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High-throughput screening for a moderately halophilic phenol-degrading strain and its salt tolerance response.

Lu ZY, Guo XJ, Li H, Huang ZZ, Lin KF, Liu YD - Int J Mol Sci (2015)

Bottom Line: Bacterial enrichments were cultivated in 48 deep well microplates instead of shake flasks or tubes.Measurement of phenol concentrations was performed in 96-well microplates instead of using the conventional spectrophotometric method or high-performance liquid chromatography (HPLC).PCR detection of the functional genes suggested that the largest subunit of multicomponent phenol hydroxylase (LmPH) and catechol 1,2-dioxygenase (C12O) were active in the phenol degradation process.

View Article: PubMed Central - PubMed

Affiliation: State Environmental Protection Key Laboratory of Environmental Risk Assessment and Control on Chemical Process, School of Resources and Environmental Engineering, East China University of Science and Technology, Shanghai 200237, China. lzy1009a@163.com.

ABSTRACT
A high-throughput screening system for moderately halophilic phenol-degrading bacteria from various habitats was developed to replace the conventional strain screening owing to its high efficiency. Bacterial enrichments were cultivated in 48 deep well microplates instead of shake flasks or tubes. Measurement of phenol concentrations was performed in 96-well microplates instead of using the conventional spectrophotometric method or high-performance liquid chromatography (HPLC). The high-throughput screening system was used to cultivate forty-three bacterial enrichments and gained a halophilic bacterial community E3 with the best phenol-degrading capability. Halomonas sp. strain 4-5 was isolated from the E3 community. Strain 4-5 was able to degrade more than 94% of the phenol (500 mg · L(-1) starting concentration) over a range of 3%-10% NaCl. Additionally, the strain accumulated the compatible solute, ectoine, with increasing salt concentrations. PCR detection of the functional genes suggested that the largest subunit of multicomponent phenol hydroxylase (LmPH) and catechol 1,2-dioxygenase (C12O) were active in the phenol degradation process.

No MeSH data available.


Related in: MedlinePlus

HPLC profile of phenol degradation by Halomonas sp. strain 4-5 at 10% (w/v) NaCl.
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ijms-16-11834-f007: HPLC profile of phenol degradation by Halomonas sp. strain 4-5 at 10% (w/v) NaCl.

Mentions: Studies of the phenol metabolic pathway focused mainly on the examination of the degradation intermediates and the detection of functional genes. HPLC was utilized to examine the intermediate products during the phenol degradation process. Figure 7 showed the degradation of phenol by Halomonas sp. strain 4-5 at 24-h time intervals. The residence times of Peak 4 and Peak 5 were 4.110 and 6.142 min, respectively. Compared with the retention time of the standard substances, Peak 4 and Peak 5 represented catechol and phenol. The HPLC profile showed that catechol was the metabolism intermediate product, indicating that degradation of phenol occurred via the catechol degradation pathway [28].


High-throughput screening for a moderately halophilic phenol-degrading strain and its salt tolerance response.

Lu ZY, Guo XJ, Li H, Huang ZZ, Lin KF, Liu YD - Int J Mol Sci (2015)

HPLC profile of phenol degradation by Halomonas sp. strain 4-5 at 10% (w/v) NaCl.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4490417&req=5

ijms-16-11834-f007: HPLC profile of phenol degradation by Halomonas sp. strain 4-5 at 10% (w/v) NaCl.
Mentions: Studies of the phenol metabolic pathway focused mainly on the examination of the degradation intermediates and the detection of functional genes. HPLC was utilized to examine the intermediate products during the phenol degradation process. Figure 7 showed the degradation of phenol by Halomonas sp. strain 4-5 at 24-h time intervals. The residence times of Peak 4 and Peak 5 were 4.110 and 6.142 min, respectively. Compared with the retention time of the standard substances, Peak 4 and Peak 5 represented catechol and phenol. The HPLC profile showed that catechol was the metabolism intermediate product, indicating that degradation of phenol occurred via the catechol degradation pathway [28].

Bottom Line: Bacterial enrichments were cultivated in 48 deep well microplates instead of shake flasks or tubes.Measurement of phenol concentrations was performed in 96-well microplates instead of using the conventional spectrophotometric method or high-performance liquid chromatography (HPLC).PCR detection of the functional genes suggested that the largest subunit of multicomponent phenol hydroxylase (LmPH) and catechol 1,2-dioxygenase (C12O) were active in the phenol degradation process.

View Article: PubMed Central - PubMed

Affiliation: State Environmental Protection Key Laboratory of Environmental Risk Assessment and Control on Chemical Process, School of Resources and Environmental Engineering, East China University of Science and Technology, Shanghai 200237, China. lzy1009a@163.com.

ABSTRACT
A high-throughput screening system for moderately halophilic phenol-degrading bacteria from various habitats was developed to replace the conventional strain screening owing to its high efficiency. Bacterial enrichments were cultivated in 48 deep well microplates instead of shake flasks or tubes. Measurement of phenol concentrations was performed in 96-well microplates instead of using the conventional spectrophotometric method or high-performance liquid chromatography (HPLC). The high-throughput screening system was used to cultivate forty-three bacterial enrichments and gained a halophilic bacterial community E3 with the best phenol-degrading capability. Halomonas sp. strain 4-5 was isolated from the E3 community. Strain 4-5 was able to degrade more than 94% of the phenol (500 mg · L(-1) starting concentration) over a range of 3%-10% NaCl. Additionally, the strain accumulated the compatible solute, ectoine, with increasing salt concentrations. PCR detection of the functional genes suggested that the largest subunit of multicomponent phenol hydroxylase (LmPH) and catechol 1,2-dioxygenase (C12O) were active in the phenol degradation process.

No MeSH data available.


Related in: MedlinePlus