Binding of calcium to L-serine and o-phospho-L-serine as affected by temperature, pH and ionic strength under milk processing conditions

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Binding of calcium to L-serine and o-phospho-L-serine as affected by temperature, pH and ionic strength under milk processing conditions. / Jiang, Yuan; Liu, Xiao-Chen; de Zawadzki, Andressa; Skibsted, Leif H.

I: International Dairy Journal, Bind 112, 104875, 2021.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Jiang, Y, Liu, X-C, de Zawadzki, A & Skibsted, LH 2021, 'Binding of calcium to L-serine and o-phospho-L-serine as affected by temperature, pH and ionic strength under milk processing conditions', International Dairy Journal, bind 112, 104875. https://doi.org/10.1016/j.idairyj.2020.104875

APA

Jiang, Y., Liu, X-C., de Zawadzki, A., & Skibsted, L. H. (2021). Binding of calcium to L-serine and o-phospho-L-serine as affected by temperature, pH and ionic strength under milk processing conditions. International Dairy Journal, 112, [104875]. https://doi.org/10.1016/j.idairyj.2020.104875

Vancouver

Jiang Y, Liu X-C, de Zawadzki A, Skibsted LH. Binding of calcium to L-serine and o-phospho-L-serine as affected by temperature, pH and ionic strength under milk processing conditions. International Dairy Journal. 2021;112. 104875. https://doi.org/10.1016/j.idairyj.2020.104875

Author

Jiang, Yuan ; Liu, Xiao-Chen ; de Zawadzki, Andressa ; Skibsted, Leif H. / Binding of calcium to L-serine and o-phospho-L-serine as affected by temperature, pH and ionic strength under milk processing conditions. I: International Dairy Journal. 2021 ; Bind 112.

Bibtex

@article{2883572b12f34217b3c695cd5c617c3c,
title = "Binding of calcium to L-serine and o-phospho-L-serine as affected by temperature, pH and ionic strength under milk processing conditions",
abstract = "Calcium binding to o-phospho-L-serine (OPS), important for calcium distribution during milk processing and for calcium bioavailability, was studied electrochemically for different conditions of temperature, pH and ionic strength in combination with quantum mechanical calculations (DFT) using L-serine (Ser) as a reference compound. Calcium binding increases strongly with increasing pH for both Ser and OPS. pH dependent binding of calcium ions was resolved using pKa values into, respectively, Kass,1, Kass,2 and Kass,3 = 20, 37 and 180 L mol−1 with ΔH0ass,1 ΔH0ass,2 ΔH0ass,3 = 16, −7.4 and −11 kJ mol−1 for binding to OPS−, OPS2− and OPS3− at an ionic strength 0.2 and 15 °C. Dissolution of CaOPS at milk pH was endothermic. The shift from endothermic binding of calcium to OPS at low pH to exothermic binding at higher pH, corresponding to a shift from hydrophobic interaction (phosphate ester) to ionic binding (carboxylate/amino chelation), was supported by DFT.",
author = "Yuan Jiang and Xiao-Chen Liu and {de Zawadzki}, Andressa and Skibsted, {Leif H.}",
year = "2021",
doi = "10.1016/j.idairyj.2020.104875",
language = "English",
volume = "112",
journal = "International Dairy Journal",
issn = "0958-6946",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Binding of calcium to L-serine and o-phospho-L-serine as affected by temperature, pH and ionic strength under milk processing conditions

AU - Jiang, Yuan

AU - Liu, Xiao-Chen

AU - de Zawadzki, Andressa

AU - Skibsted, Leif H.

PY - 2021

Y1 - 2021

N2 - Calcium binding to o-phospho-L-serine (OPS), important for calcium distribution during milk processing and for calcium bioavailability, was studied electrochemically for different conditions of temperature, pH and ionic strength in combination with quantum mechanical calculations (DFT) using L-serine (Ser) as a reference compound. Calcium binding increases strongly with increasing pH for both Ser and OPS. pH dependent binding of calcium ions was resolved using pKa values into, respectively, Kass,1, Kass,2 and Kass,3 = 20, 37 and 180 L mol−1 with ΔH0ass,1 ΔH0ass,2 ΔH0ass,3 = 16, −7.4 and −11 kJ mol−1 for binding to OPS−, OPS2− and OPS3− at an ionic strength 0.2 and 15 °C. Dissolution of CaOPS at milk pH was endothermic. The shift from endothermic binding of calcium to OPS at low pH to exothermic binding at higher pH, corresponding to a shift from hydrophobic interaction (phosphate ester) to ionic binding (carboxylate/amino chelation), was supported by DFT.

AB - Calcium binding to o-phospho-L-serine (OPS), important for calcium distribution during milk processing and for calcium bioavailability, was studied electrochemically for different conditions of temperature, pH and ionic strength in combination with quantum mechanical calculations (DFT) using L-serine (Ser) as a reference compound. Calcium binding increases strongly with increasing pH for both Ser and OPS. pH dependent binding of calcium ions was resolved using pKa values into, respectively, Kass,1, Kass,2 and Kass,3 = 20, 37 and 180 L mol−1 with ΔH0ass,1 ΔH0ass,2 ΔH0ass,3 = 16, −7.4 and −11 kJ mol−1 for binding to OPS−, OPS2− and OPS3− at an ionic strength 0.2 and 15 °C. Dissolution of CaOPS at milk pH was endothermic. The shift from endothermic binding of calcium to OPS at low pH to exothermic binding at higher pH, corresponding to a shift from hydrophobic interaction (phosphate ester) to ionic binding (carboxylate/amino chelation), was supported by DFT.

UR - http://www.scopus.com/inward/record.url?scp=85092532449&partnerID=8YFLogxK

U2 - 10.1016/j.idairyj.2020.104875

DO - 10.1016/j.idairyj.2020.104875

M3 - Journal article

AN - SCOPUS:85092532449

VL - 112

JO - International Dairy Journal

JF - International Dairy Journal

SN - 0958-6946

M1 - 104875

ER -

ID: 251257866