Temperature effect on calcium binding to aspartate and glutamate

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Temperature effect on calcium binding to aspartate and glutamate. / Liu, Xiao-Chen; Liu, Jingyuan; Skibsted, Leif H.

I: Food Research International, Bind 159, 111625, 2022.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Liu, X-C, Liu, J & Skibsted, LH 2022, 'Temperature effect on calcium binding to aspartate and glutamate', Food Research International, bind 159, 111625. https://doi.org/10.1016/j.foodres.2022.111625

APA

Liu, X-C., Liu, J., & Skibsted, L. H. (2022). Temperature effect on calcium binding to aspartate and glutamate. Food Research International, 159, [111625]. https://doi.org/10.1016/j.foodres.2022.111625

Vancouver

Liu X-C, Liu J, Skibsted LH. Temperature effect on calcium binding to aspartate and glutamate. Food Research International. 2022;159. 111625. https://doi.org/10.1016/j.foodres.2022.111625

Author

Liu, Xiao-Chen ; Liu, Jingyuan ; Skibsted, Leif H. / Temperature effect on calcium binding to aspartate and glutamate. I: Food Research International. 2022 ; Bind 159.

Bibtex

@article{f26e312c72fd4a6b8542b5819914add6,
title = "Temperature effect on calcium binding to aspartate and glutamate",
abstract = "Aspartate (Asp) mononegative ion binds calcium through both carboxylates in contrast to binding through only the side chain carboxylate for mononegative glutamate (Glu), as shown by density functional theory (DFT) calculations. A stronger binding was confirmed electrochemically for Asp compared to Glu. From temperature dependence of binding constant, 15–37 °C investigated for aqueous 0.16 M NaCl, a more negative ΔH0 of − 21 kJ·mol−1 was found for Glu compared to ΔH0 = −17 kJ·mol−1 for Asp, a difference confirmed by DFT calculations and qualitatively also by isothermal titration calorimetry. The stronger binding of calcium to Asp (Kass,c = 5.3 M−1 at 37 °C) compared to Glu (Kass,c = 3.6 M−1 at 37 °C) despite the less negative enthalpy of binding is accordingly an entropy effect due to ring formation in the complex for Asp.",
keywords = "Calcium, Casein, DFT calculations, Electrochemical measurements, Isothermal titration calorimetry",
author = "Xiao-Chen Liu and Jingyuan Liu and Skibsted, {Leif H.}",
note = "Publisher Copyright: {\textcopyright} 2022 The Author(s)",
year = "2022",
doi = "10.1016/j.foodres.2022.111625",
language = "English",
volume = "159",
journal = "Food Research International",
issn = "0963-9969",
publisher = "Pergamon Press",

}

RIS

TY - JOUR

T1 - Temperature effect on calcium binding to aspartate and glutamate

AU - Liu, Xiao-Chen

AU - Liu, Jingyuan

AU - Skibsted, Leif H.

N1 - Publisher Copyright: © 2022 The Author(s)

PY - 2022

Y1 - 2022

N2 - Aspartate (Asp) mononegative ion binds calcium through both carboxylates in contrast to binding through only the side chain carboxylate for mononegative glutamate (Glu), as shown by density functional theory (DFT) calculations. A stronger binding was confirmed electrochemically for Asp compared to Glu. From temperature dependence of binding constant, 15–37 °C investigated for aqueous 0.16 M NaCl, a more negative ΔH0 of − 21 kJ·mol−1 was found for Glu compared to ΔH0 = −17 kJ·mol−1 for Asp, a difference confirmed by DFT calculations and qualitatively also by isothermal titration calorimetry. The stronger binding of calcium to Asp (Kass,c = 5.3 M−1 at 37 °C) compared to Glu (Kass,c = 3.6 M−1 at 37 °C) despite the less negative enthalpy of binding is accordingly an entropy effect due to ring formation in the complex for Asp.

AB - Aspartate (Asp) mononegative ion binds calcium through both carboxylates in contrast to binding through only the side chain carboxylate for mononegative glutamate (Glu), as shown by density functional theory (DFT) calculations. A stronger binding was confirmed electrochemically for Asp compared to Glu. From temperature dependence of binding constant, 15–37 °C investigated for aqueous 0.16 M NaCl, a more negative ΔH0 of − 21 kJ·mol−1 was found for Glu compared to ΔH0 = −17 kJ·mol−1 for Asp, a difference confirmed by DFT calculations and qualitatively also by isothermal titration calorimetry. The stronger binding of calcium to Asp (Kass,c = 5.3 M−1 at 37 °C) compared to Glu (Kass,c = 3.6 M−1 at 37 °C) despite the less negative enthalpy of binding is accordingly an entropy effect due to ring formation in the complex for Asp.

KW - Calcium

KW - Casein

KW - DFT calculations

KW - Electrochemical measurements

KW - Isothermal titration calorimetry

U2 - 10.1016/j.foodres.2022.111625

DO - 10.1016/j.foodres.2022.111625

M3 - Journal article

C2 - 35940812

AN - SCOPUS:85134348434

VL - 159

JO - Food Research International

JF - Food Research International

SN - 0963-9969

M1 - 111625

ER -

ID: 317503033