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Coacervates of Lactotransferrin and β- or κ-Casein: Structure Determined Using SAXS

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Coacervates of Lactotransferrin and β- or κ-Casein : Structure Determined Using SAXS. / de Kruif, C G Kees; Pedersen, Jan Skov; Huppertz, Thom; Anema, Skelte G.

In: Langmuir, Vol. 29, No. 33, 2013, p. 10483-10490.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

de Kruif, CGK, Pedersen, JS, Huppertz, T & Anema, SG 2013, 'Coacervates of Lactotransferrin and β- or κ-Casein: Structure Determined Using SAXS', Langmuir, vol. 29, no. 33, pp. 10483-10490. https://doi.org/10.1021/la402236f

APA

de Kruif, C. G. K., Pedersen, J. S., Huppertz, T., & Anema, S. G. (2013). Coacervates of Lactotransferrin and β- or κ-Casein: Structure Determined Using SAXS. Langmuir, 29(33), 10483-10490. https://doi.org/10.1021/la402236f

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MLA

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Author

de Kruif, C G Kees ; Pedersen, Jan Skov ; Huppertz, Thom ; Anema, Skelte G. / Coacervates of Lactotransferrin and β- or κ-Casein : Structure Determined Using SAXS. In: Langmuir. 2013 ; Vol. 29, No. 33. pp. 10483-10490.

Bibtex

@article{25ea64c902df409cb985ce2397184c39,
title = "Coacervates of Lactotransferrin and β- or κ-Casein: Structure Determined Using SAXS",
abstract = "Lactotransferrin (LF) is a large globular protein in milk with immune-regulatory and bactericidal properties. At pH 6.5, LF (M = 78 kDa) carries a net (calculated) charge of +21. β-Casein (BCN) and κ-casein (KCN) are part of the casein micelle complex in milk. Both BCN and KCN are amphiphillic proteins with a molar mass of 24 and 19 kDa and carry net charges of -14 and -4, respectively. Both BCN and KCN form soap-like micelles, with 40 and 65 monomers, respectively. The net negative charges are located in the corona of the micelles. On mixing LF with the caseins, coacervates are formed. We analyzed the structure of these coarcervates using SAXS. It was found that LF binds to the corona of the micellar structures, at the charge neutrality point. BCN/LF and KCN/LF ratios at the charge neutrality point were found to be ~1.2 and ~5, respectively. We think that the findings are relevant for the protection mechanism of globular proteins in bodily fluids where unstructured proteins are abundant (saliva). The complexes will prevent docking of enzymes on specific charged groups on the globular protein.",
author = "{de Kruif}, {C G Kees} and Pedersen, {Jan Skov} and Thom Huppertz and Anema, {Skelte G}",
year = "2013",
doi = "10.1021/la402236f",
language = "English",
volume = "29",
pages = "10483--10490",
journal = "Langmuir",
issn = "0743-7463",
publisher = "AMER CHEMICAL SOC",
number = "33",

}

RIS

TY - JOUR

T1 - Coacervates of Lactotransferrin and β- or κ-Casein

T2 - Structure Determined Using SAXS

AU - de Kruif, C G Kees

AU - Pedersen, Jan Skov

AU - Huppertz, Thom

AU - Anema, Skelte G

PY - 2013

Y1 - 2013

N2 - Lactotransferrin (LF) is a large globular protein in milk with immune-regulatory and bactericidal properties. At pH 6.5, LF (M = 78 kDa) carries a net (calculated) charge of +21. β-Casein (BCN) and κ-casein (KCN) are part of the casein micelle complex in milk. Both BCN and KCN are amphiphillic proteins with a molar mass of 24 and 19 kDa and carry net charges of -14 and -4, respectively. Both BCN and KCN form soap-like micelles, with 40 and 65 monomers, respectively. The net negative charges are located in the corona of the micelles. On mixing LF with the caseins, coacervates are formed. We analyzed the structure of these coarcervates using SAXS. It was found that LF binds to the corona of the micellar structures, at the charge neutrality point. BCN/LF and KCN/LF ratios at the charge neutrality point were found to be ~1.2 and ~5, respectively. We think that the findings are relevant for the protection mechanism of globular proteins in bodily fluids where unstructured proteins are abundant (saliva). The complexes will prevent docking of enzymes on specific charged groups on the globular protein.

AB - Lactotransferrin (LF) is a large globular protein in milk with immune-regulatory and bactericidal properties. At pH 6.5, LF (M = 78 kDa) carries a net (calculated) charge of +21. β-Casein (BCN) and κ-casein (KCN) are part of the casein micelle complex in milk. Both BCN and KCN are amphiphillic proteins with a molar mass of 24 and 19 kDa and carry net charges of -14 and -4, respectively. Both BCN and KCN form soap-like micelles, with 40 and 65 monomers, respectively. The net negative charges are located in the corona of the micelles. On mixing LF with the caseins, coacervates are formed. We analyzed the structure of these coarcervates using SAXS. It was found that LF binds to the corona of the micellar structures, at the charge neutrality point. BCN/LF and KCN/LF ratios at the charge neutrality point were found to be ~1.2 and ~5, respectively. We think that the findings are relevant for the protection mechanism of globular proteins in bodily fluids where unstructured proteins are abundant (saliva). The complexes will prevent docking of enzymes on specific charged groups on the globular protein.

U2 - 10.1021/la402236f

DO - 10.1021/la402236f

M3 - Journal article

C2 - 23859400

VL - 29

SP - 10483

EP - 10490

JO - Langmuir

JF - Langmuir

SN - 0743-7463

IS - 33

ER -