The DOI matches its Crossref record; 131 of the 131 references it cites were found in a registry or an index.
Lignin peroxidase functionalities and prospective applications
Open accessAbstract
Ligninolytic extracellular enzymes, including lignin peroxidase, are topical owing to their high redox potential and prospective industrial applications. The prospective applications of lignin peroxidase span through sectors such as biorefinery, textile, energy, bioremediation, cosmetology, and dermatology industries. The litany of potentials attributed to lignin peroxidase is occasioned by its versatility in the degradation of xenobiotics and compounds with both phenolic and non-phenolic constituents. Over the years, ligninolytic enzymes have been studied however; research on lignin peroxidase seems to have been lagging when compared to other ligninolytic enzymes which are extracellular in nature including laccase and manganese peroxidase. This assertion becomes more pronounced when the application of lignin peroxidase is put into perspective. Consequently, a succinct documentation of the contemporary functionalities of lignin peroxidase and, some prospective applications of futuristic relevance has been advanced in this review. Some articulated applications include delignification of feedstock for ethanol production, textile effluent treatment and dye decolourization, coal depolymerization, treatment of hyperpigmentation, and skin-lightening through melanin oxidation. Prospective application of lignin peroxidase in skin-lightening functions through novel mechanisms, hence, it holds high value for the cosmetics sector where it may serve as suitable alternative to hydroquinone; a potent skin-lightening agent whose safety has generated lots of controversy and concern.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Features of promising technologies for pretreatment of lignocellulosic biomass
MOSIER, N. (2005) · Bioresource Technology · doi:10.1016/j.biortech.2004.06.025 · Cited by 6,251
The Paleozoic Origin of Enzymatic Lignin Decomposition Reconstructed from 31 Fungal Genomes
Floudas, D., Binder, M., Riley, R., Barry, K., Blanchette, R. A., Henrissat, B., Martínez, A. T., Otillar, R., Spatafora, J. W., Yadav, J. S., et al. (2012) · Science · doi:10.1126/science.1221748 · Cited by 1,779
Trends in bioconversion of lignocellulose: Biofuels, platform chemicals & biorefinery concept
Menon, V., & Rao, M. (2012) · Progress in Energy and Combustion Science · doi:10.1016/j.pecs.2012.02.002 · Cited by 1,546
Lignin-Degrading Enzyme from the Hymenomycete Phanerochaete chrysosporium Burds
Tien, M., & Kirk, T. K. (1983) · Science · doi:10.1126/science.221.4611.661 · Cited by 1,205
Hatakka, A. (1994) · FEMS Microbiology Reviews · doi:10.1016/0168-6445(94)90076-0 · Cited by 1,157
White-rot fungi and their enzymes for the treatment of industrial dye effluents
Wesenberg, D. (2003) · Biotechnology Advances · doi:10.1016/j.biotechadv.2003.08.011 · Cited by 1,149
Martı́nez, Á. T., Speranza, M., Ruiz-Dueñas, F. J., Ferreira, P., Camarero, S., Guillén, F., Martı́nez, M. J., Gutiérrez, A., & del Río, J. C. (2005) · PubMed · Cited by 1,064
Kim, Y.-J., & Uyama, H. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5054-y · Cited by 1,062
Review: lignin conversion by manganese peroxidase (MnP)
Hofrichter, M. (2002) · Enzyme and Microbial Technology · doi:10.1016/s0141-0229(01)00528-2 · Cited by 1,040
Genome sequence of the lignocellulose degrading fungus Phanerochaete chrysosporium strain RP78
Martinez, D., Larrondo, L. F., Putnam, N., Gelpke, M. D. S., Huang, K., Chapman, J., Helfenbein, K. G., Ramaiya, P., Detter, J. C., Larimer, F., et al. (2004) · Nature Biotechnology · doi:10.1038/nbt967 · Cited by 939
Cited by
A Review on Metal- and Metal Oxide-Based Nanozymes: Properties, Mechanisms, and Applications
Liu, Q., Zhang, A., Wang, R., Zhang, Q., & Cui, D. (2021) · Nano-Micro Letters · doi:10.1007/s40820-021-00674-8 · Cited by 745
Andlar, M., Rezić, T., Marđetko, N., Kracher, D., Ludwig, R., & Šantek, B. (2018) · Engineering in Life Sciences · doi:10.1002/elsc.201800039 · Cited by 667
Peroxidase enzymes as green catalysts for bioremediation and biotechnological applications: a review
Sellami, K., Couvert, A., Nasrallah, N., Maachi, R., Abouseoud, M., & Amrane, A. (2022) · Science of The Total Environment · doi:10.1016/j.scitotenv.2021.150500 · Cited by 205
Bilal, M., Rasheed, T., Iqbal, H. M. N., & Yan, Y. (2018) · Science of The Total Environment · doi:10.1016/j.scitotenv.2018.06.274 · Cited by 184
Singh, A. K., Bilal, M., Iqbal, H. M. N., & Raj, A. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.02.032 · Cited by 116
Metadata
- Authors
- Falade, A. O., Nwodo, U. U., Iweriebor, B. C., Green, E., Mabinya, L. V., & Okoh, A. I.
- Venue
- MicrobiologyOpen
- Publisher
- Wiley
- Published
- 2016-09-07
- Volume
- 6
- Issue
- 1
- Pages
- e00394
- ISSN
- 2045-8827 (ISSN-L)
- OpenAlex
- W2517999878
- Cited by
- 323
- References
- 131
- FWCI
- 17.81
- Type
- journal article
- Language
- en
- Open access
- gold
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Lignin peroxidase functionalities and prospective applications. https://app.cochat.ai/papers/10.1002/mbo3.394
- The paper
- Falade, A. O., Nwodo, U. U., Iweriebor, B. C., Green, E., Mabinya, L. V., & Okoh, A. I. (2017). Lignin peroxidase functionalities and prospective applications. MicrobiologyOpen. https://doi.org/10.1002/mbo3.394
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.