Acid gelation of enzymatically cross-linked casein: from molecular level to network formation
Caseins (80 % of protein fraction in milk) contribute essentially to structure formation in fermented milk products (yoghurt, cheese). This can be significantly influenced through an enzymatic cross-linking of casein by microbial transglutaminse. However, the enzyme's modus operandi is still poorly understood, which makes its controlled application in the milk industry difficult.
We aim to analyse the structure-function-interaction of enzymatically cross-linked casein on different length scales. For this, casein of various structural conformations is generated through the environmental conditions, and subsequently cross-linked by microbial transglutaminase. Finally, we investigate physico-chemical properties and gelation of the casein, which will be correlated to the casein's structure.
In cooperation with:
- Leibniz-Institut für Polymerforschung Dresden e.V., Polymer Separation Group (PD Dr. Albena Lederer)
Supported by:
- Deutsche Forschungsgemeinschaft
Project publications:
Raak N, Brehm L, Abbate RA, Henle T, Lederer A, Rohm H, Jaros D (2019) Self association of casein studied using enzymatic cross-linking at different temperatures. Food Bioscience 28, 89-98.
Abbate RA, Raak N, Boye S, Janke A, Rohm H, Jaros D, Lederer A (2019) Asymmetric flow field flow fractionation for the investigation of caseins cross-linked by microbial transglutaminase. Food Hydrocolloids 92, 117-124.
Project researchers and contact:
Dipl.-Ing. Norbert Raak
Biomacromolecules
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PD Dr.nat.techn. et Ing.habil Doris Jaros
Product technologies: Milk; Biomacromolecules
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Senior Professor Dipl.-Ing. Dr. nat. techn. habil. Harald Rohm
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