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Kinetics and thermal stability of two peroxidase isozymes from Eupatorium odoratum
D Nisha Rani1, T Emilia Abraham
1Polymer Science, Chemical Sciences Division, Regional Research Laboratory (CSIR), Trivandrum 695 019, India.
Eupatorium odoratum leaf peroxidase comprises multiple isozymes. Detailed studies on two specific isozymes (E5 and E7) reveal distinct thermal stability and substrate specificity, offering insights into plant enzyme function.
Area of Science:
- Biochemistry
- Plant Science
- Enzymology
Background:
- Eupatorium odoratum leaf peroxidase exhibits complex isozyme patterns.
- Understanding plant peroxidase isozymes is crucial for biochemical and biotechnological applications.
Purpose of the Study:
- To characterize the thermal stability and kinetic properties of Eupatorium odoratum leaf peroxidase isozymes.
- To investigate the substrate specificity and catalytic efficiency of selected isozymes.
Main Methods:
- Isoelectric focusing for separation of peroxidase isozymes.
- Thermal stability assays to determine inactivation parameters (activation enthalpy, free energy, activation entropy).
- Kinetic studies using ABTS and Pyrogallol as substrates to determine kinetic parameters (Km, catalytic specificity constant).
Main Results:
- At least seven distinct isozymes were identified, including cationic, anionic, and neutral forms.
- Two studied isozymes, E5 (43 kD) and E7 (50 kD), showed varying thermal stability and optimal pH in the acidic range.
- Both isozymes displayed distinct substrate specificities and high catalytic efficiency with ABTS and H2O2.
Conclusions:
- Eupatorium odoratum leaf peroxidase isozymes possess unique biochemical and kinetic characteristics.
- The distinct properties of E5 and E7 suggest specialized roles within the plant.
- Further research into these isozymes could unlock novel biotechnological applications.
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