ArticleThe protein journal2025
Exploring Wheat Leaf Urease for a Sustainable Approach: Purification, Kinetics, and Thermal Stability Characterization.
Article in The protein journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The urease enzyme has an inevitable application in cereal crops, particularly in response to foliar urea application. A holistic and novel approach was employed in the present work with the aim to purify and characterize the wheat leaf urease. This will help in exploring and enhancing its activity in assimilation of foliar urea application and a move towards sustainability. Wheat urease was purified to electrophoretic homogeneity with a 41.98 fold purification and 36.3% recovery. The molecular weight of the native enzyme was found to be ~ 290 kDa by Gel Filtration Chromatography (GFC), and a single band in Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) of ~ 103 kDa deduced its homotrimeric nature. The enzyme had a K
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