Paper Number
GN42 My Program
Session
Self-assemblies, Gels and Networks
Title
High-pressure rheology of a thermoreversible protein sol-gel
Presentation Date and Time
October 22, 2025 (Wednesday) 2:10
Track / Room
Track 2 / Sweeney Ballroom B
Authors
- Furst, Eric M. (University of Delaware, Chemical and Biomolecular Engineering)
- Teixeira, Susana (University of Delaware, Chemical and Biomolecular Engineering)
- Paul, Brian (University of Delaware)
- Wagner, Norman (University of Delaware)
- Lenhoff, Abraham (University of Delaware)
Author and Affiliation Lines
Eric M. Furst, Susana Teixeira, Brian Paul, Norman Wagner and Abraham Lenhoff
Chemical and Biomolecular Engineering, University of Delaware, Newark, DE 19716
Speaker / Presenter
Furst, Eric M.
Keywords
experimental methods; applied rheology; bio-fluid dynamics; biomaterials; gels; industrial applications; networks; rheometry
Text of Abstract
Protein gels are ubiquitous in pharmaceutical, biomedical, and food science for which protein formulations undergo a complex series of processing steps, including high hydrostatic pressure, for which the rheological effects on protein gelation are largely unexplored. With the growing need for soft biomaterials with precisely designed structural and mechanical properties, an expanded understanding of pressure-tunable protein gel behavior is highly desirable. With this goal in mind, we studied the rheology through the sol-gel transition of gelatin, a model thermoreversible protein gel. We report measurements using rotational rheometry at atmospheric pressures and microrheology measurements using a high-pressure cell. The latter significantly extends the measurement regime of these materials to process pressures. We find that the thermal gel boundary increases approximately 4C for every 100 MPa of pressure. More importantly, we find that temperature and pressure can be used to control the final gel microstructure, for instance using stepwise pathways to travel back and forth across the critical gel line to achieve the desired initial cross-linking density before quenching to lower temperature. The potential tunability of gel properties by this approach can be a powerful solution for optimizing gel characteristics for biomedical applications, where greater gel strength is not necessarily desirable, and pressure-temperature controlled manufacturing steps can yield the desired gel properties at ambient temperature.