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

5 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

Fingerprint

Casein
Transglutaminases
Caseins
proteins
Proteins
enzymes
Enzymes
Food technology
Air
interactions
Food Technology
Water
Rheology
air
Emulsions
Molecular Structure
rheology
food
foams
Molecular structure

Keywords

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

Cite this

Ridout, Michael J. ; Paananen, Arja ; Mamode, Anissa ; Linder, Markus B. ; Wilde, Peter J. / Interaction of transglutaminase with adsorbed and spread films of [beta]-casein and [kappa]-casein. In: Colloids and Surfaces B: Biointerfaces. 2015 ; Vol. 128. pp. 254-260.
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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.",
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Interaction of transglutaminase with adsorbed and spread films of [beta]-casein and [kappa]-casein. / Ridout, Michael J.; Paananen, Arja; Mamode, Anissa; Linder, Markus B.; Wilde, Peter J.

In: Colloids and Surfaces B: Biointerfaces, Vol. 128, 2015, p. 254-260.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Interaction of transglutaminase with adsorbed and spread films of [beta]-casein and [kappa]-casein

AU - Ridout, Michael J.

AU - Paananen, Arja

AU - Mamode, Anissa

AU - Linder, Markus B.

AU - Wilde, Peter J.

PY - 2015

Y1 - 2015

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AB - 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.

KW - milk protein

KW - casein

KW - enzymatic cross-linking

KW - transglutaminase

KW - air/water interface

KW - surface rheology

U2 - 10.1016/j.colsurfb.2015.01.045

DO - 10.1016/j.colsurfb.2015.01.045

M3 - Article

VL - 128

SP - 254

EP - 260

JO - Colloids and Surfaces B: Biointerfaces

JF - Colloids and Surfaces B: Biointerfaces

SN - 0927-7765

ER -