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

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

DOI

  • Hossein Mohammad-Beigi, Danmarks Tekniske Universitet, Danmark
  • Wahyu Wijaya, Danmarks Tekniske Universitet, Danmark
  • Mikkel Madsen, Danmarks Tekniske Universitet, Danmark
  • Yuya Hayashi
  • Ruifen Li, Københavns Universitet
    • ,
  • Tijs Albert Maria Rovers, Arla Foods, Danmark
  • Tanja Christine Jæger, Arla Foods, Danmark
  • Alexander K. Buell, Danmarks Tekniske Universitet, Danmark
  • Anni Bygvrå Hougaard, Københavns Universitet, Danmark
  • Jacob J.K. Kirkensgaard, Københavns Universitet, Danmark
  • Peter Westh, Danmarks Tekniske Universitet, Danmark
  • Richard Ipsen, Københavns Universitet, Danmark
  • Birte Svensson, Danmarks Tekniske Universitet, Danmark
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.
OriginalsprogEngelsk
Artikelnummer108373
TidsskriftFood Hydrocolloids
Vol/bind137
Antal sider12
ISSN0268-005X
DOI
StatusUdgivet - apr. 2023

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