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Nina Aagaard Poulsen

Influence of desialylation of caseinomacropeptide on the denaturation and aggregation of whey proteins

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Influence of desialylation of caseinomacropeptide on the denaturation and aggregation of whey proteins. / Gaspard, Sophie J.; Sunds, Anne V.; Larsen, Lotte B.; Poulsen, Nina A.; O'Mahony, James A.; Kelly, Alan L.; Brodkorb, André.

I: Journal of Dairy Science, Bind 103, Nr. 6, 2020, s. 4975-4990.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Gaspard, SJ, Sunds, AV, Larsen, LB, Poulsen, NA, O'Mahony, JA, Kelly, AL & Brodkorb, A 2020, 'Influence of desialylation of caseinomacropeptide on the denaturation and aggregation of whey proteins', Journal of Dairy Science, bind 103, nr. 6, s. 4975-4990. https://doi.org/10.3168/jds.2019-17780

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Vancouver

Author

Gaspard, Sophie J. ; Sunds, Anne V. ; Larsen, Lotte B. ; Poulsen, Nina A. ; O'Mahony, James A. ; Kelly, Alan L. ; Brodkorb, André. / Influence of desialylation of caseinomacropeptide on the denaturation and aggregation of whey proteins. I: Journal of Dairy Science. 2020 ; Bind 103, Nr. 6. s. 4975-4990.

Bibtex

@article{2b816fe57c734054bd14a9116cec1998,
title = "Influence of desialylation of caseinomacropeptide on the denaturation and aggregation of whey proteins",
abstract = "The effect of the addition of caseinomacropeptide (CMP) or desialylated CMP on the heat-induced denaturation and aggregation of whey proteins was investigated in the pH range 3 to 7 after heating at 80°C for 30 min. The rate and temperature of denaturation, the extent of aggregation, and the changes in secondary structure of the whey proteins heated in presence of CMP or desialylated CMP were measured. The sialic acid bound to CMP favored the denaturation and aggregation of whey proteins when the whey proteins were oppositely charged to CMP at pH 4. A transition occurred at pH 6, below which the removal of sialic acid enhanced the stabilizing properties of CMP against the denaturation and aggregation of the whey proteins. At pH >6, the interactions between desialylated CMP and the whey proteins led to more extensive denaturation and aggregation. Sialic acid bound to CMP influenced the denaturation and aggregation behavior of whey proteins in a pH-dependent manner, and this should be considered in future studies on the heat stability of such systems containing CMP.",
keywords = "aggregation, caseinomacropeptide, denaturation, sialic acid, whey protein",
author = "Gaspard, {Sophie J.} and Sunds, {Anne V.} and Larsen, {Lotte B.} and Poulsen, {Nina A.} and O'Mahony, {James A.} and Kelly, {Alan L.} and Andr{\'e} Brodkorb",
year = "2020",
doi = "10.3168/jds.2019-17780",
language = "English",
volume = "103",
pages = "4975--4990",
journal = "Journal of Dairy Science",
issn = "0022-0302",
publisher = "Elsevier Inc.",
number = "6",

}

RIS

TY - JOUR

T1 - Influence of desialylation of caseinomacropeptide on the denaturation and aggregation of whey proteins

AU - Gaspard, Sophie J.

AU - Sunds, Anne V.

AU - Larsen, Lotte B.

AU - Poulsen, Nina A.

AU - O'Mahony, James A.

AU - Kelly, Alan L.

AU - Brodkorb, André

PY - 2020

Y1 - 2020

N2 - The effect of the addition of caseinomacropeptide (CMP) or desialylated CMP on the heat-induced denaturation and aggregation of whey proteins was investigated in the pH range 3 to 7 after heating at 80°C for 30 min. The rate and temperature of denaturation, the extent of aggregation, and the changes in secondary structure of the whey proteins heated in presence of CMP or desialylated CMP were measured. The sialic acid bound to CMP favored the denaturation and aggregation of whey proteins when the whey proteins were oppositely charged to CMP at pH 4. A transition occurred at pH 6, below which the removal of sialic acid enhanced the stabilizing properties of CMP against the denaturation and aggregation of the whey proteins. At pH >6, the interactions between desialylated CMP and the whey proteins led to more extensive denaturation and aggregation. Sialic acid bound to CMP influenced the denaturation and aggregation behavior of whey proteins in a pH-dependent manner, and this should be considered in future studies on the heat stability of such systems containing CMP.

AB - The effect of the addition of caseinomacropeptide (CMP) or desialylated CMP on the heat-induced denaturation and aggregation of whey proteins was investigated in the pH range 3 to 7 after heating at 80°C for 30 min. The rate and temperature of denaturation, the extent of aggregation, and the changes in secondary structure of the whey proteins heated in presence of CMP or desialylated CMP were measured. The sialic acid bound to CMP favored the denaturation and aggregation of whey proteins when the whey proteins were oppositely charged to CMP at pH 4. A transition occurred at pH 6, below which the removal of sialic acid enhanced the stabilizing properties of CMP against the denaturation and aggregation of the whey proteins. At pH >6, the interactions between desialylated CMP and the whey proteins led to more extensive denaturation and aggregation. Sialic acid bound to CMP influenced the denaturation and aggregation behavior of whey proteins in a pH-dependent manner, and this should be considered in future studies on the heat stability of such systems containing CMP.

KW - aggregation

KW - caseinomacropeptide

KW - denaturation

KW - sialic acid

KW - whey protein

UR - http://www.scopus.com/inward/record.url?scp=85082532606&partnerID=8YFLogxK

U2 - 10.3168/jds.2019-17780

DO - 10.3168/jds.2019-17780

M3 - Journal article

C2 - 32229125

AN - SCOPUS:85082532606

VL - 103

SP - 4975

EP - 4990

JO - Journal of Dairy Science

JF - Journal of Dairy Science

SN - 0022-0302

IS - 6

ER -