Covalent bonding between polyphenols and proteins: Synthesis of caffeic acid-cysteine and chlorogenic acid-cysteine adducts and their quantification in dairy beverages

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Standard

Covalent bonding between polyphenols and proteins : Synthesis of caffeic acid-cysteine and chlorogenic acid-cysteine adducts and their quantification in dairy beverages. / Poojary, Mahesha M.; Hellwig, Michael; Henle, Thomas; Lund, Marianne N.

I: Food Chemistry, Bind 403, 134406, 2023.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › fagfællebedømt

Harvard

Poojary, MM, Hellwig, M, Henle, T & Lund, MN 2023, 'Covalent bonding between polyphenols and proteins: Synthesis of caffeic acid-cysteine and chlorogenic acid-cysteine adducts and their quantification in dairy beverages', Food Chemistry, bind 403, 134406. https://doi.org/10.1016/j.foodchem.2022.134406

APA

Poojary, M. M., Hellwig, M., Henle, T., & Lund, M. N. (2023). Covalent bonding between polyphenols and proteins: Synthesis of caffeic acid-cysteine and chlorogenic acid-cysteine adducts and their quantification in dairy beverages. Food Chemistry, 403, [134406]. https://doi.org/10.1016/j.foodchem.2022.134406

Vancouver

Poojary MM, Hellwig M, Henle T, Lund MN. Covalent bonding between polyphenols and proteins: Synthesis of caffeic acid-cysteine and chlorogenic acid-cysteine adducts and their quantification in dairy beverages. Food Chemistry. 2023;403. 134406. https://doi.org/10.1016/j.foodchem.2022.134406

Author

Poojary, Mahesha M. ; Hellwig, Michael ; Henle, Thomas ; Lund, Marianne N. / Covalent bonding between polyphenols and proteins : Synthesis of caffeic acid-cysteine and chlorogenic acid-cysteine adducts and their quantification in dairy beverages. I: Food Chemistry. 2023 ; Bind 403.

Bibtex

@article{a176166057c2464aa785138ff6486c83,
title = "Covalent bonding between polyphenols and proteins: Synthesis of caffeic acid-cysteine and chlorogenic acid-cysteine adducts and their quantification in dairy beverages",
abstract = "Protein-polyphenol interactions affect the structure, stability, and functional properties of proteins and polyphenols. Oxidized polyphenols (o-quinones) react rapidly with the sulfhydryl group of cysteine (Cys) residues, inducing covalent bonding between proteins and polyphenols. However, quantitative data on such reactions remain elusive, despite the importance of depicting the significance of such interactions on food structure and function. This work reports the synthesis, purification, and characterization of caffeic acid-cysteine (CA-Cys) and chlorogenic acid-cysteine (CGA-Cys) adducts and their stable isotope analogs, CA-[13C3,15N]Cys and CGA-[13C3,15N]Cys. A sensitive LC-MS/MS isotope dilution method was developed to simultaneously quantify these adducts in foods and beverages. Protein-bound CA-Cys and CGA-Cys were detected in the micro-molar range in milk samples with added CA and CGA, confirming covalent bonding between milk proteins and CA/CGA. These adducts were detected in commercial coffee-containing beverages but not in cocoa-containing drinks. Furthermore, the adducts were found to be partially stable during enzymatic protein hydrolysis.",
author = "Poojary, {Mahesha M.} and Michael Hellwig and Thomas Henle and Lund, {Marianne N.}",
year = "2023",
doi = "10.1016/j.foodchem.2022.134406",
language = "English",
volume = "403",
journal = "Food Chemistry",
issn = "0308-8146",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Covalent bonding between polyphenols and proteins

T2 - Synthesis of caffeic acid-cysteine and chlorogenic acid-cysteine adducts and their quantification in dairy beverages

AU - Poojary, Mahesha M.

AU - Hellwig, Michael

AU - Henle, Thomas

AU - Lund, Marianne N.

PY - 2023

Y1 - 2023

N2 - Protein-polyphenol interactions affect the structure, stability, and functional properties of proteins and polyphenols. Oxidized polyphenols (o-quinones) react rapidly with the sulfhydryl group of cysteine (Cys) residues, inducing covalent bonding between proteins and polyphenols. However, quantitative data on such reactions remain elusive, despite the importance of depicting the significance of such interactions on food structure and function. This work reports the synthesis, purification, and characterization of caffeic acid-cysteine (CA-Cys) and chlorogenic acid-cysteine (CGA-Cys) adducts and their stable isotope analogs, CA-[13C3,15N]Cys and CGA-[13C3,15N]Cys. A sensitive LC-MS/MS isotope dilution method was developed to simultaneously quantify these adducts in foods and beverages. Protein-bound CA-Cys and CGA-Cys were detected in the micro-molar range in milk samples with added CA and CGA, confirming covalent bonding between milk proteins and CA/CGA. These adducts were detected in commercial coffee-containing beverages but not in cocoa-containing drinks. Furthermore, the adducts were found to be partially stable during enzymatic protein hydrolysis.

AB - Protein-polyphenol interactions affect the structure, stability, and functional properties of proteins and polyphenols. Oxidized polyphenols (o-quinones) react rapidly with the sulfhydryl group of cysteine (Cys) residues, inducing covalent bonding between proteins and polyphenols. However, quantitative data on such reactions remain elusive, despite the importance of depicting the significance of such interactions on food structure and function. This work reports the synthesis, purification, and characterization of caffeic acid-cysteine (CA-Cys) and chlorogenic acid-cysteine (CGA-Cys) adducts and their stable isotope analogs, CA-[13C3,15N]Cys and CGA-[13C3,15N]Cys. A sensitive LC-MS/MS isotope dilution method was developed to simultaneously quantify these adducts in foods and beverages. Protein-bound CA-Cys and CGA-Cys were detected in the micro-molar range in milk samples with added CA and CGA, confirming covalent bonding between milk proteins and CA/CGA. These adducts were detected in commercial coffee-containing beverages but not in cocoa-containing drinks. Furthermore, the adducts were found to be partially stable during enzymatic protein hydrolysis.

U2 - 10.1016/j.foodchem.2022.134406

DO - 10.1016/j.foodchem.2022.134406

M3 - Journal article

C2 - 36191424

VL - 403

JO - Food Chemistry

JF - Food Chemistry

SN - 0308-8146

M1 - 134406

ER -

ID: 325711752