ArticleApplied and environmental microbiology2014
Latex clearing protein-an oxygenase cleaving poly(cis-1,4-isoprene) rubber at the cis double bonds.
Article in Applied and environmental microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Microbial plastic degradation: enzymes, pathways, challenges, and perspectives.Microbiology and molecular biology reviews : MMBR · 2025Review
- New insights on poly(Frontiers in bioengineering and biotechnology · 2025Article
- Computational investigation of cis-1,4-polyisoprene binding to the latex-clearing protein LcpK30.PloS one · 2024Article
- Assembly strategies for rubber-degrading microbial consortia based on omics tools.Frontiers in bioengineering and biotechnology · 2023Review
- Biodegradation of rubber in cultures of Rhodococcus rhodochrous and by its enzyme latex clearing protein.Biodegradation · 2022Article
- Characterization of Latex-Clearing Protein and Aldehyde Dehydrogenases Involved in the Utilization of poly(cis-1,4-isoprene) by Nocardia farcinica NBRC 15532Microorganisms · 2022Article
- Article
- Rubber Degrading Strains:Polymers · 2021Article
- Microbial Degradation of Rubber: Actinobacteria.Polymers · 2021Review
- Insights from the comparative genome analysis of natural rubber degradingBioinformation · 2021Article
- Characterization of the genes responsible for rubber degradation in Actinoplanes sp. strain OR16.Applied microbiology and biotechnology · 2020Article
- Global Regulator of Rubber Degradation in Gordonia polyisoprenivorans VH2: Identification and Involvement in the Regulation Network.Applied and environmental microbiology · 2020Article
- Towards the understanding of the enzymatic cleavage of polyisoprene by the dihaem-dioxygenase RoxA.AMB Express · 2019Article
- Rubber oxygenases.Applied microbiology and biotechnology · 2019Review
- Rhizobacter gummiphilus NS21 has two rubber oxygenases (RoxA and RoxB) acting synergistically in rubber utilisation.Applied microbiology and biotechnology · 2018Article
- Production of functionalized oligo-isoprenoids by enzymatic cleavage of rubber.Microbial biotechnology · 2017Article
- Structural and Functional Analysis of Latex Clearing Protein (Lcp) Provides Insight into the Enzymatic Cleavage of Rubber.Scientific reports · 2017Article
- RoxB Is a Novel Type of Rubber Oxygenase That Combines Properties of Rubber Oxygenase RoxA and Latex Clearing Protein (Lcp).Applied and environmental microbiology · 2017Article
- Assays for the Detection of Rubber Oxygenase Activities.Bio-protocol · 2017Article
- Cleavage of Rubber by the Latex Clearing Protein (Lcp) of Streptomyces sp. Strain K30: Molecular Insights.Applied and environmental microbiology · 2016Article
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6 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Gordonia polyisoprenivorans strain VH2, a potent rubber-degrading actinomycete, harbors two latex clearing proteins (Lcps), which are known to be essential for the microbial degradation of rubber. However, biochemical information on the exact role of this protein in the degradation of polyisoprene was lacking. In this study, the gene encoding Lcp1VH2 was heterologously expressed in strains of Escherichia coli, the corresponding protein was purified, and its role in rubber degradation was examined by measurement of oxygen consumption as well as by chromatographic and spectroscopic methods. It turned out that active Lcp1VH2 is a monomer and is responsible for the oxidative cleavage of poly(cis-1,4-isoprene) in synthetic as well as in natural rubber by the addition of oxygen (O2) to the cis double bonds. The resulting oligomers possess repetitive isoprene units with aldehyde (CHO-CH2-) and ketone (-CH2-CO-CH3) functional groups at the termini. Two fractions with average isoprene contents of 18 and 10, respectively, were isolated, thus indicating an endocleavage mechanism. The activity of Lcp1VH2 was determined by applying a polarographic assay. Alkenes, acyclic terpenes, or other rubber-like polymers, such as poly(cis-1,4-butadiene) or poly(trans-1,4-isoprene), are not oxidatively cleaved by Lcp1VH2. The pH and temperature optima of the enzyme are at pH 7 and 30°C, respectively. Furthermore, it was demonstrated that active Lcp1VH2 is a Cu(II)-containing oxygenase that exhibits a conserved domain of unknown function which cannot be detected in any other hitherto-characterized enzyme. The results presented here indicate that this domain might represent a new protein family of oxygenases.
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