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

Combustion and thermal behaviors of the novel UV-cured intumescent flame retardant coatings containing phosphorus and nitrogen

e-Polymers ◽  
2010 ◽  
Vol 10 (1) ◽  
Author(s):  
WeiYi Xing ◽  
Lei Song ◽  
Yuan Hu ◽  
Xiaoqi Lv ◽  
Xin Wang
Keyword(s):  
Flame Retardant ◽  
Cone Calorimeter ◽  
Degradation Mechanism ◽  
Intumescent Flame Retardant ◽  
The Novel ◽  
Uv Curable ◽  
Peak Heat Release Rate ◽  
Phosphorus Containing ◽  
Fire Properties ◽  
Triglycidyl Isocyanurate

AbstractPhosphorus-containing tri(acryloyloxyethyl) phosphate (TAEP) was blended with triglycidyl isocyanurate acrylate (TGICA) in different ratios to obtain a series of UV curable intumescent flame retardant resins. The fire properties of the cured films were characterized by limited oxygen index (LOI), UL 94 and Cone Calorimeter. A distinct synergistic effect was found between TAEP and TGICA. The sample TAEP2 had the highest LOI (44) value among all resins. The cone calorimeter results showed that the sample TAEP2 had the lowest peak heat release rate (297 KW/M2). The thermal degradation was monitored by thermogravimetric analysis (TGA) and real-time Fourier transform infrared spectroscopy (RT-FTIR). The degradation mechanism is suggested in which the phosphate group in TAEP first degraded to form poly(phosphoric acid)s, which further catalyzed the degradation of the material to form char with emission of nitrogen volatiles from TGICA, leading to the formation of expanding char.

scholarly journals Hydrolysis and Photolysis Kinetics, and Identification of Degradation Products of the Novel Bactericide 2-(4-Fluorobenzyl)-5-(Methylsulfonyl)-1,3,4-Oxadiazole in Water

2018 ◽  
Vol 15 (12) ◽  
pp. 2741 ◽  
Author(s):  
Xingang Meng ◽  
Lingzhu Chen ◽  
Yuping Zhang ◽  
Deyu Hu ◽  
Baoan Song
Keyword(s):  
Degradation Product ◽  
High Performance ◽  
Degradation Products ◽  
Degradation Mechanism ◽  
The Novel ◽  
Initial Concentration ◽  
First Order ◽  
First Order Kinetics ◽  
Kinetics Of ◽  
High Resolution Mass Spectrometer

Hydrolysis and photolysis kinetics of Fubianezuofeng (FBEZF) in water were investigated in detail. The hydrolysis half-lives of FBEZF depending on pH, initial concentration, and temperature were (14.44 d at pH = 5; 1.60 d at pH = 7), (36.48 h at 1.0 mg L−1; 38.51 h at 5.0 mg L−1; and 31.51 h at 10.0 mg L−1), and (77.02 h at 15 °C; 38.51 h at 25 °C; 19.80 h at 35 °C; and 3.00 h at 45 °C), respectively. The photolysis half-life of FBEZF in different initial concentrations were 8.77 h at 1.0 mg L−1, 8.35 h at 5.0 mg L−1, and 8.66 h at 10.0 mg L−1, respectively. Results indicated that the degradation of FBEZF followed first-order kinetics, as the initial concentration of FBEZF only had a slight effect on the UV irradiation effects, and the increase in pH and temperature can substantially accelerate the degradation. The hydrolysis Ea of FBEZF was 49.90 kJ mol−1, which indicates that FBEZF belongs to medium hydrolysis. In addition, the degradation products were identified using ultra-high-performance liquid chromatography coupled with an Orbitrap high-resolution mass spectrometer. One degradation product was extracted and further analyzed by 1H-NMR, 13C-NMR, 19F-NMR, and MS. The degradation product was identified as 2-(4-fluorobenazyl)-5-methoxy-1,3,4-oxadiazole, therefore a degradation mechanism of FBEZF in water was proposed. The research on FBEZF can be helpful for its safety assessment and increase the understanding of FBEZF in water environments.

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

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.

The novel steroidal glycoside from the dried bulb of Allium Macrostemon Bunge inhibits platelet activation

2010 ◽  
Vol 34 (8) ◽  
pp. S33-S33
Author(s):  
Wenchao Ou ◽  
Haifeng Chen ◽  
Yun Zhong ◽  
Benrong Liu ◽  
Keji Chen
Keyword(s):  
Platelet Activation ◽  
The Novel ◽  
Steroidal Glycoside ◽  
Allium Macrostemon
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