Characterization of Aniline Degradation by A Previously Isolated Molybdenum-reducing Pseudomonas sp.

Microorganisms play an integral role in detoxification and removal of toxic compounds from the environment. Aniline is the simplest aromatic amine, consisting of a phenyl group attached to an amino group that is used as herbicide to control weeds. Aniline is detrimental to both environment and health. In this research, six previously isolated bacteria (isolate A-F) were screened on Bushnell Hass media for their potential to grow and utilize aniline as a sole carbon source. Isolate A (Pseudomonas sp.) was found to tolerate and grow best with aniline sole source of carbon. Optimum conditions for aniline degradation by this isolate were found to be pH 6.0, temperature between 30 and 37 °C, inoculums size of 600 μL, aniline concentration of 200 mg/L and incubation time of 96 h. The capacity of this isolate to reduce toxic aniline to less toxic form is novel and makes the bacterium important instrument for bioremediation of this pollutant.

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Characterization of Morganella sp. for its Paraquat Degradation Potential

Asian Journal of Plant Biology ◽

10.54987/ajpb.v3i2.636 ◽

2021 ◽

Vol 3 (2) ◽

pp. 12-16

Author(s):

S.D. Haruna ◽

A.J. Sufyan ◽

S. Ibrahim ◽

A. Babandi ◽

D. Shehu ◽

...

Keyword(s):

Carbon Source ◽

Sole Carbon Source ◽

Microbial Population ◽

Culture Collection ◽

Inoculum Size ◽

Optimum Conditions ◽

Toxic Compounds ◽

Characterization Study ◽

Agar Media

One of the beneficial roles of the microbial population is their ability to convert toxic herbicides to lesser toxic compounds such as water and carbon (IV) oxide. Paraquat which is an acutely toxic herbicide is used on farmlands and has been found to affect human health. This study was aimed at characterizing bacteria with the potential to degrade paraquat. Previously isolated bacteria from culture collection labelled A-F were screened for their potential to degrade and utilized paraquat as the sole carbon source in Bushnell Hass agar media. Of the six isolates, isolate E (Morganella sp.) was observed to have the highest growth and tolerance to paraquat after 72 h of incubation at 37 ºC. Characterization study revealed that Morganella sp. can utilize and grow with optimum conditions of pH 6.5, the temperature of 30 ºC and can tolerate up to 400 mg/L paraquat concentration with an increase in growth as inoculum size increases. Thus, these findings showed that Morganella sp. can degrade toxic paraquat to a less toxic form and therefore can be a good isolate for the future bioremediation process of the pollutant.

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Biodegradation of malathion by Bacillus licheniformis strain ML-1

Archives of Biological Sciences ◽

10.2298/abs141218007k ◽

2016 ◽

Vol 68 (1) ◽

pp. 51-59 ◽

Cited By ~ 15

Author(s):

Sara Khan ◽

Habiba Zaffar ◽

Usman Irshad ◽

Raza Ahmad ◽

Abdul Khan ◽

...

Keyword(s):

Carbon Source ◽

Bacillus Licheniformis ◽

Sole Carbon Source ◽

Sole Source ◽

Minimal Salt Medium ◽

Organophosphate Pesticide ◽

Soil Enrichment ◽

Enrichment Technique ◽

Malathion Carboxylesterase

Malathion, a well-known organophosphate pesticide, has been used in agriculture over the last two decades for controlling pests of economically important crops. In the present study, a single bacterium, ML-1, was isolated by soil-enrichment technique and identified as Bacillus licheniformis on the basis of the 16S rRNA technique. The bacterium was grown in carbon-free minimal salt medium (MSM) and was found to be very efficient in utilizing malathion as the sole source of carbon. Biodegradation experiments were performed in MSM without carbon source to determine the malathion degradation by the selected strain, and the residues of malathion were determined quantitatively using HPLC techniques. Bacillus licheniformis showed very promising results and efficiently consumed malathion as the sole carbon source via malathion carboxylesterase (MCE), and about 78% malathion was degraded within 5 days. The carboxylesterase activity was determined by using crude extract while using malathion as substrate, and the residues were determined by HPLC. It has been found that the MCE hydrolyzed 87% malathion within 96 h of incubation. Characterization of crude MCE revealed that the enzyme is robust in nature in terms of organic solvents, as it was found to be stable in various concentrations of ethanol and acetonitrile. Similarly, and it can work in a wide pH and temperature range. The results of this study highlighted the potential of Bacillus licheniformis strain ML-1 as a biodegrader that can be used for the bioremediation of malathion-contaminated soil.

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Isolation and characterization of aPseudomonassp. strain PH1 utilizing meta-aminophenol

Canadian Journal of Microbiology ◽

10.1139/w99-132 ◽

2000 ◽

Vol 46 (3) ◽

pp. 211-217 ◽

Cited By ~ 15

Author(s):

Razia Kutty ◽

Hemant J Purohit ◽

Purushottam Khanna

Keyword(s):

Nitrogen Source ◽

16S Rdna ◽

Sole Source ◽

Rdna Sequence ◽

Pseudomonas Sp ◽

16S Rdna Sequence ◽

Industry Waste ◽

Isolation And Characterization ◽

Dye Industry

Pseudomonas sp. strain PH1 was isolated from soil contaminated with pharmaceutical and dye industry waste. The isolate PH1 could use m-aminophenol as a sole source of carbon, nitrogen, and energy to support the growth. PH1 could degrade up to 0.32 mM m-aminophenol in 120 h, when provided as nitrogen source at 0.4 mM concentration with citrate (0.5 mM) as a carbon source in the growth medium. The presence of ammonium chloride as an additional nitrogen source repressed the degradation of m-aminophenol by PH1. To identify strain PH1, the 16S rDNA sequence was amplified by PCR using conserved eubacterial primers. The FASTA program was used to analyze the 16S rDNA sequence and the resulting homology patterns suggested that PH1 is a Pseudomonas.Key words: m-aminophenol, resorcinol, DNA sequencing.

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Characterization of some naphthalene using bacteria isolated from contaminated Cooum Riverine sediment of the Bay of Bengal (India)

Journal of the Serbian Chemical Society ◽

10.2298/jsc180724088r ◽

2019 ◽

Vol 84 (2) ◽

pp. 225-236

Author(s):

Sancho Rajan ◽

Anwesha Pattanaik ◽

Venkatesh Kumaresan ◽

Prasanth Bhatt ◽

Senthilarasu Gunasekaran ◽

...

Keyword(s):

16S Rdna ◽

Bay Of Bengal ◽

Morphological Characteristics ◽

Sole Source ◽

Pseudomonas Sp ◽

16S Rdna Sequencing ◽

Naphthalene Degradation ◽

Rdna Sequencing ◽

Riverine Sediment

Microorganisms capable of using naphthalene as the sole carbon source were isolated from the contaminated sediment of Cooum River. Twenty one isolates were recovered and nine were selected for enrichment due to differences in their morphological characteristics. Out of nine isolates, only four (NS3-SRMND14B, NS14-SRMND14A, NS15-SRMND14D and NS19- -SRMND14E) were capable of completely utilizing naphthalene as the sole source of carbon in carbon free minimal medium (CFMM) supplemented with naphthalene. 16S rDNA sequencing showed that all the four isolates were distantly related to each other and belongs to Bacillus sp. (NS3-SRMND14B), Pseudomonas sp. (NS14-SRMND14A), Cellulosimicrobium sp. (NS15-SRMND14D) and Sphingobacterium sp. (NS19-SRMND14E), respectively. Based on the phylogenetic analysis of 16S rDNA sequencing, the isolate Sphingobacterium sp. (NS19-SRMND14E) has been identified as novel strain. Polymerase chain reaction (PCR) technique showed the presence of naphthalene dioxygenase (ndo) gene responsible for naphthalene degradation only in the Pseudomonas sp. (NS14-SRMND14A). We observed that the ndo gene is not the only gene responsible for naphthalene degradation. Based on our study, the indigenous microorganisms isolated from Cooum Riverine sediment can be used for bioremediation of the polluted sediment along the Bay of Bengal.

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Pandrug-resistant Pseudomonas sp. expresses New Delhi metallo-β-lactamase-1 and consumes ampicillin as sole carbon source

Clinical Microbiology and Infection ◽

10.1016/j.cmi.2020.10.032 ◽

2020 ◽

Author(s):

Vivek Kumar Ranjan ◽

Shriparna Mukherjee ◽

Subarna Thakur ◽

Krutika Gupta ◽

Ranadhir Chakraborty

Keyword(s):

Carbon Source ◽

Sole Carbon Source ◽

New Delhi ◽

Pseudomonas Sp

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Isolation and characterization of a novel rhamnolipid producer Pseudomonas sp. LGMS7 from a highly contaminated site in Ain El Arbaa region of Ain Temouchent, Algeria

3 Biotech ◽

10.1007/s13205-021-02751-6 ◽

2021 ◽

Vol 11 (4) ◽

Author(s):

Abdelkrim Chaida ◽

Alif Chebbi ◽

Farid Bensalah ◽

Andrea Franzetti

Keyword(s):

Contaminated Site ◽

Pseudomonas Sp ◽

Isolation And Characterization

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Mucopolysaccharidases from Pseudomonas sp.. Isolation and partial characterization of constitutive enzymes involved in the degradation of keratan sulfate and chondroitin sulfate

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1986.tb10134.x ◽

1986 ◽

Vol 161 (1) ◽

pp. 139-147 ◽

Cited By ~ 6

Author(s):

Denise S. P. Q. HORTON ◽

Yara M. MICHELACCI

Keyword(s):

Chondroitin Sulfate ◽

Keratan Sulfate ◽

Partial Characterization ◽

Pseudomonas Sp

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Crystal structure of thermostable alkylsulfatase SdsAP from Pseudomonas sp. S9

Bioscience Reports ◽

10.1042/bsr20170001 ◽

2017 ◽

Vol 37 (3) ◽

Author(s):

Lifang Sun ◽

Pu Chen ◽

Yintao Su ◽

Zhixiong Cai ◽

Lingwei Ruan ◽

...

Keyword(s):

Crystal Structure ◽

Sodium Dodecyl ◽

Titration Calorimetry ◽

Pseudomonas Sp ◽

Sterol Carrier Protein ◽

Dimerization Domain ◽

Alkyl Chains ◽

Hydrolysis Of

A novel alkylsulfatase from bacterium Pseudomonas sp. S9 (SdsAP) was identified as a thermostable alkylsulfatases (type III), which could hydrolyze the primary alkyl sulfate such as sodium dodecyl sulfate (SDS). Thus, it has a potential application of SDS biodegradation. The crystal structure of SdsAP has been solved to a resolution of 1.76 Å and reveals that SdsAP contains the characteristic metallo-β-lactamase-like fold domain, dimerization domain, and C-terminal sterol carrier protein type 2 (SCP-2)-like fold domain. Kinetic characterization of SdsAP to SDS by isothermal titration calorimetry (ITC) and enzymatic activity assays of constructed mutants demonstrate that Y246 and G263 are important residues for its preference for the hydrolysis of ‘primary alkyl’ chains, confirming that SdsAP is a primary alkylsulfatase.

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