Dataset Information

Biodegradation of Phenol by Rhodococcus sp. Strain SKC: Characterization and Kinetics Study.

ABSTRACT: This study focuses on the kinetics of a pure strain of bacterium Rhodococcus sp. SKC, isolated from phenol-contaminated soil, for the biodegradation of phenol as its sole carbon and energy source in aqueous medium. The kinetics of phenol biodegradation including the lag phase, the maximum phenol degradation rate, maximum growth rate (Rm) and maximum yield coefficient (Y) for each Si (initial phenol concentration, mg/L) were fitted using the Gompertz and Haldane models of substrate inhibition (R2 > 0.9904, RMSE < 0.00925). The values of these parameters at optimum conditions were μmax = 0.30 h-1, Ks = 36.40 mg/L, and Ki = 418.79 mg/L, and that means the inhibition concentration of phenol was 418.79 mg/L. By comparing with other strains of bacteria, Rhodococcus sp. SKC exhibited a high yield factor and tolerance towards phenol. This study demonstrates the potential application of Rhodococcus sp. SKC for the bioremediation of phenol contaminate.

SUBMITTER: Wen Y

PROVIDER: S-EPMC7463884 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature

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Biodegradation of Phenol by Rhodococcus sp. Strain SKC: Characterization and Kinetics Study.

Wen Yujuan Y Li Chaofan C Song Xiaoming X Yang Yuesuo Y

Molecules (Basel, Switzerland) 20200812 16

This study focuses on the kinetics of a pure strain of bacterium Rhodococcus sp. SKC, isolated from phenol-contaminated soil, for the biodegradation of phenol as its sole carbon and energy source in aqueous medium. The kinetics of phenol biodegradation including the lag phase, the maximum phenol degradation rate, maximum growth rate (Rm) and maximum yield coefficient (Y) for each Si (initial phenol concentration, mg/L) were fitted using the Gompertz and ...[more]

PMID: 32806514

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Project description:Isoprene (2-methyl-1,3-butadiene) is a climate-active gas released to the atmosphere in large quantities, comparable to methane in magnitude. Several bacteria have been isolated which can grow on isoprene as a sole carbon and energy source, but very little information is available about the degradation of isoprene by these bacteria at the biochemical level. Isoprene utilization is dependent on a multistep pathway, with the first step being the oxidation of isoprene to epoxy-isoprene. This is catalyzed by a four-component soluble diiron monooxygenase, isoprene monooxygenase (IsoMO). IsoMO is a six-protein complex comprising an oxygenase (IsoABE), containing the di-iron active site, a Rieske-type ferredoxin (IsoC), a NADH reductase (IsoF), and a coupling/effector protein (IsoD), homologous to the soluble methane monooxygenase and alkene/aromatic monooxygenases. Here, we describe the purification of the IsoMO components from Rhodococcus sp. AD45 and reconstitution of isoprene-oxidation activity in vitro. Some IsoMO components were expressed and purified from the homologous host Rhodococcus sp. AD45-ID, a Rhodococcus sp. AD45 strain lacking the megaplasmid which contains the isoprene metabolic gene cluster. Others were expressed in Escherichia coli and purified as fusion proteins. We describe the characterization of these purified components and demonstrate their activity when combined with Rhodococcus sp. AD45 cell lysate. Demonstration of IsoMO activity in vitro provides a platform for further biochemical and biophysical characterization of this novel soluble diiron center monooxygenase, facilitating new insights into the enzymatic basis for the bacterial degradation of isoprene. IMPORTANCE Isoprene is a highly abundant climate-active gas and a carbon source for some bacteria. Analyses of the genes encoding isoprene monooxygenase (IsoMO) indicate this enzyme is a soluble diiron center monooxygenase in the same family of oxygenases as soluble methane monooxygenase, alkene monooxygenase, and toluene monooxygenase. We report the initial biochemical characterization of IsoMO from Rhodococcus, the first from any bacterium, describing the challenging purification and reconstitution of in vitro activity of its four components. This study lays the foundation for future detailed mechanistic studies of IsoMO, a key enzyme in the global isoprene cycle.

Dataset Information

Biodegradation of Phenol by Rhodococcus sp. Strain SKC: Characterization and Kinetics Study.

Publications

Biodegradation of Phenol by <i>Rhodococcus</i> sp. Strain SKC: Characterization and Kinetics Study.

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