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Updated: Jul 20, 2025
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Ice Generation and the Heat and Mass Transfer Phenomena of Introducing Water to a Cold Bath of Brine
Published on: March 13, 2017
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Does supercooled water retain its universal nucleation behavior under shear at high pressure?
Snehitha Srirangam1, Mangesh Bhendale1, Jayant K Singh1,2
1Department of Chemical Engineering, Indian Institute of Technology Kanpur, Uttar Pradesh, 208016, India. jayantks@iitk.ac.in.
Physical Chemistry Chemical Physics : PCCP
|August 7, 2023
Summary
High pressure enhances ice nucleation under shear, crucial for cryopreservation. Optimal shear rates show non-monotonic pressure dependence, impacting biological sample preservation.
Area of Science:
- Physical Chemistry
- Biophysics
- Materials Science
Background:
- High pressure is essential for protein crystallization and cryopreservation, preventing biological sample freezing.
- Understanding ice nucleation under shear at high pressures is critical for these applications.
Purpose of the Study:
- To investigate ice nucleation behavior in supercooled water under shear at various high pressures.
- To explore the universal nucleation dynamics of sheared systems at elevated pressures.
Main Methods:
- Computed nucleation rates using the TIP4P/Ice model and extended classical nucleation theory (CNT) with a seeding method.
- Analyzed pressure dependence of transport and thermodynamic properties, including shear rate.
- Simulations conducted at pressures from 1 to 1000 bar and 240 K.
Main Results:
- Observed decreased Δμliq-ice and viscosity, and increased diffusivity with rising pressure.
- Demonstrated a non-monotonic dependence of nucleation rate on shear, with a peak at optimal shear rates (107–108 s-1).
- Revealed a non-monotonic pressure dependence of optimal shear rates, potentially due to Stokes-Einstein relation violation.
Conclusions:
- High pressure significantly influences ice nucleation kinetics under shear.
- Optimal shear rates for nucleation are pressure-dependent and exhibit non-monotonic behavior.
- Findings offer insights into cryopreservation and protein crystallization under extreme conditions.
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