Horseradish Peroxidase Oxidation of Tyrosine-Containing Peptides and Their Subsequent Polymerization:  A Kinetic Study†

Biochemistry ◽  
1997 ◽  
Vol 36 (28) ◽  
pp. 8504-8513 ◽  
Author(s):  
Thierry Michon ◽  
Michel Chenu ◽  
Nicolas Kellershon ◽  
Michel Desmadril ◽  
Jacques Guéguen
Keyword(s):  
Horseradish Peroxidase ◽  
Kinetic Study ◽  
Peroxidase Oxidation

Studies on Horseradish Peroxidase. VII. A Kinetic Study of the Oxidation of Iodide by Horseradish Peroxidase Compound II

1971 ◽  
Vol 49 (18) ◽  
pp. 3059-3063 ◽  
Author(s):  
R. Roman ◽  
H. B. Dunford ◽  
M. Evett
Keyword(s):  
Ionic Strength ◽  
Horseradish Peroxidase ◽  
Kinetic Study ◽  
Rate Constant ◽  
Ph Dependence ◽  
Order Rate Constant ◽  
Acid Dissociation ◽  
Ph Range ◽  
Compound Ii ◽  
Kinetics Of

The kinetics of the oxidation of iodide ion by horseradish peroxidase compound II have been studied as a function of pH at 25° and ionic strength of 0.11. The logarithm of the second-order rate constant decreases linearly from 2.3 × 105 to 0.1 M−1 s−1 with increasing pH over the pH range 2.7 to 9.0. The pH dependence of the reaction is explained in terms of an acid dissociation outside the pH range of the study.

Kinetic study on the removal of toxic phenol and chlorophenol from waste water by horseradish peroxidase

Chemosphere ◽  
1998 ◽  
Vol 37 (8) ◽  
pp. 1571-1577 ◽  
Author(s):  
Zhang Tong ◽  
Zhao Qingxiang ◽  
Huang Hui ◽  
Li Qin ◽  
Zhang Yi ◽  
...  
Keyword(s):  
Waste Water ◽  
Horseradish Peroxidase ◽  
Kinetic Study

Stopped-Flow, Pre-Steady-State Kinetic Study of Horseradish Peroxidase Catalysis in Nonaqueous Media

1996 ◽  
Vol 799 (1 Enzyme Engine) ◽  
pp. 364-375
Author(s):  
SHUNGUANG WANG ◽  
WEI LIU ◽  
XINSONG Ji ◽  
LIN MA ◽  
TIEJIN Li ◽  
...  
Keyword(s):  
Steady State ◽  
Horseradish Peroxidase ◽  
Kinetic Study ◽  
Stopped Flow ◽  
Nonaqueous Media ◽  
Steady State Kinetic ◽  
State Kinetic

scholarly journals HORSERADISH PEROXIDASE CATALYZED DEGRADATION OF BROMOPHENOL BLUE DYE

2020 ◽  
Vol 64 (1) ◽  
pp. 93-98
Author(s):  
Anna A. Solovyeva ◽  
Thi Trinh Pham ◽  
Olga E. Lebedeva ◽  
Maria N. Ustinova
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase ◽  
Dye Degradation ◽  
Enzymatic Reaction ◽  
Oxidative Degradation ◽  
Bromophenol Blue ◽  
Blue Dye ◽  
Time Interval ◽  
Bromophenol Blue Dye ◽  
Peroxidase Oxidation

In this study, the oxidative destruction of bromophenol blue dye with hydrogen peroxide was carried out at pH 4.0-4.1 in the presence of a commercial horseradish peroxidase, as well as peroxidase isolated directly from horseradish roots (Armoracia rusticana). To determine peroxidase activity, a model reaction of the oxidation of phenol to quinone was used. With a dye concentration of 32.7 μM, the optimal concentration of hydrogen peroxide was 0.04 mM at peroxidase concentration of 1.15 nM. The optimal temperature of the enzymatic reaction was determined: at 23 °С for 10 min 90% of the dye was exposed to destruction. When the temperature rises to 50 °С, the reaction rate decreases, and the degree of destruction is 56% for the same time interval. It was shown that the initial rate of peroxidase oxidation of bromophenol blue follows Michaelis-Menten equation. The kinetic parameters of the enzymatic reaction were determined by linearizing Michaelis-Menten equation in Lineweaver-Burk coordinates. It was found that for the peroxidase oxidation reaction of bromophenol blue Michaelis constant and maximum rate were 42.7 μM and 57.5 μM·min–1, respectively. In this work, а high percentage of dye degradation was also achieved when using peroxidase isolated from horseradish roots. The experiments were conducted at a temperature of 30оС and pH 4.1. With the increase in the volume of the extract from 0.1 to 0.2 ml, the percentage decolorization increases from 75% to 90%. The results demonstrate the high degradation efficiency of bromophenol blue with the participation of the commercial horseradish peroxidase and peroxidase isolated from horseradish roots. Enzymatic oxidative degradation can be considered as an alternative to biodegradation.

A Kinetic Study of the Reaction of Horseradish Peroxidase with Hydrogen Peroxide

1975 ◽  
Vol 53 (5) ◽  
pp. 495-501 ◽  
Author(s):  
D. Dolman ◽  
G. A. Newell ◽  
M. D. Thurlow ◽  
H. B. Dunford
Keyword(s):  
Hydrogen Peroxide ◽  
Horseradish Peroxidase ◽  
Kinetic Study ◽  
Enzyme Analysis ◽  
Cyanide Binding ◽  
Rate Of Reaction ◽  
Form Compound ◽  
Ph Range ◽  
Kinetics Of ◽  
Ionizable Groups

A kinetic study has been carried out over the pH range of 2.63–9.37 for the reaction of horseradish peroxidase with hydrogen peroxide to form compound 1 of the enzyme. Analysis of the results, indicates that there are two kinetic influencing, ionizable groups on the enzyme with pKa values of 3.2 and 3.9. Protonation of these groups results in a decrease in the rate of reaction of the enzyme with H2O2.A previous study of the kinetics of cyanide binding to horseradish peroxidase (Ellis, W. D. &Dunford, H. B.: Biochemistry 7, 2054–2062 (1968)) has been extended down to pH 2.55, and analysis of these results also indicates the presence of two kinetically important ionizable groups on the enzyme with pKa values of 2.9 and 3.9.

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