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Related Experiment Video

Updated: Jan 20, 2026

Capsular Serotyping of Streptococcus pneumoniae by Latex Agglutination
09:11

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Published on: September 25, 2014

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Solimonas fluminis has an active latex-clearing protein.

Jakob Birke1,2, Dieter Jendrossek3

  • 1Institute of Microbiology, University of Stuttgart, Allmandring 31, 70569, Stuttgart, Germany.

Applied Microbiology and Biotechnology
|September 6, 2019
PubMed
Summary

This study reveals that Gram-negative bacteria can utilize latex-clearing proteins (Lcps) as rubber oxygenases, breaking down polyisoprene. This finding expands our understanding of rubber biodegradation pathways.

Keywords:
BiodegradationHaem dioxygenaseLatex-clearing proteinPolyisopreneRubber oxygenase

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Area of Science:

  • Microbiology
  • Biochemistry
  • Polymer Science

Background:

  • Rubber-degrading bacteria use rubber oxygenases to break down polyisoprene for carbon.
  • Gram-negative bacteria typically use RoxA/RoxB, while Gram-positive bacteria use Lcp proteins.

Purpose of the Study:

  • To investigate the presence and function of Lcp-type rubber oxygenases in Gram-negative bacteria.
  • To characterize the biochemical activity and properties of an Lcp protein from Solimonas fluminis.

Main Methods:

  • Identification and cloning of an lcp orthologue from Solimonas fluminis.
  • Heterologous expression and purification of the Lcp protein (LcpHR-BB) in E. coli.
  • Biochemical assays and spectroscopic analysis to determine enzyme activity and structure.

Main Results:

  • LcpHR-BB from S. fluminis successfully cleaved polyisoprene into C20 and higher oligoisoprenoids.
  • The enzyme exhibited a specific activity of 1.5 U/mg.
  • Spectroscopic data identified LcpHR-BB as a b-haem-containing protein with an open haem center.

Conclusions:

  • This is the first report of an active Lcp-type rubber oxygenase in a Gram-negative bacterium.
  • The findings suggest a broader diversity of rubber-degrading mechanisms than previously known.