Microbial Degradation Mechanism of Textile Dye and Its Metabolic Pathway for Environmental Safety

2016 ◽  
pp. 413-454 ◽  
Keyword(s):  
Microbial Degradation ◽  
Metabolic Pathway ◽  
Degradation Mechanism ◽  
Environmental Safety ◽  
Textile Dye

Microbial Degradation Mechanism and Pathway of the Novel Insecticide Paichongding by a Newly Isolated Sphingobacterium sp. P1-3 from Soil

2015 ◽  
Vol 63 (15) ◽  
pp. 3823-3829 ◽  
Author(s):  
Zhiqiang Cai ◽  
Wenjie Zhang ◽  
Shanshan Li ◽  
Jiangtao Ma ◽  
Jing Wang ◽  
...  
Keyword(s):  
Microbial Degradation ◽  
Degradation Mechanism ◽  
The Novel

Microbial degradation and metabolic pathway of pyridine by a Paracoccus sp. strain BW001

2008 ◽  
Vol 19 (6) ◽  
pp. 915-926 ◽  
Author(s):  
Yaohui Bai ◽  
Qinghua Sun ◽  
Cui Zhao ◽  
Donghui Wen ◽  
Xiaoyan Tang
Keyword(s):  
Microbial Degradation ◽  
Metabolic Pathway

scholarly journals Removal of Hydrophobic Contaminants from the Soil by Adsorption onto Carbon Materials and Microbial Degradation

2021 ◽  
Vol 7 (4) ◽  
pp. 83
Author(s):  
Shippi Dewangan ◽  
Amarpreet K. Bhatia ◽  
Ajaya Kumar Singh ◽  
Sónia A. C. Carabineiro
Keyword(s):  
Microbial Degradation ◽  
Organic Contaminants ◽  
Raw Materials ◽  
Low Cost ◽  
Environmental Safety ◽  
Hydrophobic Organic Contaminants ◽  
Adsorption Mechanisms ◽  
Environmental Treatment ◽  
Sufficient Food ◽  
Practicable Method

The pollution of soil is a worldwide concern as it has harmful consequences on the environment and human health. With the continuous expansion of industry and agriculture, the content of hydrophobic organic pollutants in the soil has been increasing, which has caused serious pollution to the soil. The removal of hydrophobic organic contaminants from soil, aiming to recover environmental safety, is an urgent matter to guarantee sufficient food and water for populations. Adsorption has proven to be an effective and economically practicable method for removing organic contaminants. This paper summarizes the use of low-cost adsorbents, such as biochar and activated carbon, for removing hydrophobic organic contaminants from soil. Biochar is usually appropriate for the adsorption of organic contaminants via the adsorption mechanisms of electrostatic interaction, precipitation, and ion exchange. Biochar also has numerous benefits, such as being obtained from several kinds of raw materials, having low costs, recyclability, and potential for environmental treatment. This paper illustrates biochar’s adsorption mechanism for organic contaminants and discusses the microbial degradation of hydrophobic organic contaminants.

Microbial degradation mechanism of pyridine by Paracoccus sp. NJUST30 newly isolated from aerobic granules

2018 ◽  
Vol 344 ◽  
pp. 86-94 ◽  
Author(s):  
Jing Wang ◽  
Xinbai Jiang ◽  
Xiaodong Liu ◽  
Xiuyun Sun ◽  
Weiqing Han ◽  
...  
Keyword(s):  
Microbial Degradation ◽  
Degradation Mechanism ◽  
Aerobic Granules

scholarly journals Metabolic Pathway Involved in 6-Chloro-2-Benzoxazolinone Degradation by Pigmentiphaga sp. Strain DL-8 and Identification of the Novel Metal-Dependent Hydrolase CbaA

2016 ◽  
Vol 82 (14) ◽  
pp. 4169-4179 ◽  
Author(s):  
Weiliang Dong ◽  
Fei Wang ◽  
Fei Huang ◽  
Yicheng Wang ◽  
Jie Zhou ◽  
...  
Keyword(s):  
Metabolic Pathway ◽  
Specific Activity ◽  
Degradation Mechanism ◽  
Draft Genome ◽  
Proton Donor ◽  
Binding Motif ◽  
Resting Cells ◽  
Content Type ◽  
Peptide Mass ◽  
Donor And Acceptor

ABSTRACT6-Chloro-2-benzoxazolinone (CDHB) is a precursor of herbicide, insecticide, and fungicide synthesis and has a broad spectrum of biological activity.Pigmentiphagasp. strain DL-8 can transform CDHB into 2-amino-5-chlorophenol (2A5CP), which it then utilizes as a carbon source for growth. The CDHB hydrolase (CbaA) was purified from strain DL-8, which can also hydrolyze 2-benzoxazolinone (BOA), 5-chloro-2-BOA, and benzamide. The specific activity of purified CbaA was 5,900 U · mg protein−1for CDHB, withKmandkcatvalues of 0.29 mM and 8,500 s−1, respectively. The optimal pH for purified CbaA was 9.0, the highest activity was observed at 55°C, and the inactive metal-free enzyme could be reactivated by Mg2+, Ni2+, Ca2+, or Zn2+. Based on the results obtained for the CbaA peptide mass fingerprinting and draft genome sequence of strain DL-8,cbaA(encoding 339 amino acids) was cloned and expressed inEscherichia coliBL21(DE3). CbaA shared 18 to 21% identity with some metal-dependent hydrolases of the PF01499 family and contained the signature metal-binding motif Q127XXXQ131XD133XXXH137. The conserved amino acid residues His288 and Glu301 served as the proton donor and acceptor.E. coliBL21(DE3-pET-cbaA) resting cells could transform 0.2 mM CDHB into 2A5CP. The mutant strain DL-8ΔcbaAlost the ability to degrade CDHB but retained the ability to degrade 2A5CP, consistent with strain DL-8. These results indicated thatcbaAwas the key gene responsible for CDHB degradation by strain DL-8.IMPORTANCE2-Benzoxazolinone (BOA) derivatives are widely used as synthetic intermediates and are also an important group of allelochemicals acting in response to tissue damage or pathogen attack in gramineous plants. However, the degradation mechanism of BOA derivatives by microorganisms is not clear. In the present study, we reported the identification of CbaA and metabolic pathway responsible for the degradation of CDHB inPigmentiphagasp. DL-8. This will provide microorganism and gene resources for the bioremediation of the environmental pollution caused by BOA derivatives.

scholarly journals Further Understanding of Degradation Pathways of Microcystin-LR by an Indigenous Sphingopyxis sp. in Environmentally Relevant Pollution Concentrations

Toxins ◽  
2018 ◽  
Vol 10 (12) ◽  
pp. 536 ◽  
Author(s):  
Qin Ding ◽  
Kaiyan Liu ◽  
Kai Xu ◽  
Rongli Sun ◽  
Juan Zhang ◽  
...  
Keyword(s):  
Microbial Degradation ◽  
Degradation Products ◽  
Lake Taihu ◽  
Environmental Safety ◽  
Degradation Pathways ◽  
Environment Friendly ◽  
Degradation Rates ◽  
Degrading Bacteria ◽  
Full Scan ◽  
Pollution Concentrations

Microcystin-LR (MC-LR) is the most widely distributed microcystin (MC) that is hazardous to environmental safety and public health, due to high toxicity. Microbial degradation is regarded as an effective and environment-friendly method to remove it, however, the performance of MC-degrading bacteria in environmentally relevant pollution concentrations of MC-LR and the degradation pathways remain unclear. In this study, one autochthonous bacterium, Sphingopyxis sp. m6 which exhibited high MC-LR degradation ability, was isolated from Lake Taihu, and the degrading characteristics in environmentally relevant pollution concentrations were demonstrated. In addition, degradation products were identified by utilizing the full scan mode of UPLC-MS/MS. The data illustrated that strain m6 could decompose MC-LR (1–50 μg/L) completely within 4 h. The degradation rates were significantly affected by temperatures, pH and MC-LR concentrations. Moreover, except for the typical degradation products of MC-LR (linearized MC-LR, tetrapeptide, and Adda), there were 8 different products identified, namely, three tripeptides (Adda-Glu-Mdha, Glu-Mdha-Ala, and Leu-MeAsp-Arg), three dipeptides (Glu-Mdha, Mdha-Ala, and MeAsp-Arg) and two amino acids (Leu, and Arg). To our knowledge, this is the first report of Mdha-Ala, MeAsp-Arg, and Leu as MC-LR metabolites. This study expanded microbial degradation pathways of MC-LR, which lays a foundation for exploring degradation mechanisms and eliminating the pollution of microcystins (MCs).

Structures of c-di-GMP/cGAMP degrading phosphodiesterase VcEAL: identification of a novel conformational switch and its implication

2019 ◽  
Vol 476 (21) ◽  
pp. 3333-3353 ◽  
Author(s):  
Malti Yadav ◽  
Kamalendu Pal ◽  
Udayaditya Sen
Keyword(s):  
Active Site ◽  
Metal Binding ◽  
Metal Ion ◽  
Triosephosphate Isomerase ◽  
Catalytic Mechanism ◽  
Degradation Mechanism ◽  
Structural Basis ◽  
Conserved Residues ◽  
Phosphodiester Bond ◽  
Cyclic Dinucleotides

Cyclic dinucleotides (CDNs) have emerged as the central molecules that aid bacteria to adapt and thrive in changing environmental conditions. Therefore, tight regulation of intracellular CDN concentration by counteracting the action of dinucleotide cyclases and phosphodiesterases (PDEs) is critical. Here, we demonstrate that a putative stand-alone EAL domain PDE from Vibrio cholerae (VcEAL) is capable to degrade both the second messenger c-di-GMP and hybrid 3′3′-cyclic GMP–AMP (cGAMP). To unveil their degradation mechanism, we have determined high-resolution crystal structures of VcEAL with Ca2+, c-di-GMP-Ca2+, 5′-pGpG-Ca2+ and cGAMP-Ca2+, the latter provides the first structural basis of cGAMP hydrolysis. Structural studies reveal a typical triosephosphate isomerase barrel-fold with substrate c-di-GMP/cGAMP bound in an extended conformation. Highly conserved residues specifically bind the guanine base of c-di-GMP/cGAMP in the G2 site while the semi-conserved nature of residues at the G1 site could act as a specificity determinant. Two metal ions, co-ordinated with six stubbornly conserved residues and two non-bridging scissile phosphate oxygens of c-di-GMP/cGAMP, activate a water molecule for an in-line attack on the phosphodiester bond, supporting two-metal ion-based catalytic mechanism. PDE activity and biofilm assays of several prudently designed mutants collectively demonstrate that VcEAL active site is charge and size optimized. Intriguingly, in VcEAL-5′-pGpG-Ca2+ structure, β5–α5 loop adopts a novel conformation that along with conserved E131 creates a new metal-binding site. This novel conformation along with several subtle changes in the active site designate VcEAL-5′-pGpG-Ca2+ structure quite different from other 5′-pGpG bound structures reported earlier.

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