Covalent bonding of 4-methylcatechol to β-lactoglobulin results in the release of cysteine-4-methylcatechol adducts after in vitro digestion

Khadija Waqar; Kasper Engholm-Keller; Marcel S. Joehnke; Dereck E.W. Chatterton; Mahesha M. Poojary; Marianne N. Lund

doi:10.1016/j.foodchem.2022.133775

Covalent bonding of 4-methylcatechol to β-lactoglobulin results in the release of cysteine-4-methylcatechol adducts after in vitro digestion

Khadija Waqar, Kasper Engholm-Keller, Marcel S. Joehnke, Dereck E.W. Chatterton, Mahesha M. Poojary, Marianne N. Lund^*

^*Corresponding author af dette arbejde

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

10 Citationer (Scopus)

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Abstract

Protein-polyphenol adducts are formed upon covalent bonding between oxidized polyphenols and proteins. 4-Methylcatechol (4MC) is a polyphenol with origin in coffee and is oxidized to 4-methylbenzoquinone (4MBQ) under conditions used during food processing. The present study characterizes 4MBQ-induced covalent modifications on β-lactoglobulin (β-LG) from bovine milk, (henceforth β-LQ) and the effect on protein digestibility. Significant thiol and amine loss was found in β-LQ compared to β-LG. Site-specific 4MBQ-induced modifications were identified on Cys, Lys, Arg, His and Trp in β-LQ. No significant differences between β-LG and β-LQ on in vitro digestibility were observed by assessment with SDS-PAGE, degree of hydrolysis and LC-MS/MS unmodified peptide intensities. Cys-4MC adduct (1.7 ± 0.1 µmol/g) was released from β-LQ after in vitro digestion. Thus, it is relevant to investigate how released Cys-4MC adducts are absorbed in vivo in future studies.

Originalsprog	Engelsk
Artikelnummer	133775
Tidsskrift	Food Chemistry
Vol/bind	397
Antal sider	9
ISSN	0308-8146
DOI	https://doi.org/10.1016/j.foodchem.2022.133775
Status	Udgivet - 2022

Bibliografisk note

Funding Information:
Marianne Nissen Lund reports financial support was provided by Independent Research Fund Denmark. Khadija Waqar reports financial support was provided by Punjab Educational Endowment Fund.

Funding Information:
Punjab Educational Endowment Fund (PEEF) is acknowledged for financial support of PhD scholarship to KW, and Independent Research Fund Denmark for funding of grant no. 7017-00133B to MNL.

Publisher Copyright:
© 2022 The Authors

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10.1016/j.foodchem.2022.133775Licens: CC BY

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Citationsformater

Covalent bonding of 4-methylcatechol to β-lactoglobulin results in the release of cysteine-4-methylcatechol adducts after in vitro digestion. / Waqar, Khadija; Engholm-Keller, Kasper; Joehnke, Marcel S.; Chatterton, Dereck E.W.; Poojary, Mahesha M.; Lund, Marianne N.

I: Food Chemistry, Bind 397, 133775, 2022.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

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title = "Covalent bonding of 4-methylcatechol to β-lactoglobulin results in the release of cysteine-4-methylcatechol adducts after in vitro digestion",

abstract = "Protein-polyphenol adducts are formed upon covalent bonding between oxidized polyphenols and proteins. 4-Methylcatechol (4MC) is a polyphenol with origin in coffee and is oxidized to 4-methylbenzoquinone (4MBQ) under conditions used during food processing. The present study characterizes 4MBQ-induced covalent modifications on β-lactoglobulin (β-LG) from bovine milk, (henceforth β-LQ) and the effect on protein digestibility. Significant thiol and amine loss was found in β-LQ compared to β-LG. Site-specific 4MBQ-induced modifications were identified on Cys, Lys, Arg, His and Trp in β-LQ. No significant differences between β-LG and β-LQ on in vitro digestibility were observed by assessment with SDS-PAGE, degree of hydrolysis and LC-MS/MS unmodified peptide intensities. Cys-4MC adduct (1.7 ± 0.1 µmol/g) was released from β-LQ after in vitro digestion. Thus, it is relevant to investigate how released Cys-4MC adducts are absorbed in vivo in future studies.",

keywords = "4-methylbenzoquinone, Amino acid-polyphenol adducts, Michael addition reaction, Polyphenols, Protein-polyphenol bonding, Whey protein",

author = "Khadija Waqar and Kasper Engholm-Keller and Joehnke, {Marcel S.} and Chatterton, {Dereck E.W.} and Poojary, {Mahesha M.} and Lund, {Marianne N.}",

note = "Publisher Copyright: {\textcopyright} 2022 The Authors",

year = "2022",

doi = "10.1016/j.foodchem.2022.133775",

language = "English",

volume = "397",

journal = "Food Chemistry",

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AU - Waqar, Khadija

AU - Engholm-Keller, Kasper

AU - Joehnke, Marcel S.

AU - Chatterton, Dereck E.W.

AU - Poojary, Mahesha M.

AU - Lund, Marianne N.

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N2 - Protein-polyphenol adducts are formed upon covalent bonding between oxidized polyphenols and proteins. 4-Methylcatechol (4MC) is a polyphenol with origin in coffee and is oxidized to 4-methylbenzoquinone (4MBQ) under conditions used during food processing. The present study characterizes 4MBQ-induced covalent modifications on β-lactoglobulin (β-LG) from bovine milk, (henceforth β-LQ) and the effect on protein digestibility. Significant thiol and amine loss was found in β-LQ compared to β-LG. Site-specific 4MBQ-induced modifications were identified on Cys, Lys, Arg, His and Trp in β-LQ. No significant differences between β-LG and β-LQ on in vitro digestibility were observed by assessment with SDS-PAGE, degree of hydrolysis and LC-MS/MS unmodified peptide intensities. Cys-4MC adduct (1.7 ± 0.1 µmol/g) was released from β-LQ after in vitro digestion. Thus, it is relevant to investigate how released Cys-4MC adducts are absorbed in vivo in future studies.

AB - Protein-polyphenol adducts are formed upon covalent bonding between oxidized polyphenols and proteins. 4-Methylcatechol (4MC) is a polyphenol with origin in coffee and is oxidized to 4-methylbenzoquinone (4MBQ) under conditions used during food processing. The present study characterizes 4MBQ-induced covalent modifications on β-lactoglobulin (β-LG) from bovine milk, (henceforth β-LQ) and the effect on protein digestibility. Significant thiol and amine loss was found in β-LQ compared to β-LG. Site-specific 4MBQ-induced modifications were identified on Cys, Lys, Arg, His and Trp in β-LQ. No significant differences between β-LG and β-LQ on in vitro digestibility were observed by assessment with SDS-PAGE, degree of hydrolysis and LC-MS/MS unmodified peptide intensities. Cys-4MC adduct (1.7 ± 0.1 µmol/g) was released from β-LQ after in vitro digestion. Thus, it is relevant to investigate how released Cys-4MC adducts are absorbed in vivo in future studies.

KW - 4-methylbenzoquinone

KW - Amino acid-polyphenol adducts

KW - Michael addition reaction

KW - Polyphenols

KW - Protein-polyphenol bonding

KW - Whey protein

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