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 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.
| Original language | English |
|---|---|
| Pages (from-to) | 254-260 |
| Journal | Colloids and Surfaces B: Biointerfaces |
| Volume | 128 |
| DOIs | |
| Publication status | Published - 2015 |
| MoE publication type | A1 Journal article-refereed |
Keywords
- milk protein
- casein
- enzymatic cross-linking
- transglutaminase
- air/water interface
- surface rheology