Oxidation of Whey Proteins during Thermal Treatment Characterized by a Site-Specific LC–MS/MS-Based Proteomic Approach

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Standard

Oxidation of Whey Proteins during Thermal Treatment Characterized by a Site-Specific LC–MS/MS-Based Proteomic Approach. / Li, Chengkang; Nielsen, Søren B. ; Engholm-Keller, Kasper; Lund, Marianne N.

In: Journal of Agricultural and Food Chemistry, Vol. 70, No. 14, 2022, p. 4391-4406.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Li, C, Nielsen, SB, Engholm-Keller, K & Lund, MN 2022, 'Oxidation of Whey Proteins during Thermal Treatment Characterized by a Site-Specific LC–MS/MS-Based Proteomic Approach', Journal of Agricultural and Food Chemistry, vol. 70, no. 14, pp. 4391-4406. https://doi.org/10.1021/acs.jafc.1c07946

APA

Li, C., Nielsen, S. B., Engholm-Keller, K., & Lund, M. N. (2022). Oxidation of Whey Proteins during Thermal Treatment Characterized by a Site-Specific LC–MS/MS-Based Proteomic Approach. Journal of Agricultural and Food Chemistry, 70(14), 4391-4406. https://doi.org/10.1021/acs.jafc.1c07946

Vancouver

Li C, Nielsen SB, Engholm-Keller K, Lund MN. Oxidation of Whey Proteins during Thermal Treatment Characterized by a Site-Specific LC–MS/MS-Based Proteomic Approach. Journal of Agricultural and Food Chemistry. 2022;70(14):4391-4406. https://doi.org/10.1021/acs.jafc.1c07946

Author

Li, Chengkang ; Nielsen, Søren B. ; Engholm-Keller, Kasper ; Lund, Marianne N. / Oxidation of Whey Proteins during Thermal Treatment Characterized by a Site-Specific LC–MS/MS-Based Proteomic Approach. In: Journal of Agricultural and Food Chemistry. 2022 ; Vol. 70, No. 14. pp. 4391-4406.

Bibtex

@article{37cbedd47d0643de841f4d2172fde614,
title = "Oxidation of Whey Proteins during Thermal Treatment Characterized by a Site-Specific LC–MS/MS-Based Proteomic Approach",
abstract = "Thermal treatment is often employed in food processing to tailor product properties by manipulating the ingredient functionality, but these elevated temperatures may accelerate oxidation and nutrient loss. Here, oxidation of different whey protein systems [α-lactalbumin (α-LA), β-lactoglobulin (β-LG), a mix of α-LA and β-LG (whey model), and a commercial whey protein isolate (WPI)] was investigated during heat treatment at 60–90 °C and a UHT-like treatment by LC-MS-based proteomic analysis. The relative modification levels of each oxidation site were calculated and compared among different heat treatments and sample systems. Oxidation increased significantly in protein systems after heating at ≥90 °C but decreased in systems with higher complexity [pure protein (α-LA > β-LG) > whey model > WPI]. In α-LA, Cys, Met, and Trp residues were found to be most prone to oxidation. In β-LG-containing protein systems, Cys residues were suggested to scavenge most of the reactive oxidants and undergo an oxidation-mediated disulfide rearrangement. The rearranged disulfide bonds contributed to protein aggregation, which was suggested to provide physical protection against oxidation. Overall, limited loss of amino acid residues was detected after acidic hydrolysis followed by UHPLC analysis, which showed only a minor effect of heat treatment on protein oxidation in these protein systems.",
author = "Chengkang Li and Nielsen, {S{\o}ren B.} and Kasper Engholm-Keller and Lund, {Marianne N.}",
year = "2022",
doi = "10.1021/acs.jafc.1c07946",
language = "English",
volume = "70",
pages = "4391--4406",
journal = "Journal of Agricultural and Food Chemistry",
issn = "0021-8561",
publisher = "American Chemical Society",
number = "14",

}

RIS

TY - JOUR

T1 - Oxidation of Whey Proteins during Thermal Treatment Characterized by a Site-Specific LC–MS/MS-Based Proteomic Approach

AU - Li, Chengkang

AU - Nielsen, Søren B.

AU - Engholm-Keller, Kasper

AU - Lund, Marianne N.

PY - 2022

Y1 - 2022

N2 - Thermal treatment is often employed in food processing to tailor product properties by manipulating the ingredient functionality, but these elevated temperatures may accelerate oxidation and nutrient loss. Here, oxidation of different whey protein systems [α-lactalbumin (α-LA), β-lactoglobulin (β-LG), a mix of α-LA and β-LG (whey model), and a commercial whey protein isolate (WPI)] was investigated during heat treatment at 60–90 °C and a UHT-like treatment by LC-MS-based proteomic analysis. The relative modification levels of each oxidation site were calculated and compared among different heat treatments and sample systems. Oxidation increased significantly in protein systems after heating at ≥90 °C but decreased in systems with higher complexity [pure protein (α-LA > β-LG) > whey model > WPI]. In α-LA, Cys, Met, and Trp residues were found to be most prone to oxidation. In β-LG-containing protein systems, Cys residues were suggested to scavenge most of the reactive oxidants and undergo an oxidation-mediated disulfide rearrangement. The rearranged disulfide bonds contributed to protein aggregation, which was suggested to provide physical protection against oxidation. Overall, limited loss of amino acid residues was detected after acidic hydrolysis followed by UHPLC analysis, which showed only a minor effect of heat treatment on protein oxidation in these protein systems.

AB - Thermal treatment is often employed in food processing to tailor product properties by manipulating the ingredient functionality, but these elevated temperatures may accelerate oxidation and nutrient loss. Here, oxidation of different whey protein systems [α-lactalbumin (α-LA), β-lactoglobulin (β-LG), a mix of α-LA and β-LG (whey model), and a commercial whey protein isolate (WPI)] was investigated during heat treatment at 60–90 °C and a UHT-like treatment by LC-MS-based proteomic analysis. The relative modification levels of each oxidation site were calculated and compared among different heat treatments and sample systems. Oxidation increased significantly in protein systems after heating at ≥90 °C but decreased in systems with higher complexity [pure protein (α-LA > β-LG) > whey model > WPI]. In α-LA, Cys, Met, and Trp residues were found to be most prone to oxidation. In β-LG-containing protein systems, Cys residues were suggested to scavenge most of the reactive oxidants and undergo an oxidation-mediated disulfide rearrangement. The rearranged disulfide bonds contributed to protein aggregation, which was suggested to provide physical protection against oxidation. Overall, limited loss of amino acid residues was detected after acidic hydrolysis followed by UHPLC analysis, which showed only a minor effect of heat treatment on protein oxidation in these protein systems.

U2 - 10.1021/acs.jafc.1c07946

DO - 10.1021/acs.jafc.1c07946

M3 - Journal article

C2 - 35380828

VL - 70

SP - 4391

EP - 4406

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

SN - 0021-8561

IS - 14

ER -

ID: 303256966