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Purification and Characterization of a Nylon-Degrading Enzyme
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A nylon-degrading enzyme found in the extracellular medium of a ligninolytic culture of the white rot fungus strain IZU-154 was purified by ion-exchange chromatography, gel filtration chromatography, and hydrophobic chromatography. The characteristics of the purified protein (i.e., molecular weight, absorption spectrum, and requirements for 2,6-dimethoxyphenol oxidation) were identical to those of manganese peroxidase, which was previously characterized as a key enzyme in the ligninolytic systems of many white rot fungi, and this result led us to conclude that nylon degradation is catalyzed by manganese peroxidase. However, the reaction mechanism for nylon degradation differed significantly from the reaction mechanism reported for manganese peroxidase. The nylon-degrading activity did not depend on exogenous H 2 O 2 but nevertheless was inhibited by catalase, and superoxide dismutase inhibited the nylon-degrading activity strongly. These features are identical to those of the peroxidase-oxidase reaction catalyzed by horseradish peroxidase. In addition, α-hydroxy acids which are known to accelerate the manganese peroxidase reaction inhibited the nylon-degrading activity strongly. Degradation of nylon-6 fiber was also investigated. Drastic and regular erosion in the nylon surface was observed, suggesting that nylon is degraded to soluble oligomers and that nylon is degraded selectively.
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“Polyurethane-degrading enzymes have already been reviewed two decades ago, 122 and PA degrading microbes have been described decades ago, too (though the functioning/enzymes of PA-degradation are still unconstrained).123,124”
From The fate of plastic in the ocean environment – a minireview (2021) · cites this paper as [124]
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Metadata
- Authors
- Deguchi, T., Kitaoka, Y., Kakezawa, M., & Nishida, T.
- Affiliations
- Kobe Steel (Japan) (JP)
- Shizuoka University (JP)
- Venue
- Applied and Environmental Microbiology
- Publisher
- American Society for Microbiology
- Published
- 1998-04
- Volume
- 64
- Issue
- 4
- Pages
- 1366-1371
- ISSN
- 0099-2240 (ISSN-L)
- 1098-5336
- PMC
- PMC106156
- OpenAlex
- W1608809237
- Cited by
- 175
- References
- 34
- Citations by year
- 2026: 7 · 2025: 8 · 2024: 7 · 2023: 18 · 2022: 8 · 2021: 11 · 2020: 9 · 2019: 7 · 2018: 3 · 2017: 6 · 2016: 6 · 2015: 5 · 2014: 5 · 2013: 6 · 2012: 7
- FWCI
- 3.40
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Applied and Environmental Microbiology (publishedVersion)
- PubMed Central (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed (publishedVersion)
- 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 › Environmental Science › Pollution › Microbial bioremediation and biosurfactants
- Keywords
- manganese peroxidase, white-rot fungi, ligninolytic fungi, enzyme purification, peroxidase-oxidase reaction, superoxide dismutase inhibition, catalase inhibition, α-hydroxy acids, extracellular enzymes
- MeSH terms
- Amidohydrolases, Biodegradation, Environmental, Caprolactam, Chromatography, Mitosporic Fungi, Microscopy, Electron, Scanning, Molecular Weight, Magnetic Resonance Spectroscopy, Nylons, Peroxidases, Polymers, Reactive Oxygen Species
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