AI Article Synopsis
- Enzymes can be used in food technology to modify protein networks, leading to stronger and more stable foams and emulsions.
- The study focused on how transglutaminase (TG) helps cross-link β-casein and к-casein films at the air/water interface, affecting their stability.
- Results highlighted that the timing and method of adding TG is crucial for strengthening the interfacial properties, with variations between β-casein and к-casein showing the importance of molecular structure in forming elastic protein networks.
Article Abstract
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 β-casein and к-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 β-casein and к-casein at the air/water interface verified the importance of molecular structure and close packing for formation of an elastic protein network.
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| http://dx.doi.org/10.1016/j.colsurfb.2015.01.045 | DOI Listing |
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