April 14-17, 2026 | Krakow, Poland
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Food, despite its complexity, may be examined in the framework of physics.
Many processes and concepts familiar to physicists are involved in food processing, including van der Waals forces, phase separation, diffusion, and phase transitions, to mention a few.
Food systems also involve modern physics difficulties that are still poorly understood, such as percolation, gelation, and the nature of the glass transition.
Physical properties of foods can be changed by preparation and/or food processing, as well as ingredient selection and modification, and become apparent prior, during, and after consumption.
The Food Physics research group conducts multidisciplinary research integrating Physics, Chemistry, Microbiology, Process Engineering, Sensory Science, and Human Physiology, and collaborates closely with other working groups inside and outside the university.
The research activities range from objective measurements of relevant functional, technological, and sensory attributes of liquid and solid products (e.g., flow and fracture behaviour, visco-elasticity, sound emission, adhesion, macro-structure, colour, surface tension, density, and so on) to process and product optimization, as well as human oral processing.
Our purpose is to produce novel mesostructures and application concepts for academic partners, industry, and society, as well as to teach students to implement such integration in their future jobs.
Most of our research projects include rheology, from fundamental rheology utilising an Anton Paar MCR302 and a Kinexus Pro+ to more applied rheology and texture employing Texture Analyzers, Extensographs, and Fluorgraphs.
Collaborations with academic and industry partners from the Food Sector, as well as other fields, are encouraged.
Projects might range from simple, individual measurements through small-scale contract research, method development, and bigger research consortia.
Close connections with several institutions at BOKU allow for the integration of many fields into rheological research.
The Windberger lab is located at Medical University Vienna, Austria. We handle with biological samples, including patient blood, and often use the comparative approach (using samples from well-selected animal species) to formulate structure-function relationships. We test blood and blood clots by rheometry, and deal with clinical and forensic questions.
We described the properties of blood of several mammalian species(1) including also camels or seals, developed mathematical models for animal blood suspensions(2), and defined uncertainties in simulations(3). We elaborate the role of blood plasma in creating a stabile halo around RBCs(4) and an elastic shear layer on surfaces(5). This has consequences for cell-plasma coupling and for the blood flow through capillaries.
References:
Crime scene re-enactment requires substantial blood volumes from human or large animal species, but the type and quality of the blood source can vary significantly between forensic laboratories. Therefore the tests carried out may also vary. We examined the maximum storage time for pig and cow blood at optimized conditions and found out that pig and cow blood must be discarded on the 21st day after collection(1,2).
References:
Fibrin networks show strain hardening, Mullins effect, and nonlinear stress-relaxation. This rich mechanical response can be accessed by rheometry. Viscoelastic tests together with treatment protocols based on cut-off values are already used for postoperative patient care, but only the linear behavior of clots can be accessed by these methods. Measuring at broader ranges of shear deformation will add valuable information to pure kinetic tests because blood flow compels clots into a dynamic non-linear response that alters clot remodeling. We therefore looked for an easy-to-use rheological protocol to identify the mechanical phenotype of a blood clot at large strains. The protocol(1) can also identify amyloidic fibrin fiber networks(2). It translates well to other gels that contain fibers, such as collagen hydrogels with or without embedded cells(3,4).
References