Interaction of transglutaminase with adsorbed and spread films of [beta]-casein and [kappa]-casein

Michael J. Ridout, Arja Paananen, Anissa Mamode, Markus B. Linder, Peter J. Wilde

Research output: Contribution to journalArticleScientificpeer-review

7 Citations (Scopus)

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 languageEnglish
Pages (from-to)254-260
JournalColloids and Surfaces B: Biointerfaces
Volume128
DOIs
Publication statusPublished - 2015
MoE publication typeA1 Journal article-refereed

Keywords

  • milk protein
  • casein
  • enzymatic cross-linking
  • transglutaminase
  • air/water interface
  • surface rheology

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