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

doi:10.1016/j.foodhyd.2022.108373

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

Department of Molecular Biology and Genetics - Cellular Health, Intervention, and Nutrition

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Abstract

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 language	English
Article number	108373
Journal	Food Hydrocolloids
Volume	137
Number of pages	12
ISSN	0268-005X
DOIs	https://doi.org/10.1016/j.foodhyd.2022.108373
Publication status	Published - Apr 2023

Keywords

Aggregation propensity
Caseins
Chaperone
Colloidal stability
Milk
β-lactoglobulin

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Mohammad-Beigi, H., Wijaya, W., Madsen, M., Hayashi, Y., Li, R., Maria Rovers, T. A., Jæger, T. C., Buell, A. K., Hougaard, A. B., Kirkensgaard, J. J. K., Westh, P., Ipsen, R., & Svensson, B. (2023). Association of caseins with β-lactoglobulin influenced by temperature and calcium ions: A multi-parameter analysis. Food Hydrocolloids, 137, Article 108373. https://doi.org/10.1016/j.foodhyd.2022.108373

@article{8eace07d38a0494481c06a82f2f9978a,

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

abstract = "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.",

keywords = "Aggregation propensity, Caseins, Chaperone, Colloidal stability, Milk, β-lactoglobulin",

author = "Hossein Mohammad-Beigi and Wahyu Wijaya and Mikkel Madsen and Yuya Hayashi and Ruifen Li and {Maria Rovers}, {Tijs Albert} and J{\ae}ger, {Tanja Christine} and Buell, {Alexander K.} and Hougaard, {Anni Bygvr{\aa}} and Kirkensgaard, {Jacob J.K.} and Peter Westh and Richard Ipsen and Birte Svensson",

year = "2023",

month = apr,

doi = "10.1016/j.foodhyd.2022.108373",

language = "English",

volume = "137",

journal = "Food Hydrocolloids",

issn = "0268-005X",

publisher = "Elsevier BV",

}

Mohammad-Beigi, H, Wijaya, W, Madsen, M, Hayashi, Y, Li, R, Maria Rovers, TA, Jæger, TC, Buell, AK, Hougaard, AB, Kirkensgaard, JJK, Westh, P, Ipsen, R & Svensson, B 2023, 'Association of caseins with β-lactoglobulin influenced by temperature and calcium ions: A multi-parameter analysis', Food Hydrocolloids, vol. 137, 108373. https://doi.org/10.1016/j.foodhyd.2022.108373

Association of caseins with β-lactoglobulin influenced by temperature and calcium ions: A multi-parameter analysis. / Mohammad-Beigi, Hossein; Wijaya, Wahyu; Madsen, Mikkel et al.
In: Food Hydrocolloids, Vol. 137, 108373, 04.2023.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

TY - JOUR

T1 - Association of caseins with β-lactoglobulin influenced by temperature and calcium ions

T2 - A multi-parameter analysis

AU - Mohammad-Beigi, Hossein

AU - Wijaya, Wahyu

AU - Madsen, Mikkel

AU - Hayashi, Yuya

AU - Li, Ruifen

AU - Maria Rovers, Tijs Albert

AU - Jæger, Tanja Christine

AU - Buell, Alexander K.

AU - Hougaard, Anni Bygvrå

AU - Kirkensgaard, Jacob J.K.

AU - Westh, Peter

AU - Ipsen, Richard

AU - Svensson, Birte

PY - 2023/4

Y1 - 2023/4

N2 - 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.

AB - 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.

KW - Aggregation propensity

KW - Caseins

KW - Chaperone

KW - Colloidal stability

KW - Milk

KW - β-lactoglobulin

U2 - 10.1016/j.foodhyd.2022.108373

DO - 10.1016/j.foodhyd.2022.108373

M3 - Journal article

SN - 0268-005X

VL - 137

JO - Food Hydrocolloids

JF - Food Hydrocolloids

M1 - 108373

ER -

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

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Keywords

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