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Oxidation of non‐phenolic substrates: An expanded role for laccase in lignin biodegradation
Abstract
In the presence of substrates such as Remazol Blue and 2,2'‐azinobis(3‐ethylbenzthiazoline‐6‐sulphonate) (ABTS), laccases Coriolus (Trametes) versicolor can also oxidize non‐phenolic lignin model compounds. Veratryl alcohol (I) and 1‐(3,4‐dimethoxyphenyl)‐2‐(2‐methoxyphenoxy)‐propane‐1, 3‐diol (III) were oxidized by laccase and mediator to give the α‐carbonyl derivatives. The β‐1 lignin model dimer, 1‐(3,4‐dimethoxyphenyl)‐2‐phenoxy‐ethane‐1, 2‐diol(II) was cleaved by laccase in the presence of ABTS to give veratraldehyde and benzaldehyde. On the basis of these observations, we propose that laccase is capable of oxidizing both phenolic and non‐phenolic moieties of lignin but that the latter is dependent on the co‐presence of primary laccase substrates.
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Solomon, E. I., Sundaram, U. M., & Machonkin, T. E. (1996) · Chemical Reviews · doi:10.1021/cr950046o · Cited by 3,664
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Thurston, C. F. (1994) · Microbiology · doi:10.1099/13500872-140-1-19 · Cited by 1,941
Laccases: a never-ending story
Giardina, P., Faraco, V., Pezzella, C., Piscitelli, A., Vanhulle, S., & Sannia, G. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0169-1 · Cited by 1,007
Piontek, K., Antorini, M., & Choinowski, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204571200 · Cited by 909
Ruiz‐Dueñas, F. J., & Martínez, Á. T. (2009) · Microbial Biotechnology · doi:10.1111/j.1751-7915.2008.00078.x · Cited by 561
Structure–function relationship among bacterial, fungal and plant laccases
Dwivedi, U. N., Singh, P., Pandey, V. P., & Kumar, A. (2011) · Journal of Molecular Catalysis B: Enzymatic · doi:10.1016/j.molcatb.2010.11.002 · Cited by 481
Husain, Q. (2006) · Critical Reviews in Biotechnology · doi:10.1080/07388550600969936 · Cited by 429
Can laccases catalyze bond cleavage in lignin?
Munk, L., Sitarz, A. K., Kalyani, D. C., Mikkelsen, J. D., & Meyer, A. S. (2015) · Biotechnology Advances · doi:10.1016/j.biotechadv.2014.12.008 · Cited by 395
Engineering and Applications of fungal laccases for organic synthesis
Kunamneni, A., Camarero, S., García-Burgos, C., Plou, F. J., Ballesteros, A., & Alcalde, M. (2008) · Microbial Cell Factories · doi:10.1186/1475-2859-7-32 · Cited by 340
Laccases and Their Applications: A Patent Review
Kunamneni, A., Plou, F., Ballesteros, A., & Alcalde, M. (2008) · Recent Patents on Biotechnology · doi:10.2174/187220808783330965 · Cited by 310
Rivera-Hoyos, C. M., Morales-Álvarez, E. D., Poutou-Piñales, R. A., Pedroza-Rodríguez, A. M., RodrÍguez-Vázquez, R., & Delgado-Boada, J. M. (2013) · Fungal Biology Reviews · doi:10.1016/j.fbr.2013.07.001 · Cited by 256
Bioprospecting and biotechnological applications of fungal laccase
Upadhyay, P., Shrivastava, R., & Agrawal, P. K. (2016) · 3 Biotech · doi:10.1007/s13205-015-0316-3 · Cited by 242
Palmieri, G., Cennamo, G., & Sannia, G. (2005) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2004.03.026 · Cited by 204
Aptitude of Oxidative Enzymes for Treatment of Wastewater Pollutants: A Laccase Perspective
Unuofin, J. O., Okoh, A. I., & Nwodo, U. U. (2019) · Molecules · doi:10.3390/molecules24112064 · Cited by 172
Use of laccase together with redox mediators to decolourize Remazol Brilliant Blue R
Soares, G. M. B., de Amorim, M. T. P., & Costa-Ferreira, M. (2001) · Journal of Biotechnology · doi:10.1016/s0168-1656(01)00302-9 · Cited by 165
Biocatalysis with Laccases: An Updated Overview
Bassanini, I., Ferrandi, E. E., Riva, S., & Monti, D. (2020) · Catalysts · doi:10.3390/catal11010026 · Cited by 139
van der Wal, A., de Boer, W., Smant, W., & van Veen, J. A. (2007) · Plant and Soil · doi:10.1007/s11104-007-9437-8 · Cited by 106
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Cannatelli, M. D., & Ragauskas, A. J. (2017) · The Chemical Record · doi:10.1002/tcr.201600033 · Cited by 99
Sitarz, A. K., Mikkelsen, J. D., & Meyer, A. S. (2016) · Critical Reviews in Biotechnology · doi:10.3109/07388551.2014.949617 · Cited by 99
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Gu, Y., Yuan, L., Jia, L., Xue, P., & Yao, H. (2021) · RSC Advances · doi:10.1039/d1ra05104k · Cited by 80
Solís-Oba, M., Ugalde-Saldívar, V. M., González, I., & Viniegra-González, G. (2005) · Journal of Electroanalytical Chemistry · doi:10.1016/j.jelechem.2005.01.025 · Cited by 79
Fungal laccases as tools for biodegradation of industrial dyes
Zucca, P., Cocco, G., Sollai, F., & Sanjust, E. (2016) · Biocatalysis · doi:10.1515/boca-2015-0007 · Cited by 75
Lignin degrading system of white-rot fungi and its exploitation for dye decolorization
Shah, V., & Nerud, F. (2002) · Canadian Journal of Microbiology · doi:10.1139/w02-090 · Cited by 70
González Arzola, K., Arévalo, M. C., & Falcón, M. A. (2009) · Electrochimica Acta · doi:10.1016/j.electacta.2008.10.059 · Cited by 59
A Semi-Rational Approach to Engineering Laccase Enzymes
Miele, A., Giardina, P., Notomista, E., Piscitelli, A., Sannia, G., & Faraco, V. (2010) · Molecular Biotechnology · doi:10.1007/s12033-010-9289-y · Cited by 28
Fujita, M., Era, A., Ike, M., Soda, S., Miyata, N., & Hirao, T. (2000) · Journal of Bioscience and Bioengineering · doi:10.1016/s1389-1723(01)80006-2 · Cited by 27
Lignin‐Degrading Enzymes: An Overview
Hatti‐Kaul, R., & Ibrahim, V. (2013) · Bioprocessing Technologies in Biorefinery for Sustainable Production of Fuels, Chemicals, and Polymers · doi:10.1002/9781118642047.ch10 · Cited by 25
Metadata
- Authors
- Bourbonnais, R., & Paice, M. G.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1990-07-02
- Volume
- 267
- Issue
- 1
- Pages
- 99-102
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1604648834
- Cited by
- 1,337
- References
- 0
- FWCI
- 11.75
- Type
- journal article
- Language
- en
- Open access
- closed
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