scholarly journals Solar photolysis versus TiO2-mediated solar photocatalysis: a kinetic study of the degradation of naproxen and diclofenac in various water matrices

2016 ◽  
Vol 23 (17) ◽  
pp. 17437-17448 ◽  
Author(s):  
Devagi Kanakaraju ◽  
Cherie A. Motti ◽  
Beverley D. Glass ◽  
Michael Oelgemöller
2013 ◽  
Vol 53 (8) ◽  
pp. 2049-2058 ◽  
Author(s):  
Sadek Igoud ◽  
Fatiha Souahi ◽  
Chems Eddine Chitour ◽  
Lynda Amrouche ◽  
Arezki Moussaoui ◽  
...  

2006 ◽  
Vol 53 (3) ◽  
pp. 1-8 ◽  
Author(s):  
K.-D. Zoh ◽  
T.-S. Kim ◽  
J.-G. Kim ◽  
K. Choi ◽  
S.-M. Yi

The solar photocatalytic degradation of methyl parathion was investigated using a circulating TiO2/solar light reactor. Under solar photocatalysis condition, parathion was more effectively degraded than solar photolysis and TiO2-only conditions. With solar photocatalysis, 20 mg/L of parathion was completely degraded within 60 min with a TOC decrease of 63% after 150 min. The main ionic byproducts during photocatalysis recovered from parathion degradation were mainly as NO3−, NO2− and NH4+, 80% of the sulphur as SO42−, and 5% of phosphorus as PO43−. The organic intermediates 4-nitrophenol and methyl paraoxon were also identified, and these were further degraded in solar photocatalytic condition. Two different bioassays (Vibrio fischeri and Daphnia magna) were used to test the acute toxicity of solutions treated by solar photocatalysis and photolysis. The Microtox test using V. fischeri showed that the toxicity expressed as EC50 (%) value increased from 5.5% to >82% in solar photocatalysis, indicating that the treated solution is non-toxic, but only increased from 4.9 to 20.5% after 150 min in solar photolysis. The acute toxicity test using D. magna showed that EC50 (%) increased from 0.05 to 1.08% under solar photocatalysis, but only increased to 0.12% after 150 min with solar photolysis, indicating the solution is still toxic. The pattern of toxicity reduction parallels the decrease in TOC and the parathion concentrations.


1976 ◽  
Vol 73 ◽  
pp. 283-286 ◽  
Author(s):  
H. S. Singh ◽  
A. K. Sisodia ◽  
S. M. Singh ◽  
R. K. Singh ◽  
R. N. Singh

2008 ◽  
Vol 105 (12) ◽  
pp. 601-608
Author(s):  
Seung Min Han ◽  
Dong Joon Min ◽  
Joo Hyun Park ◽  
Jung Ho Park ◽  
Jong Min Park
Keyword(s):  

1983 ◽  
Vol 49 (03) ◽  
pp. 199-203 ◽  
Author(s):  
V M Yomtova ◽  
N A Stambolieva ◽  
B M Blagoev

SummaryIt was found that the effect of heparin on the amidase activity of urokinase (E C 3.4.21.31), plasmin (E C 3.4.21.7) and trypsin (E C 3.4.21.4) depended on the substrate used. No effect of heparin on the amidase activity of urokinase and trypsin was observed when Pyro Glu-Gly-Arg-p-nitroanilide (S-2444) and α-N-acetyl-L-lysine-p-nitroanilide (ALNA) were used as substrates. Heparin acted as a uncompetitive inhibitor of trypsin (Ki = 1.2×10-6 M), plasmin (Ki = 4.9×10-6 M) and urokinase (Ki = l.0×10-7 M) when Bz-Phe-Val-Arg-p-nitroanilide (S-2160), H-D-Val-Leu-Lys-p-nitroanilide (S-2251) and plasminogen, respectively, were used as substrates. These results, as well as the data obtained by studying the effect of the simultaneous presence of heparin and competitive inhibitors suggest that although heparin is not bound at the active center of these enzymes, it may influence the effectivity of catalysis.


1981 ◽  
Vol 31 (1) ◽  
pp. 388-394 ◽  
Author(s):  
Mahmoud El-Sawi ◽  
Antonio Iannibello ◽  
Fernando Morelli ◽  
Ganfranco Gatalano ◽  
Francesco Intrieri ◽  
...  
Keyword(s):  

1967 ◽  
Vol 56 (1_Suppl) ◽  
pp. S76 ◽  
Author(s):  
E. Menini ◽  
L. L. Engel
Keyword(s):  

Sign in / Sign up

Export Citation Format

Share Document