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Exploring Wheat Leaf Urease for a Sustainable Approach: Purification, Kinetics, and Thermal Stability
Surbhi Sahewalla1, Sonam Sihag2, Anil Duhan3
1Department of Biochemistry, College of Basic Sciences and Humanities, Chaudhary Charan Singh Haryana Agricultural University, Hisar, Haryana, 125 004, India. surbhisahewalla04@gmail.com.
The Protein Journal
|September 15, 2025
Summary
Researchers purified and characterized wheat leaf urease, revealing its homotrimeric structure and optimal activity at pH 7.5 and 40°C. Nickel enhanced activity, while copper inhibited it, offering insights for sustainable agriculture.
Area of Science:
- Biochemistry
- Plant Science
- Enzymology
Background:
- Urease enzyme is crucial for cereal crops, especially with foliar urea application.
- Understanding wheat urease is key to improving nitrogen assimilation and promoting sustainable agricultural practices.
Purpose of the Study:
- To purify and characterize wheat leaf urease.
- To explore and potentially enhance urease activity for efficient foliar urea assimilation.
Main Methods:
- Purification of wheat urease to electrophoretic homogeneity.
- Determination of molecular weight using Gel Filtration Chromatography (GFC) and SDS-PAGE.
- Enzyme kinetics (Km, Vmax), optimum conditions (pH, temperature), and thermodynamic parameters were analyzed.
Main Results:
- Purified wheat urease (41.98-fold) has a native molecular weight of ~290 kDa and is homotrimeric (~103 kDa subunits).
- Optimal activity observed at pH 7.5 and 40°C, with specific kinetic parameters (Km=1.0 mM, Vmax=63.25 units mL-1).
- Nickel ions enhanced urease activity, while copper ions showed inhibitory effects; histidine identified at the active site.
Conclusions:
- This study provides novel insights into the largely unexplored wheat leaf urease.
- Characterization data offers a basis for strategies to enhance urease activity in vivo for sustainable agriculture.
- Understanding urease function is vital for optimizing nitrogen use efficiency in cereal crops.
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