Enzymes can be used to enable a specific and controlled approach for structural modifications of protein networks in food technology. Enzymatically induced cross-links between proteins in the continuous phase and/or at interfaces result in better stabilisation and enhanced material properties in foams and emulsions. In this work the interfacial properties of ß-casein and ?-casein films were investigated with a special focus on the mechanism of transglutaminase (TG) induced cross-linking at the air/water interface. The surface rheology results showed that for the enhanced interfacial strength the order and timing of TG addition matters: TG reaction was most effective when the enzyme was applied during adsorption of proteins to the interface. Differences observed between enzymatic cross-linking of ß-casein and ?-casein at the air/water interface verified the importance of molecular structure and close packing for formation of an elastic protein network.
- milk protein
- enzymatic cross-linking
- air/water interface
- surface rheology
Ridout, M. J., Paananen, A., Mamode, A., Linder, M. B., & Wilde, P. J. (2015). Interaction of transglutaminase with adsorbed and spread films of [beta]-casein and [kappa]-casein. Colloids and Surfaces B: Biointerfaces, 128, 254-260. https://doi.org/10.1016/j.colsurfb.2015.01.045