# Function and Engineering of a Food Enzyme Under Coupled High-Temperature–Pressure Conditions: Insights from Molecular Dynamics Simulation and Experimental Validation

## TL;DR

This study explores how temperature and pressure affect the structure and function of a food enzyme using simulations and experiments.

## Contribution

The study provides new insights into the structural adaptability of EC hydrolase under coupled high-temperature–pressure conditions.

## Key findings

- MD simulations revealed structural changes in EC hydrolase under varying temperature and pressure.
- The enzyme's adaptability was linked to dynamic changes in RMSD, RMSF, Rg, SASA, and hydrogen bonding.
- Computer-aided engineering supported the enzyme's functional resilience under extreme conditions.

## Abstract

The relationship between protein structure and function is intrinsically interconnected, as the structure of a protein directly determines its functional properties. To investigate the effects of temperature and pressure on protein function, this study employed ethyl carbamate (EC) hydrolase as a model food enzyme and conducted molecular dynamics (MD) simulations under varying temperature and pressure levels to elucidate its structure–function relationship. By systematically analyzing the dynamic changes in root mean square deviation (RMSD), root mean square fluctuation (RMSF), radius of gyration (Rg), solvent accessible surface area (SASA), hydrogen bonding, catalytic pocket conformation, and packing density under different temperature and pressure conditions, we revealed the structural adaptability of EC hydrolase. Furthermore, we analyzed the characteristics of EC hydrolase using molecular dynamics simulations with temperature and pressure levels, as well as conformational bias-based computer-aided engineering, providing both theoretical and experimental foundation for the adaptability mechanisms of enzymes under extreme conditions.