The DOI matches its Crossref record; 221 of the 221 references it cites were found in a registry or an index.
Horseradish peroxidase (HRP) as a tool in green chemistry
Abstract
The horseradish peroxidase (HRP) potential in organic synthesis.
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In the citing paper
“The enzymes responsible for dye decolorisation belong to the family of oxidoreductases (EC: 1), which catalyse oxidation and reduction reactions, finding application in various domains varying from diagnostics to wastewater treatment and production of chemicals or potentially biofuels 112-118 .”
From Degradation of anthraquinone dyes from effluents: A review focusing on enzymatic dye degradation with industrial potential (2020) · cites this paper as [115]
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Citations
Cites
Comprehensive Coordination Chemistry
Eaborn, C. (1988) · Journal of Organometallic Chemistry · doi:10.1016/0022-328x(88)83103-6 · Cited by 7,162
Improvement of enzyme activity, stability and selectivity via immobilization techniques
Mateo, C., Palomo, J. M., Fernandez-Lorente, G., Guisan, J. M., & Fernandez-Lafuente, R. (2007) · Enzyme and Microbial Technology · doi:10.1016/j.enzmictec.2007.01.018 · Cited by 3,375
Comprehensive Coordination Chemistry II
McCleverty, J. A., & Meyer, T. (2003) · Bristol Research (University of Bristol) · Cited by 2,690
Enzyme immobilisation in biocatalysis: why, what and how
Sheldon, R. A., & van Pelt, S. (2013) · Chem. Soc. Rev. · doi:10.1039/c3cs60075k · Cited by 2,675
Enzyme Immobilization: The Quest for Optimum Performance
Sheldon, R. A. (2007) · Advanced Synthesis & Catalysis · doi:10.1002/adsc.200700082 · Cited by 2,083
Modifying enzyme activity and selectivity by immobilization
Rodrigues, R. C., Ortiz, C., Berenguer-Murcia, Á., Torres, R., & Fernández-Lafuente, R. (2013) · Chem. Soc. Rev. · doi:10.1039/c2cs35231a · Cited by 1,810
Potential of Different Enzyme Immobilization Strategies to Improve Enzyme Performance
Garcia‐Galan, C., Berenguer‐Murcia, Á., Fernández‐Lafuente, R., & Rodrigues, R. C. (2011) · Advanced Synthesis & Catalysis · doi:10.1002/adsc.201100534 · Cited by 1,617
Horseradish peroxidase: a modern view of a classic enzyme
Veitch, N. C. (2004) · Phytochemistry · doi:10.1016/j.phytochem.2003.10.022 · Cited by 1,379
Biotransformations in Organic Chemistry
Faber, K. (2000) · Springer eBooks · doi:10.1007/978-3-642-98071-8 · Cited by 1,279
Peroxidases in chemistry and biology
Everse, J., Everse, K. E., & Grisham, M. B. (1990) · CRC Press eBooks · Cited by 1,028
Research works printed but not linked: 6
- Planche, 1810, Bull. de Pharmacie, 2, 578
- H. B. Dunford , Heme peroxidases, Wiley–VCH, New York, 1999
- M.-R. Kula , in Enzyme Catalysis in Organic Synthesis, ed. H. W. Karlheinz Drauz, Wiley-VCH, Mörlenbach, 2002, pp. 1–39
- Hernandez-Ruiz, 2001, Biochem. J., 354, 107, 10.1042/bj3540107 · DOI
- Tonami, 2002, e-Polym., 3, 1
- Lee, 2008, J. Microbiol. Biotechnol., 18, 107
Cited by
Routoula, E., & Patwardhan, S. V. (2020) · Environmental Science & Technology · doi:10.1021/acs.est.9b03737 · Cited by 579
Crosslinking strategies for silk fibroin hydrogels: promising biomedical materials
Farokhi, M., Aleemardani, M., Solouk, A., Mirzadeh, H., Teuschl, A. H., & Redl, H. (2021) · Biomedical Materials · doi:10.1088/1748-605x/abb615 · Cited by 95
Metadata
- Authors
- Lopes, G. R., Pinto, D. C. G. A., & Silva, A. M. S.
- Venue
- RSC Adv.
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2014
- Volume
- 4
- Issue
- 70
- Pages
- 37244-37265
- ISSN
- 2046-2069
- Cited by
- 154
- References
- 221
- Language
- en
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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.
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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.
