Size Modulation of Enzymatically Cross-Linked Sodium Caseinate Nanoparticles via Ionic Strength Variation Affects the Properties of Acid-Induced Gels

Norbert Raak*, Lars Leonhardt, Harald Rohm, Doris Jaros

*Corresponding author for this work

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

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Abstract

Enzymatic cross-linking by microbial transglutaminase is a prominent approach to modify the structure and techno-functional properties of food proteins such as casein. However, some of the factors that influence structure-function-interrelations are still unknown. In this study, the size of cross-linked sodium caseinate nanoparticles was modulated by varying the ionic milieu during incubation with the enzyme. As was revealed by size exclusion chromatography, cross-linking at higher ionic strength resulted in larger casein particles. These formed acid-induced gels with higher stiffness and lower susceptibility to forced syneresis compared to those where the same number of ions was added after the cross-linking process. The results show that variations of the ionic milieu during enzymatic cross-linking of casein can be helpful to obtain specific modifications of its molecular structure and certain techno-functional properties. Such knowledge is crucial for the design of protein ingredients with targeted structure and techno-functionality.
Original languageEnglish
JournalDairy - Open Access Journal
Volume2
Issue1
Pages (from-to)148-164
Number of pages17
ISSN2624-862X
DOIs
Publication statusPublished - Mar 2021

Keywords

  • acidification
  • casein
  • cross-linking
  • forced syneresis
  • gelation
  • ionic milieu
  • milk protein
  • size exclusion chromatography
  • structure-function-interrelations
  • transglutaminase

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