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Protein Preferential Solvation in (Sucralose + Water) Mixtures
Isamu Kuroiwa1, Yasuyuki Maki2, Koichi Matsuo3
1Graduate School of Science, Kyushu University, Fukuoka 819-0395, Japan.
The Journal of Physical Chemistry. B
|January 10, 2024
Summary
Sucrose stabilizes proteins by exclusion, but sucralose, a sucrose derivative, destabilizes proteins through direct interaction. This study reveals sucralose
Area of Science:
- Biochemistry
- Protein Chemistry
- Physical Chemistry
Background:
- Sugars like sucrose stabilize proteins against heat through preferential exclusion.
- Sucralose is a chlorinated sucrose derivative with potential applications as a sweetener.
Purpose of the Study:
- To investigate the impact of sucralose on protein stability and solvation.
- To compare the effects of sucrose and sucralose on myoglobin denaturation.
Main Methods:
- Circular dichroism spectroscopy to assess protein structure and denaturation.
- Small-angle X-ray scattering to analyze protein conformation and solvation.
- Physicochemical property measurements of aqueous sucralose solutions (density, sound velocity, viscosity, osmolality).
Main Results:
- Sucrose increased myoglobin's denaturation temperature and was preferentially excluded.
- Sucralose decreased myoglobin's denaturation temperature and was preferentially adsorbed.
- Physicochemical analysis showed no significant indirect destabilization effects of sucralose via water structure modification.
Conclusions:
- Sucralose directly interacts with proteins, leading to destabilization.
- Unlike sucrose, sucralose adsorption to proteins causes thermal instability.
- The findings highlight the importance of direct solute-protein interactions in protein stabilization/destabilization.
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