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Daniel Otzen

Stabilizing vitamin D₃ using the molten globule state of α-lactalbumin

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Stabilizing vitamin D₃ using the molten globule state of α-lactalbumin. / Pedersen, Jannik Nedergaard; Sørensen, Henrik V ; Otzen, Daniel E.

In: Journal of Dairy Science, Vol. 101, No. 3, 03.2018, p. 1817–1826.

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

Vancouver

Pedersen JN, Sørensen HV , Otzen DE. Stabilizing vitamin D₃ using the molten globule state of α-lactalbumin. Journal of Dairy Science. 2018 Mar;101(3):1817–1826. Epub 2018 Jan 10. doi: 10.3168/jds.2017-13818

Author

Pedersen, Jannik Nedergaard ; Sørensen, Henrik V ; Otzen, Daniel E. / Stabilizing vitamin D₃ using the molten globule state of α-lactalbumin. In: Journal of Dairy Science. 2018 ; Vol. 101, No. 3. pp. 1817–1826.

Bibtex

@article{c22336b952d84f149015fd217eff913c,

title = "Stabilizing vitamin D3 using the molten globule state of α-lactalbumin",

abstract = "α-Lactalbumin (α-LA) is the second most abundant bovine whey protein. It has been intensively studied because of its readiness to populate the molten globular (MG) state, a partially folded state with native levels of secondary structure but loss of tertiary structure. The MG state of α-LA exposes a significant number of hydrophobic patches that could be used to bind and stabilize small hydrophobic molecules such as vitamin D3 (vitD). Accordingly, we tested the ability of α-LA to stabilize vitD in a pH interval from 7.4 to 2; over this pH interval, α-LA transitions from the folded state to the MG state. The MG state stabilized vitD better than the folded state and was superior to the major bovine whey protein β-lactoglobulin (β-LG), which is known to stabilize vitD. At pH 7.4, β-LG and α-LA stabilized vitD to the same extent. Tryptophan fluorescence quenching measurements indicated that α-LA has one binding site at pH 7.4 but acquires an additional binding site when the pH is lowered to pH 2 to 4. Stability measurements of the vitD in the α-LA-vitD complex at different temperatures suggest that UHT processing would lead to little loss of vitD. This study demonstrates the potential of α-LA as a component in vitD fortification, particularly for low pH applications.",

keywords = "Journal Article",

author = "Pedersen, {Jannik Nedergaard} and S{\o}rensen, {Henrik V} and Otzen, {Daniel E}",

year = "2018",

month = mar,

doi = "10.3168/jds.2017-13818",

language = "English",

volume = "101",

pages = "1817–1826",

journal = "Journal of Dairy Science",

issn = "0022-0302",

publisher = "Elsevier Inc.",

number = "3",

}

RIS

TY - JOUR

T1 - Stabilizing vitamin D3 using the molten globule state of α-lactalbumin

AU - Pedersen, Jannik Nedergaard

AU - Sørensen, Henrik V

AU - Otzen, Daniel E

PY - 2018/3

Y1 - 2018/3

N2 - α-Lactalbumin (α-LA) is the second most abundant bovine whey protein. It has been intensively studied because of its readiness to populate the molten globular (MG) state, a partially folded state with native levels of secondary structure but loss of tertiary structure. The MG state of α-LA exposes a significant number of hydrophobic patches that could be used to bind and stabilize small hydrophobic molecules such as vitamin D3 (vitD). Accordingly, we tested the ability of α-LA to stabilize vitD in a pH interval from 7.4 to 2; over this pH interval, α-LA transitions from the folded state to the MG state. The MG state stabilized vitD better than the folded state and was superior to the major bovine whey protein β-lactoglobulin (β-LG), which is known to stabilize vitD. At pH 7.4, β-LG and α-LA stabilized vitD to the same extent. Tryptophan fluorescence quenching measurements indicated that α-LA has one binding site at pH 7.4 but acquires an additional binding site when the pH is lowered to pH 2 to 4. Stability measurements of the vitD in the α-LA-vitD complex at different temperatures suggest that UHT processing would lead to little loss of vitD. This study demonstrates the potential of α-LA as a component in vitD fortification, particularly for low pH applications.

AB - α-Lactalbumin (α-LA) is the second most abundant bovine whey protein. It has been intensively studied because of its readiness to populate the molten globular (MG) state, a partially folded state with native levels of secondary structure but loss of tertiary structure. The MG state of α-LA exposes a significant number of hydrophobic patches that could be used to bind and stabilize small hydrophobic molecules such as vitamin D3 (vitD). Accordingly, we tested the ability of α-LA to stabilize vitD in a pH interval from 7.4 to 2; over this pH interval, α-LA transitions from the folded state to the MG state. The MG state stabilized vitD better than the folded state and was superior to the major bovine whey protein β-lactoglobulin (β-LG), which is known to stabilize vitD. At pH 7.4, β-LG and α-LA stabilized vitD to the same extent. Tryptophan fluorescence quenching measurements indicated that α-LA has one binding site at pH 7.4 but acquires an additional binding site when the pH is lowered to pH 2 to 4. Stability measurements of the vitD in the α-LA-vitD complex at different temperatures suggest that UHT processing would lead to little loss of vitD. This study demonstrates the potential of α-LA as a component in vitD fortification, particularly for low pH applications.

KW - Journal Article

U2 - 10.3168/jds.2017-13818

DO - 10.3168/jds.2017-13818

M3 - Journal article

C2 - 29331461

VL - 101

SP - 1817

EP - 1826

JO - Journal of Dairy Science

JF - Journal of Dairy Science

SN - 0022-0302

IS - 3

ER -