Behzad Shareghi; Maryam Kazemi Nafchi
Volume 5, Issue 1 , September 2016, , Pages 1-8
Abstract
Abstract Peroxidases are a group of oxidoreductases that are produced by a number of microorganisms and plants, and catalyse the reduction of peroxides. Peroxidases are widely used in clinical biochemistry and enzyme immunoassay. Horseradish peroxidase isoenzyme C (HRP) is one of the characterized peroxidases. ...
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Abstract Peroxidases are a group of oxidoreductases that are produced by a number of microorganisms and plants, and catalyse the reduction of peroxides. Peroxidases are widely used in clinical biochemistry and enzyme immunoassay. Horseradish peroxidase isoenzyme C (HRP) is one of the characterized peroxidases. The structure of the enzyme is largely alpha helical. Kinetics studies of peroxidase enzyme were performed using a spectrophotometer UV-Vis fitted with electronic control system at 35oC and 45oC and pH4 and in the presence ethanol and butanediol. Kinetic parameters show that ethanol and butanediol organic solvents becomes caused the increase of maximum speed (VMAX) and activity of the enzyme. Organic solvents have effect on electrostatic interactions of proteins because their dielectric constant with water is different. In general, reduce properties of polar solvents and decreased dielectric constant becomes caused the increases electrostatic repulsion, leading to the opening of the proteins. Enzymes activity in such organic environments increases stability, activity or facilitate reactions that are difficult to perform in aquatic environments.
