Biodegradation of Natural and Synthetic Rubbers

Steinbüchel, Alexander

doi:10.1002/3527600035.bpol2010

Cited by 24 publications

(18 citation statements)

References 57 publications

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“…It is evident that no rubber mountains raise from the shoulders of our highways or accumulate elsewhere; because rubber does not significantly degrade chemically under the conditions present in the environment efficient biological degradation processes must be present. Accordingly, many studies on isolation of rubber‐degrading micro‐organisms and on investigation of the biodegradation process of rubber materials were published in the past [see ; for reviews see (Linos and Steinbüchel 2001; Rose and Steinbüchel 2005)]. So far, only two polypeptides, namely Lcp from Streptomyces sp.…”

Section: Discussionmentioning

confidence: 99%

Development of a homologous expression system for rubber oxygenase RoxA from Xanthomonas sp.

Hambsch

Schmitt

Jendrossek

2010

Journal of Applied Microbiology

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Aims: Natural rubber (poly‐[cis‐1,4‐isoprene]) can be cleaved into 12‐oxo‐4,8‐dimethyltrideca‐4,8‐diene‐1‐al by rubber oxygenase A (RoxA) isolated from Xanthomonas sp. RoxA is a novel type of dihaem dioxygenase with unknown cleavage mechanism of the rubber carbon backbone. Analysis of mutant RoxA after mutagenesis could be a way to investigate the function of selected amino acids of RoxA during catalysis. Unfortunately, expression of functional RoxA in recombinant Escherichia coli or in recombinant γ‐Proteobacteria such as Pseudomonas putida was not possible in our hands. Therefore, expression of recombinant RoxA in the homologous host, Xanthomonas, was performed. Methods and Results: A transformation system via electroporation was established, and a conjugation system was optimized for Xanthomonas sp. Inactivation of the chromosomal roxA gene by insertional mutagenesis resulted in inability of Xanthomonas sp. to produce active RoxA and to utilize rubber as a sole source of carbon and energy. When an intact copy of roxA was cloned under control of a rhamnose‐inducible promoter in a broad host range vector and was transferred to Xanthomonas sp., high expression levels of functional RoxA in the presence of rhamnose were obtained. Conclusions and Significance and Impact of the Study: Purification of recombinantly expressed RoxA was simplified because of drastically shortened fermentation times and because separation of RoxA from remaining rubber latex particles was not necessary with rhamnose‐induced cultures. About 6 mg purified RoxA were obtained from 1 l of cell‐free culture fluid. Purified recombinant RoxA was highly active and revealed comparable spectral properties as RoxA purified from the wild type. The results of our study are the methodical basis for molecular biological manipulation in Xanthomonas sp. and will simplify investigation into the biochemical mechanisms by which rubber can be biodegraded in the environment by this novel extracellular dihaem dioxygenase RoxA.

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Section: Discussionmentioning

confidence: 99%

Development of a homologous expression system for rubber oxygenase RoxA from Xanthomonas sp.

Hambsch

Schmitt

Jendrossek

2010

Journal of Applied Microbiology

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“…Although we do not have direct experimental evidence so far one might speculate that the 70 kDa protein is involved directly or indirectly in the oxidation of rubber. An extracellular 16 kDa protein has been found in rubbergrown Gordonia polyisoprenivorans culture that had some similarity in the N-terminal amino acid sequence to a dioxygenase [2]. Since all attempts to show any enzyme activity in vitro with cell-free culture £uid of rubber-grown Xanthomonas sp.…”

Section: Analysis Of the Amino Acid Sequence Of The 70 Kda Proteinmentioning

confidence: 99%

Sequence analysis of a gene product synthesized byXanthomonassp. during growth on natural rubber latex

Jendrossek

Reinhardt

2003

FEMS Microbiology Letters

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Xanthomonas sp. secretes an extracellular protein (M r W70 þ 5 kDa) during growth on purified natural rubber [poly(1,4-cis-isoprene)] but not during growth on water-soluble carbon sources such as glucose or gluconate. A 1.3 kbp DNA fragment coding for an internal part of the structural gene of the 70 kDa protein was amplified by nested polymerase chain reaction (PCR) using amino acid sequence information obtained after Edman degradation of selected trypsin-generated peptides of the purified 70 kDa protein. The PCR product was used as a DNA probe to clone the complete structural gene from genomic DNA of Xanthomonas sp. The sequenced DNA contained a 2037 bp open reading frame which coded for a polypeptide of 678 amino acids (M r 74.6 kDa) and which included the features of the N-terminal signal peptidase cleavage site (M r W72.9 kDa for the mature protein). Analysis of the amino acid sequence revealed the presence of two heme binding motifs (CXXCH) and a W20 amino acids long sequence that is conserved in the Paracoccus denitrificans and Pseudomonas aeruginosa diheme cytochrome c peroxidases (CCPs). This region includes a histidine residue (H 519 in Xanthomonas sp. and H 265 and H 271 in the Pseudomonas strains, respectively) that is essential for activity in CCPs and that is also conserved in other bacterial oxidases. Blast analysis confirmed the relatedness of the 70 kDa protein to heme-containing oxidases and suggested that it is a member of a new family of relatively large (W500 to W1000 amino acids) extracellular proteins with so far unknown function being only far related in amino acid sequence to P. denitrificans and P. aeruginosa CCPs.

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“…(Berekaa et al 2005). Previous studies have also shown that actinomycetes play the most important role in decomposing natural rubber waste materials (Tsuchii and Takeda, 1990;Heisey and Papadatos, 1995;Linos and Steinbüchel, 2001).…”

Section: Introductionmentioning

confidence: 94%

Biodegradation of a blended starch/natural rubber foam biopolymer and rubber gloves by Streptomyces coelicolor CH13

Watcharakul¹,

Umsakul²,

Hodgson³

et al. 2012

Electro Journal of Biotech

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Background:The growing problem of environmental pollution caused by synthetic plastics has led to the search for alternative materials such as biodegradable plastics. Of the biopolymers presently under development, starch/natural rubber is one promising alternative. Several species of bacteria and fungi are capable of degrading natural rubber and many can degrade starch. Results: Streptomyces coelicolor CH13 was isolated from soil according to its ability to produce translucent halos on a mineral salts medium, MSM, supplemented with natural rubber and to degrade starch. Scanning electron microscope studies showed that it colonized the surfaces of strips of a new starch/natural rubber biopolymer and rubber gloves and caused degradation by forming holes, and surface degradation. Starch was completely removed and polyisoprene chains were broken down to produce aldehyde and/or carbonyl groups. After 6 weeks of cultivation with strips of the polymers in MSM, S. coelicolor CH13 reduced the weight of the starch/NR biopolymer by 92% and that of the rubber gloves by 14.3%. Conclusions: This study indicated that this bacterium causes the biodegradation of the new biopolymer and natural rubber and confirms that this new biopolymer can be degraded in the environment and would be suitable as a 'green plastic' derived from natural sources.

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Biodegradation of Natural and Synthetic Rubbers

Abstract: Introduction Historical Outline General Considerations Early Investigations on the Biodegradation of Natural Rubber Biodegradation of Rubber Pipe Joint Rings Degradation by Fungi Recent Developments Investigations in the Authors' Laboratory … Show more

Cited by 24 publications

References 57 publications

Development of a homologous expression system for rubber oxygenase RoxA from Xanthomonas sp.

Development of a homologous expression system for rubber oxygenase RoxA from Xanthomonas sp.

Sequence analysis of a gene product synthesized byXanthomonassp. during growth on natural rubber latex

Biodegradation of a blended starch/natural rubber foam biopolymer and rubber gloves by Streptomyces coelicolor CH13

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