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Updated: Nov 8, 2025
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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
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Correlating Bromelain's activity with its structure and active-site dynamics and the medium's physical properties in
Nilimesh Das1, Tanmoy Khan, Navin Subba
1Department of Chemistry, Indian Institute of Technology Kanpur, Kanpur - 208 016, UP, India. psen@iitk.ac.in.
Physical Chemistry Chemical Physics : PCCP
|April 22, 2021
Summary
Deep eutectic solvents (DESs) can enhance bromelain enzyme activity. This study shows DESs influence enzyme structure and dynamics, with optimal activity found in more polar, less viscous conditions.
Area of Science:
- Biocatalysis
- Protein Chemistry
- Green Chemistry
Background:
- Deep eutectic solvents (DESs) are gaining traction as sustainable media for biocatalysis.
- Bromelain, a key industrial enzyme, is investigated in a novel non-ionic DES.
Purpose of the Study:
- To investigate the behavior of bromelain in a ternary acetamide-urea-sorbitol DES.
- To understand how DES concentration and hydration affect bromelain's structure, dynamics, and activity.
Main Methods:
- Enzyme activity assays.
- Structural analysis of bromelain.
- Analysis of protein dynamics in DES.
Main Results:
- Bromelain adopts a compact structure at low DES concentrations and an elongated one at higher concentrations.
- Enzyme activity is retained and sometimes enhanced in DES, correlating with structural compactness and active-site flexibility.
- Optimal activity is observed in media with higher polarity and lower viscosity.
Conclusions:
- DESs can be effective media for biocatalysis, modulating enzyme structure and activity.
- Understanding the interplay between enzyme conformation, dynamics, and medium properties is crucial for designing efficient DES biocatalytic systems.
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