ArticleBMC microbiology2016
Biochemical and spectroscopic characterization of purified Latex Clearing Protein (Lcp) from newly isolated rubber degrading Rhodococcus rhodochrous strain RPK1 reveals novel properties of Lcp.
Article in BMC microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 60 citations in OpenAlex.
- Deep eutectic solvent-assisted bacterial devulcanization, detoxification, and degradation of waste tyre rubber.RSC advances · 2026Article
- Whole-genomic and transcriptomic analyses elucidateApplied and environmental microbiology · 2026Article
- Screening and identification of fungal species associated with early-stage deterioration of natural rubber.MycoKeys · 2026Article
- Review
- Endophytic bacterial diversity in the latex-bearing caulosphere of Hevea brasiliensis Müll. Arg.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024Article
- Investigation of potential rubber-degrading bacteria and genes involved.Archives of microbiology · 2024Article
- Computational investigation of cis-1,4-polyisoprene binding to the latex-clearing protein LcpK30.PloS one · 2024Article
- Genomic insights intoFrontiers in microbiology · 2024Article
- Microbial enzymes will offer limited solutions to the global plastic pollution crisis.Microbial biotechnology · 2023Review
- 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
- Poly-cis-isoprene Degradation by Nocardia sp. BSTN01 Isolated from Industrial Waste.Applied biochemistry and biotechnology · 2022Article
- Rubber Degrading Strains:Polymers · 2021Article
- Microbial Degradation of Rubber: Actinobacteria.Polymers · 2021Review
- 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
- First report of cis-1,4-polyisoprene degradation by Gordonia paraffinivorans.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2019Article
- Rubber oxygenases.Applied microbiology and biotechnology · 2019Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundBiodegradation of rubber (polyisoprene) is initiated by oxidative cleavage of the polyisoprene backbone and is performed either by an extracellular rubber oxygenase (RoxA) from Gram-negative rubber degrading bacteria or by a latex clearing protein (Lcp) secreted by Gram-positive rubber degrading bacteria. Only little is known on the biochemistry of polyisoprene cleavage by Lcp and on the types and functions of the involved cofactors.
resultsA rubber-degrading bacterium was isolated from the effluent of a rubber-processing factory and was taxonomically identified as a Rhodococcus rhodochrous species. A gene of R. rhodochrous RPK1 that coded for a polyisoprene-cleaving latex clearing protein (lcp Rr ) was identified, cloned, expressed in Escherichia coli and purified. Purified LcpRr had a specific activity of 3.1 U/mg at 30 °C and degraded poly(1,4-cis-isoprene) to a mixture of oligoisoprene molecules with terminal keto and aldehyde groups. The pH optimum of LcpRr was higher (pH 8) than for other rubber-cleaving enzymes (≈ pH 7). UVvis spectroscopic analysis of LcpRr revealed a cytochrome-specific absorption spectrum with an additional feature at long wavelengths that has not been observed for any other rubber-cleaving enzyme. The presence of one b-type haem in LcpRr as a co-factor was confirmed by (i) metal analysis, (ii) solvent extraction, (iii) bipyridyl assay and (iv) detection of haem-b specific m/z values via mass-spectrometry.
conclusionsOur data point to substantial differences in the active sites of Lcp proteins obtained from different rubber degrading bacteria.
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