Horseradish peroxidase catalyzed oxidation of thiocyanate by hydrogen peroxide: comparison with lactoperoxidase-catalysed oxidation and role of distal histidine

Author(s):  
Sandeep Modi ◽  
Digambar V. Behere ◽  
Mitra Samaresh
1973 ◽  
Vol 51 (7) ◽  
pp. 1066-1071 ◽  
Author(s):  
C. R. Lyttle ◽  
T. McNabb ◽  
P. H. Jellinck

The role of 2,4-dichlorophenol in enhancing the conversion of [4-14C]estradiol to water-soluble products by a uterine preparation in the presence of hydrogen peroxide has been investigated. The addition of this phenol to a solution of uterine or horseradish peroxidase in 8 M urea restored the activity of the enzyme and also that of horseradish peroxidase inactivated by heating. It also protected the enzyme from inactivation during incubation. It is proposed that 2,4-dichlorophenol exerts its effect by activating peroxidase and protecting the enzyme from inactivation by the products of the reaction.


2013 ◽  
Vol 67 (3) ◽  
pp. 419-426
Author(s):  
Vladan Djuric ◽  
Nebojsa Deletic ◽  
Vesna Stankov-Jovanovic ◽  
Ranko Simonovic

Primary role of peroxidase enzyme is to decompose endogenous hydrogen peroxide, when oxygen radical is being replaced by a less potent radical, which is its cosubstrates oxidized form. During this study, catalytic activity of horseradish peroxidase has been observed in the presence of antioxidants from vitamin group, such as C, E and A, i.e. their water-soluble forms. It was found that vitamin E showed no effect on the enzyme activity and fate of cosubstrate radicals from the group of benzidine derivatives. Vitamin C proceeds enzymatic reaction showing its antioxidative character, and absorbs electrons from radicals, bringing cosubstrate back to its relaxed state. On the other hand, vitamin A plays a role of uncompetitive peroxidase inhibitor, which is visible through decreasing initial rate of catalytic reaction, and is reflected as virtual decrease of enzyme concentration. Furthermore, it prolongs life of endogenous hydrogen peroxide, which could potentially lead to oxidative stress of cells. This inhibitory effect can be used in analytical purpose, for determination of retinol acetate content in a sample.


1996 ◽  
Vol 34 (10) ◽  
pp. 151-159 ◽  
Author(s):  
Hossein Ganjidoust ◽  
Kenji Tatsumi ◽  
Shinji Wada ◽  
Mitsuo Kawase

Chlorophenols removal from industrial wastewater by horseradish peroxidase and coagulant was investigated. It was found that an enzymatic reaction time of less than one hour was enough for the reaction to reach 95% completion. Chitosan, which is a natural coagulant, was an effective coagulant as compared to mineral coagulants such as aluminum sulfate (ALUM), hexamethylene diamine epichlorohydrin polycondensate (HX), polyacrylamide (PAM), and polyethyleneimine (PEI). A combination of 0.4 U/mL peroxidase to 2 ppm chitosan along with 0.8 mM of hydrogen peroxide resulted in over 95% chlorophenol removal from aqueous solution.


1985 ◽  
Vol 55 ◽  
pp. 215-224 ◽  
Author(s):  
Massimo Broggini ◽  
Cosmo Rossi ◽  
Emilio Benfenati ◽  
Maurizio D'Incalci ◽  
Roberto Fanelli ◽  
...  

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