Influence of calcium and magnesium on the secondary structure in solutions of individual caseins and binary casein mixtures

Manpreet Kaur Grewal; Todor Vasiljevic; Thom Huppertz

doi:10.1016/j.idairyj.2020.104879

Influence of calcium and magnesium on the secondary structure in solutions of individual caseins and binary casein mixtures

Manpreet Kaur Grewal, Todor Vasiljevic, Thom Huppertz^*

^*Corresponding author for this work

Food Quality and Design

Research output: Contribution to journal › Article › Academic › peer-review

17 Citations (Scopus)

Abstract

The influence of Ca and Mg addition on the secondary structure of α_S1-, α_S2-, β- and κ-CN in solutions of individual and binary mixtures of caseins was investigated using FTIR spectroscopy. Both in individual and their binary mixtures, addition of Ca and Mg resulted in increase in β-sheet structures and decrease in triple helices and turns, implying binding of cations to similar sites. Binding of cations with phosphoseryl clusters with loop-helix-loop motifs explained the reduction in helical element. In addition, the binding of cations to electronegative regions reduced electrostatic repulsion, resulting in an increase in hydrophobic interactions accounting for increase in sheet structures. Compared with Mg, it seemed that Ca had more affinity for caseins, especially when they were in a binary mixture. The information presented here expands the present understanding of casein interactions.

Original language	English
Article number	104879
Journal	International Dairy Journal
Volume	112
Early online date	28 Sept 2020
DOIs	https://doi.org/10.1016/j.idairyj.2020.104879
Publication status	Published - Jan 2021

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title = "Influence of calcium and magnesium on the secondary structure in solutions of individual caseins and binary casein mixtures",

abstract = "The influence of Ca and Mg addition on the secondary structure of αS1-, αS2-, β- and κ-CN in solutions of individual and binary mixtures of caseins was investigated using FTIR spectroscopy. Both in individual and their binary mixtures, addition of Ca and Mg resulted in increase in β-sheet structures and decrease in triple helices and turns, implying binding of cations to similar sites. Binding of cations with phosphoseryl clusters with loop-helix-loop motifs explained the reduction in helical element. In addition, the binding of cations to electronegative regions reduced electrostatic repulsion, resulting in an increase in hydrophobic interactions accounting for increase in sheet structures. Compared with Mg, it seemed that Ca had more affinity for caseins, especially when they were in a binary mixture. The information presented here expands the present understanding of casein interactions.",

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T1 - Influence of calcium and magnesium on the secondary structure in solutions of individual caseins and binary casein mixtures

AU - Grewal, Manpreet Kaur

AU - Vasiljevic, Todor

AU - Huppertz, Thom

PY - 2021/1

Y1 - 2021/1

N2 - The influence of Ca and Mg addition on the secondary structure of αS1-, αS2-, β- and κ-CN in solutions of individual and binary mixtures of caseins was investigated using FTIR spectroscopy. Both in individual and their binary mixtures, addition of Ca and Mg resulted in increase in β-sheet structures and decrease in triple helices and turns, implying binding of cations to similar sites. Binding of cations with phosphoseryl clusters with loop-helix-loop motifs explained the reduction in helical element. In addition, the binding of cations to electronegative regions reduced electrostatic repulsion, resulting in an increase in hydrophobic interactions accounting for increase in sheet structures. Compared with Mg, it seemed that Ca had more affinity for caseins, especially when they were in a binary mixture. The information presented here expands the present understanding of casein interactions.

AB - The influence of Ca and Mg addition on the secondary structure of αS1-, αS2-, β- and κ-CN in solutions of individual and binary mixtures of caseins was investigated using FTIR spectroscopy. Both in individual and their binary mixtures, addition of Ca and Mg resulted in increase in β-sheet structures and decrease in triple helices and turns, implying binding of cations to similar sites. Binding of cations with phosphoseryl clusters with loop-helix-loop motifs explained the reduction in helical element. In addition, the binding of cations to electronegative regions reduced electrostatic repulsion, resulting in an increase in hydrophobic interactions accounting for increase in sheet structures. Compared with Mg, it seemed that Ca had more affinity for caseins, especially when they were in a binary mixture. The information presented here expands the present understanding of casein interactions.

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DO - 10.1016/j.idairyj.2020.104879

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VL - 112

JO - International Dairy Journal

JF - International Dairy Journal

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Influence of calcium and magnesium on the secondary structure in solutions of individual caseins and binary casein mixtures

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