza-Rodríguez, A. M., & Quevedo-Hidalgo, B. E. (2021) · Molecules · doi:10.3390/molecules26133813 · Cited by 544
Zimbardi, A., Camargo, P., Carli, S., Aquino Neto, S., Meleiro, L., Rosa, J., De Andrade, A., Jorge, J., & Furriel, R. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17050672 · Cited by 71
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)
- 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
- 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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- Si, J., Peng, F., & Cui, B. (2013). Purification, biochemical characterization and dye decolorization capacity of an alkali-resistant and metal-tolerant laccase from Trametes pubescens. Bioresource Technology. https://doi.org/10.1016/j.biortech.2012.10.085