Temperature effects on calcium binding to caseins
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Temperature effects on calcium binding to caseins. / Liu, Xiao Chen; Jiang, Yuan; Ahrné, Lilia M.; Skibsted, Leif H.
In: Food Research International, Vol. 154, 110981, 2022.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Temperature effects on calcium binding to caseins
AU - Liu, Xiao Chen
AU - Jiang, Yuan
AU - Ahrné, Lilia M.
AU - Skibsted, Leif H.
N1 - Funding Information: This work was supported by the China Scholarship Council [CSC, No. 201806360266] and the Danish Dairy Research Council/Innovation Fund Denmark as the project Procalcium. We are grateful for the help with ICP measurement from Jing Wang at the Department of Food Science, University of Copenhagen. Funding Information: This work was supported by the China Scholarship Council [CSC, No. 201806360266 ] and the Danish Dairy Research Council/Innovation Fund Denmark as the project Procalcium. We are grateful for the help with ICP measurement from Jing Wang at the Department of Food Science, University of Copenhagen. Publisher Copyright: © 2022 The Authors
PY - 2022
Y1 - 2022
N2 - The kinetics of binding of calcium ions in molar excess to individual caseins and casein ingredients was studied in pH 6.4 aqueous solutions using stopped-flow absorption spectroscopy. An initial second-order reaction, faster for β-casein than for αs-casein due to lower energy of activation (ΔEa1,β = 8.2 kJ∙mol−1; ΔEa1,α = 18.1 kJ∙mol−1, respectively), is followed by a slower first-order reaction with similar energies of activation (ΔEa2,β = 25.3 kJ∙mol−1 and ΔEa2,α = 20.7 kJ∙mol−1) as determined from temperature dependence of rate between 25 °C and 50 °C. Sodium caseinate reacts faster with calcium than both αs-casein and β-casein in the first reaction of the two consecutive reactions, while the rate of the second falls between αs-casein and β-casein. Global spectral analysis showed the UV–visible spectra of the reaction intermediates of the caseins to be more similar to the final products than to the initial casein reactants. Dynamic and static light scattering indicated decreasing particle sizes and increasing particle surface upon calcium-binding most significantly at low temperatures. The calcium binding to casein was found endothermic by isothermal titration calorimetry. Calcium binding seems to be controlled by enthalpy/entropy compensation corresponding to an isoequilibrium temperature of 38 °C in agreement with binding of calcium to o-phosphoserine rather than to aspartate or glutamate side chains of the caseins. Binding capacity and affinity for calcium to αs-casein and sodium caseinate both increased with increasing temperature in agreement with the endothermic nature of the binding. Decreasing enthalpy of binding for each calcium indicating a decrease in heat capacity of the caseins upon calcium-binding. The small difference between binding enthalpy and energy of activation for association of calcium to αs-casein lead to the conclusion that calcium dissociation goes through an early transition state. The rate of calcium dissociation hardly depends on temperature also explaining why calcium binding to caseins is important for calcium bioaccessibility.
AB - The kinetics of binding of calcium ions in molar excess to individual caseins and casein ingredients was studied in pH 6.4 aqueous solutions using stopped-flow absorption spectroscopy. An initial second-order reaction, faster for β-casein than for αs-casein due to lower energy of activation (ΔEa1,β = 8.2 kJ∙mol−1; ΔEa1,α = 18.1 kJ∙mol−1, respectively), is followed by a slower first-order reaction with similar energies of activation (ΔEa2,β = 25.3 kJ∙mol−1 and ΔEa2,α = 20.7 kJ∙mol−1) as determined from temperature dependence of rate between 25 °C and 50 °C. Sodium caseinate reacts faster with calcium than both αs-casein and β-casein in the first reaction of the two consecutive reactions, while the rate of the second falls between αs-casein and β-casein. Global spectral analysis showed the UV–visible spectra of the reaction intermediates of the caseins to be more similar to the final products than to the initial casein reactants. Dynamic and static light scattering indicated decreasing particle sizes and increasing particle surface upon calcium-binding most significantly at low temperatures. The calcium binding to casein was found endothermic by isothermal titration calorimetry. Calcium binding seems to be controlled by enthalpy/entropy compensation corresponding to an isoequilibrium temperature of 38 °C in agreement with binding of calcium to o-phosphoserine rather than to aspartate or glutamate side chains of the caseins. Binding capacity and affinity for calcium to αs-casein and sodium caseinate both increased with increasing temperature in agreement with the endothermic nature of the binding. Decreasing enthalpy of binding for each calcium indicating a decrease in heat capacity of the caseins upon calcium-binding. The small difference between binding enthalpy and energy of activation for association of calcium to αs-casein lead to the conclusion that calcium dissociation goes through an early transition state. The rate of calcium dissociation hardly depends on temperature also explaining why calcium binding to caseins is important for calcium bioaccessibility.
KW - Intermediate spectrum
KW - Isothermal titration calorimetry
KW - Sodium caseinate
KW - Stepwise calcium association
KW - Stopped-flow spectroscopy
KW - α-casein
U2 - 10.1016/j.foodres.2022.110981
DO - 10.1016/j.foodres.2022.110981
M3 - Journal article
C2 - 35337555
AN - SCOPUS:85125474983
VL - 154
JO - Food Research International
JF - Food Research International
SN - 0963-9969
M1 - 110981
ER -
ID: 300067049