Characterization and functional expression of a rubber degradation gene of a Nocardia degrader from a rubber-processing factory

A rubber-degrading bacterial consortium named H2DA was obtained from an enrichment culture with natural rubber latex and rubber-processing factory waste in Vietnam. Gel permeation chromatography analysis revealed that only the strain NVL3 degraded synthetic poly(cis-1,4-isoprene) into low-molecular-...

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Published in:Journal of bioscience and bioengineering 2017-04, Vol.123 (4), p.412-418
Main Authors: Linh, Dao Viet, Huong, Nguyen Lan, Tabata, Michiro, Imai, Shunsuke, Iijima, Sou, Kasai, Daisuke, Anh, To Kim, Fukuda, Masao
Format: Article
Language:English
Subjects:
Aldehydes - chemistry
Aldehydes - metabolism
Base Sequence
Degradation
Escherichia coli - genetics
Functional expression
Genes, Bacterial - genetics
Hemiterpenes - chemistry
Hemiterpenes - metabolism
Industry
Latex - chemistry
Latex - metabolism
Latex-clearing protein
Nocardia
Nocardia - classification
Nocardia - genetics
Nocardia - metabolism
Rubber
Rubber - chemistry
Rubber - metabolism
Vietnam
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Summary:A rubber-degrading bacterial consortium named H2DA was obtained from an enrichment culture with natural rubber latex and rubber-processing factory waste in Vietnam. Gel permeation chromatography analysis revealed that only the strain NVL3 degraded synthetic poly(cis-1,4-isoprene) into low-molecular-weight intermediates among the three strains found in the H2DA. The 16S-rRNA gene sequence of NVL3 showed the highest identity with that of Nocardia farcinica DSM 43665T. NVL3 accumulated aldehyde intermediates from synthetic poly(cis-1,4-isoprene) on a rubber-overlay plate as indicated by Schiff's staining. NVL3 also degraded deproteinized natural rubber into low-molecular-weight aldehyde intermediates. A latex-clearing protein (lcp) gene ortholog was identified within the genome sequence of NVL3, and it showed a moderate amino-acid identity (54–75%) with the lcp genes from previously reported rubber degraders. The heterologous expression of the NVL3 lcp in Escherichia coli BL21(DE3) allowed us to purify the 46.8-kDa His-tagged lcp gene product (His-Lcp). His-Lcp degraded synthetic poly(cis-1,4-isoprene) and accumulated aldehyde intermediates from deproteinized natural rubber suggesting the functional expression of the lcp gene from a Nocardia degrader in E. coli. Quantitative reverse transcription PCR analysis indicated the strong transcriptional induction of the lcp gene in NVL3 in the presence of synthetic poly(cis-1,4-isoprene). These results suggest the involvement of the lcp gene in rubber degradation in NVL3.
ISSN:1389-1723
1347-4421
DOI:10.1016/j.jbiosc.2016.11.012