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Unraveling Structural Changes and the Reaction Mechanism in Urease upon Infrared Physical Inactivation
Tongtong Shen1, Ying Liu2, Wenjuan Qu1,3
1School of Food Science and Engineering, Jiangsu University, 301 Xuefu Road, Zhenjiang, Jiangsu 212013, PR China.
Journal of Agricultural and Food Chemistry
|July 9, 2026
Summary
This study introduces an infrared physical field (IPF) method to inhibit urease, significantly reducing enzyme activity by 97.55% with optimal treatment. The method disrupts the enzyme
Area of Science:
- Biochemistry
- Enzyme kinetics
- Physical chemistry
Background:
- Urease is a key enzyme in nitrogen cycling and causes significant economic losses.
- Developing efficient methods to inhibit urease is crucial for energy efficiency and industrial applications.
Purpose of the Study:
- To develop and elucidate the mechanism of an infrared physical field (IPF) method for urease inactivation.
- To optimize IPF treatment parameters for maximum urease inhibition.
Main Methods:
- Experimental approaches including circular dichroism and hydrophobicity assays.
- Computational simulations using molecular dynamics.
- Enzyme activity assays to determine inhibition efficiency.
Main Results:
- Optimal IPF treatment (130 °C-9 min) reduced urease activity by 97.55%.
- IPF treatment increased random coil content and surface hydrophobicity.
- Simulations revealed disruption of hydrogen bonds, van der Waals, and electrostatic interactions, leading to reduced catalytic efficiency.
Conclusions:
- IPF is an effective method for urease inactivation.
- The mechanism involves significant disruption of enzyme structure and function.
- Optimized IPF treatment offers a promising approach for urease inhibition.
Keywords:
binding energy calculationenzyme structural responseinfrared physical fieldmolecular dynamics/dockingurease inhibition mechanismMore Related Videos
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