Why is peroxidase important in plants?

Peroxidases are a family of isozymes found in all plants; they are heme-containing monomeric glycoproteins that utilize either H(2)O(2) or O(2) to oxidize a wide variety of molecules. These important enzymes are used in enzyme immunoassays, diagnostic assays and industrial enzymatic reactions.

Why is peroxidase an important enzyme?

Peroxidase is an enzyme found in a wide variety of organisms, from plants to humans to bacteria. Its function is to break down hydrogen peroxide (H2O2), which is one of the toxins produced as a byproduct of using oxygen for respiration. (The fact that it’s toxic is what makes hydrogen peroxide useful in first aid kits.

Is peroxidase enzyme A protein?

Heme Proteins Peroxidases are a group of enzymes that catalyze the oxidation of a substrate by hydrogen peroxide or an organic peroxide. Most peroxidases are ferric heme proteins; one notable exception being the glutathione peroxidase, which is a selenium-containing enzyme.

What are the optimal conditions for peroxidase?

Our results showed optimum temperature is 40 °C for both peroxidase activity. Like most chemical reactions, with increase of temperature from 27 ºC, gradually, activity of peroxidase increased so; we reached to maximum of activity at 40 ºC (300 \%) (Fig.

How is peroxidase activity determined?

Peroxidase activity was measured by determining the absorbance of yellow product at 450 nm. Increase in absorbance was directly proportional to the peroxidase activity.

Why is horseradish peroxidase important?

Horseradish peroxidase (HRP) mediates efficient conversion of many phenolic contaminants and thus has potential applications for pollution control. Such potentially important applications suffer however from the fact that the enzyme becomes quickly inactivated during phenol oxidation and polymerization.

What factors affect peroxidase?

The results of this experiment demonstrated that the performance of hydrogen peroxidase was greatly affected by all three factors, temperature, concentration level, and pH.

Which plant material is used to study the enzyme activity of peroxidase?

They catalyses reduction of peroxide and generate reactive oxygen species. In the present study we demonstrated that insect infestation induces peroxidase activity in sap and total soluble protein (TSP) of plant leaves. Three important crop plants viz. tomato, cowpea and cotton were used for this study.

What is the role of peroxidase in the ELISA test?

One commonly used enzyme conjugate in ELISA is horseradish peroxidase. Horseradish peroxidase (HRP) is a 40,000 Dalton protein, which catalyzes the reduction of hydrogen peroxide (H2O2) to water (H2O) [1]. Amplex® Red is a substrate for use with HRP containing assays [2].

What is the substrate for peroxidase?

Peroxidases are a group of enzymes that catalyze the oxidation of a substrate by hydrogen peroxide or an organic peroxide.

What is the substrate of the enzyme peroxidase?

Why is alkaline phosphatase used in ELISA?

Most ELISA tests have used alkaline phosphatase conjugated antibodies for the detection system as it used the substrate p-nitrophenyl phosphate which produces a water-soluble yellow reaction product. It can be added to the finished plate to make the oxidation product completely soluble and to stop the reaction.

How to extract protein from leaves of 80 different medicinal plants?

Methods: Crude extract were obtained from the leaves of 80 different medicinal plants. Tris-HCl buffer was used as the extraction buffer and the supernatants obtained were used for determination of total protein and protease activity using spectrophotometric methods.

How do you determine the specific activity of an enzyme?

specific activity of the enzyme could be determined. Enzymologists determine specific activity in order to determine the purity of the enzyme sample mixture. As the enzyme becomes more pure in a mixture, the specific activity value increases. Purified proteins are valuable for production of growth factors,

How do you test for protease activity in protein samples?

Tris-HCl buffer was used as the extraction buffer and the supernatants obtained were used for determination of total protein and protease activity using spectrophotometric methods. Qualitative screening for the presence of protease was carried out with agar diffusion method by incorporating the substrate.

Do proteolytic enzymes from medicinally important plants influence medicinal use?

Earlier investigations have focused on the occurrence of proteases in medicinally unimportant plants. Therefore it has been aimed to study the occurrence of proteolytic enzymes from medicinally important plants establish any correlation exists between protease activity and medicinal use of individual plants.