JG Julian Gerhäuser

M.Sc. Julian Gerhäuser

  • Postanschrift: Kaiserstr. 12
    Liefer- und Besucheranschrift: Gotthard-Franz-Straße 3
    Geb. 50.31, 4. OG
    D-76131 Karlsruhe

About myself

After graduating from high school, I first completed an apprenticeship as biotechnological assistant in Heidelberg. Afterwards I studied biotechnology at Mannheim University of Applied Sciences. Since 2019, I have been a research assistant at the Institute of Food Process Engineering, working on ice-binding molecules.

Research focus

Ice-binding molecules are able to influence the growth of ice crystals. In particular, they effect the recrystallization process during frozen storage. Due to the rearrangement of water molecules, large ice crystals become increasingly larger and small ice crystals disappear, while the ice content remains constant. Therefore, recrystallization is considered one of the main damage mechanisms during frozen storage causing severe damage of sensitive products such as dough, fruit and, in the medical field, cells as well as organs. In the case of ice cream, the coarsening of the ice crystal structure due to recrystallization also leads to an unpleasant mouthfeel when consumed.

The best-known group of ice-binding molecules are ice-binding proteins also known as antifreeze proteins. Meanwhile, these proteins have been found in a wide variety of living organisms. However, the interaction mechanisms between protein and the ice crystal as well as the further development of the ice surface structure are still unclear. This is also true for other ice-binding molecules such as kappa-carrageenan. Although viscosity-independent recrystallization inhibition and a change in ice crystal shape have already been found for kappa-carrageenan, binding to the ice crystal surface has not yet been demonstrated beyond doubt.


Molecular dynamic (MD-) simulations are used to gain insight at the molecular level into the ice binding of these molecules. In this way, ice binding can be verified and molecular groups important for the interaction can be identified. The interactions between the individual atoms are used to calculate the trajectories of motion. In addition to the simulations, the properties of ice-binding molecules are investigated by recrystallization experiments. Furthermore, ice-binding proteins can be efficiently purified by ice affinity chromatographic methods.


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