Association of caseins with β-lactoglobulin influenced by temperature and calcium ions: A multi-parameter analysis

Hossein Mohammad-Beigi*, Wahyu Wijaya, Mikkel Madsen, Yuya Hayashi, Ruifen Li, Tijs Albert Maria Rovers, Tanja Christine Jæger, Alexander K. Buell, Anni Bygvrå Hougaard, Jacob J.K. Kirkensgaard, Peter Westh, Richard Ipsen, Birte Svensson*

*Corresponding author for this work

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Aggregation of the major whey protein in bovine milk, β-lactoglobulin (β-Lg) is strongly influenced by association with caseins (CNs). Here, by using combined differential scanning fluorimetry and dynamic light scattering, the conformational stability and aggregation propensity of β-Lg and three types of CNs (α, β and ĸCNs) as well as their mixture have been systematically evaluated at different temperatures and Ca2+ concentrations in a multi-parametric approach. While β-Lg was affected significantly through denaturation and resulting aggregation by heat treatment with little dependency on Ca2+, αCN and βCN were influenced considerably by Ca2+. Through modifying the aggregation of β-Lg, CNs showed a different chaperone-like activity among the three types which were markedly dependent on the temperature and Ca2+ concentration. The presence of CNs resulted in smaller mixed aggregates compared to pure β-Lg aggregates, mainly through interaction of CNs with unfolded β-Lg and also by influencing the process of β-Lg unfolding. This was further confirmed by small angle X-ray scattering and isothermal titration calorimetry indicating that Ca2+ enhanced the interaction between β-Lg and CNs. Our experimental approach sheds light on molecular understanding of CN-β-Lg interactions and provides insight into how micro-structural assembly of milk proteins can be modulated to enable different functionalities in milk-based products.
Original languageEnglish
Article number108373
JournalFood Hydrocolloids
Number of pages12
Publication statusPublished - 2023


  • Aggregation propensity
  • β-lactoglobulin
  • Caseins
  • Chaperon
  • Milk
  • Collodial stability


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