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Kinetics of enzymatic modification of quercetin with cysteine by horseradish peroxidase

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Title Kinetics of enzymatic modification of quercetin with cysteine by horseradish peroxidase
 
Creator Savic, Sasa R
Petronijevic, Zivomir B
 
Subject Horseradish peroxidase
Quercetin
Cysteine
Kinetic mechanism
Spectrophotometry
 
Description 221-226
The kinetic mechanism of enzymatic modification of flavonol quercetin
with L-cysteine by horseradish peroxidase (HRP) was studied. Reaction of
modification of quercetin was followed by recording spectral changes over time
at 380 nm. All reactions were performed in 100 mM phosphate buffer pH, 6.0 at
20ºC. Kinetic parameters were
determined from graphics of linear
Michaelis-Menten equation. The values obtained at specified intervals were:
Vmax = 0.17 ÷ 0.91 ΔA380/min,
Km = 0.023 ÷ 0.5 mM, kcat = 0.21 ÷ 1.14 ΔA380/min∙nM-1
and Vmax/Km = 0.83 ÷ 26.55 ΔA380/min∙mM-1.
It was found that all
investigated reactions of the
modification of quercetin with L-cysteine by HRP followed an ordered mechanism. We propose that HRP initially
reacts with H2O2 than with
quercetin and finally with L-cysteine, leading to the introduction of L-cysteine in the structure of quercetin.
 
Date 2013-06-04T13:13:20Z
2013-06-04T13:13:20Z
2013-06
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/18694
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.50(3) [June 2013]