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Rhodococcus jostii RHA1 is an oleaginous bacterium that has attracted considerable attention due to its capacity to use different carbon sources to accumulate significant levels of triacylglycerols that might be converted into biofuels. However, this strain cannot transform xylose into lipids reducing its potential when growing on saccharified lignocellulosic biomass. In this work, we demonstrate that wild type R. jostii RHA1 can be evolved by adaptive laboratory evolution (ALE) to metabolize xylose without engineering heterologous metabolic pathways in the host. We have generated a phenotypically adapted ALE-xyl strain able to use xylose as the sole carbon and energy source more efficiently that an engineered recombinant strain harbouring heterologous xylA and xylB genes encoding a xylose isomerase metabolic pathway. The R. jostii RHA1 ALE-xyl strain accumulates lipids very efficiently using xylose as substrate, but even more importantly it can consume glucose and xylose at the same time. Transcriptomic analyses of ALE-xyl strain growing with glucose or xylose revealed the existence of a silent pentose metabolizing operon that is overexpressed in the presence of xylose. The detection of a xylose reductase activity together with the presence of xylitol in the cytoplasm of ALE-xyl strain suggests that xylose is consumed by a reductase pathway. This study demonstrates that, in cases where a clear phenotypic selection method is available, ALE can be used to improve very efficiently industrial microbial strains without using genetic engineering tools. Strategies focused to exploit the silent phenotypic flexibility of microorganisms to metabolize different carbon sources are powerful tools for the production of microbial value-added products using saccharified lignocellulosic wastes.
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http://dx.doi.org/10.1186/s13036-025-00503-1 | DOI Listing |
Enzyme Microb Technol
December 2025
Environmental Technology Unit, Industrial Technology Institute, 363 Bauddhaloka Mawatha, Colombo 00700, Sri Lanka. Electronic address:
Poly and per fluorinated substances (PFAS) are emerging contaminants of concern that are thought to be involved in causing numerous adverse health effects, such as immunosuppression, increased chance of cancer development, and altered levels of hepatic enzyme levels in humans. However, PFAS are considered highly persistent and resistant to biodegradation given the fact that the C-F bond can have a bond dissociation energy of up to 544 kJ/mol. Though many studies have reported PFAS biodefluorination by bacterial isolates and microbial communities, little is known regarding the molecular foundations for biodefluorination.
View Article and Find Full Text PDFFront Microbiol
June 2025
Department of Biotechnology, Centro de Investigaciones Biológicas Margarita Salas, Consejo Superior de Investigaciones Científicas (CSIC), Madrid, Spain.
By exploring the use of plasmids to confer RHA1 the possibility of utilizing xylose to produce lipids we have observed that the plasmid used was not always maintained in the transformants as expected. Instead, we observed an illegitimate integration of the antibiotic resistance gene from the plasmid into the recombinant cells. Genome sequencing of the transformants has provided evidence that this illegitimate integration is not size-, site-or sequence-specific.
View Article and Find Full Text PDFMethods Enzymol
June 2025
Department of Chemistry, University of Warwick, Coventry CV4 7AL, United Kingdom.
Accessory enzymes have been identified in lignin-degrading fungi and bacteria that can generate hydrogen peroxide, which is used as a co-substrate by lignin-oxidising peroxidases. This article describes a glycolate oxidase enzyme from lignin-degrading bacterium Rhodococcus jostii RHA1, which functions as an efficient accessory enzyme for degradation of polymeric lignin substrates by bacterial DyP-type peroxidases. The article describes: (1) enzyme purification; (2) assays for enzyme activity; (3) analysis of substrate specificity; (4) assays for enzyme combinations with bacterial DyP-type peroxidases; (5) analysis of low molecular weight products obtained using enzyme combinations.
View Article and Find Full Text PDFJ Biol Eng
April 2025
Department of Biotechnology, Centro de Investigaciones Biológicas Margarita Salas, Consejo Superior de Investigaciones Científicas (CSIC), Madrid, Spain.
Rhodococcus jostii RHA1 is an oleaginous bacterium that has attracted considerable attention due to its capacity to use different carbon sources to accumulate significant levels of triacylglycerols that might be converted into biofuels. However, this strain cannot transform xylose into lipids reducing its potential when growing on saccharified lignocellulosic biomass. In this work, we demonstrate that wild type R.
View Article and Find Full Text PDFJ Biol Chem
November 2024
Department of Microbiology and Immunology, Life Sciences Institute and Bioproducts Institute, The University of British Columbia, Vancouver, Canada. Electronic address:
Cytochromes P450 (P450s) are a superfamily of heme-containing enzymes possessing a broad range of monooxygenase activities. One such activity is O-demethylation, an essential and rate-determining step in emerging strategies to valorize lignin that employ carbon-carbon bond cleavage. We recently identified PbdA, a P450 from Rhodococcus jostii RHA1, and PbdB, its cognate reductase, which catalyze the O-demethylation of para-methoxylated benzoates (p-MBAs) to initiate growth of RHA1 on these compounds.
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