Combination of light and oxygen accelerates formation of covalent protein-polyphenol bonding during chill storage of meat added 4-methyl catechol

Research output: Contribution to journal › Journal article › Research › peer-review

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Combination of light and oxygen accelerates formation of covalent protein-polyphenol bonding during chill storage of meat added 4-methyl catechol. / Zainudin, Mohd Asraf Mohd; Jongberg, Sisse; Lund, Marianne N.

In: Food Chemistry, Vol. 334, 127611, 2021.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Zainudin, MAM, Jongberg, S & Lund, MN 2021, 'Combination of light and oxygen accelerates formation of covalent protein-polyphenol bonding during chill storage of meat added 4-methyl catechol', Food Chemistry, vol. 334, 127611. https://doi.org/10.1016/j.foodchem.2020.127611

APA

Zainudin, M. A. M., Jongberg, S., & Lund, M. N. (2021). Combination of light and oxygen accelerates formation of covalent protein-polyphenol bonding during chill storage of meat added 4-methyl catechol. Food Chemistry, 334, [127611]. https://doi.org/10.1016/j.foodchem.2020.127611

Vancouver

Zainudin MAM, Jongberg S, Lund MN. Combination of light and oxygen accelerates formation of covalent protein-polyphenol bonding during chill storage of meat added 4-methyl catechol. Food Chemistry. 2021;334. 127611. https://doi.org/10.1016/j.foodchem.2020.127611

Author

Zainudin, Mohd Asraf Mohd ; Jongberg, Sisse ; Lund, Marianne N. / Combination of light and oxygen accelerates formation of covalent protein-polyphenol bonding during chill storage of meat added 4-methyl catechol. In: Food Chemistry. 2021 ; Vol. 334.

Bibtex

@article{e0013b938ed94330b569d48c8670fb0c,
title = "Combination of light and oxygen accelerates formation of covalent protein-polyphenol bonding during chill storage of meat added 4-methyl catechol",
abstract = "Plant polyphenols applied as natural antioxidant ingredients, are known to bind to cysteine residues on meat proteins. The aim of this study was to examine the effect of light exposure on the formation of cysteine-phenol adduct in meat added 4-methylcatechol (4MC), a model polyphenol, during storage through quantitative LC-MS/MS-based analysis. Cysteine-4-methylcatechol adduct (Cys-4MC) formation in meat added 1500 ppm 4-MC increased significantly (by 50%) when stored under light in oxygen at 4 °C for 7 days as compared to storage in the dark. This was reflected by a significant decrease in thiol concentrations in the same sample. Gel electrophoresis showed loss in myosin heavy chain (MHC), and a resulting increase in cross-linked MHC (CL-MHC) and larger protein polymers in samples added 4MC. Protein blots stained with nitroblue tetrazolium (NBT) showed intensive protein-polyphenol binding in the meat samples added 4MC, but no major differences between storage conditions.",
keywords = "Cysteine-phenol adduct, Meat, Michael addition, Photo-oxidation, Protein cross-linking, Protein oxidation, Thiol-quinone adduct, Thiols",
author = "Zainudin, {Mohd Asraf Mohd} and Sisse Jongberg and Lund, {Marianne N.}",
year = "2021",
doi = "10.1016/j.foodchem.2020.127611",
language = "English",
volume = "334",
journal = "Food Chemistry",
issn = "0308-8146",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Combination of light and oxygen accelerates formation of covalent protein-polyphenol bonding during chill storage of meat added 4-methyl catechol

AU - Zainudin, Mohd Asraf Mohd

AU - Jongberg, Sisse

AU - Lund, Marianne N.

PY - 2021

Y1 - 2021

N2 - Plant polyphenols applied as natural antioxidant ingredients, are known to bind to cysteine residues on meat proteins. The aim of this study was to examine the effect of light exposure on the formation of cysteine-phenol adduct in meat added 4-methylcatechol (4MC), a model polyphenol, during storage through quantitative LC-MS/MS-based analysis. Cysteine-4-methylcatechol adduct (Cys-4MC) formation in meat added 1500 ppm 4-MC increased significantly (by 50%) when stored under light in oxygen at 4 °C for 7 days as compared to storage in the dark. This was reflected by a significant decrease in thiol concentrations in the same sample. Gel electrophoresis showed loss in myosin heavy chain (MHC), and a resulting increase in cross-linked MHC (CL-MHC) and larger protein polymers in samples added 4MC. Protein blots stained with nitroblue tetrazolium (NBT) showed intensive protein-polyphenol binding in the meat samples added 4MC, but no major differences between storage conditions.

AB - Plant polyphenols applied as natural antioxidant ingredients, are known to bind to cysteine residues on meat proteins. The aim of this study was to examine the effect of light exposure on the formation of cysteine-phenol adduct in meat added 4-methylcatechol (4MC), a model polyphenol, during storage through quantitative LC-MS/MS-based analysis. Cysteine-4-methylcatechol adduct (Cys-4MC) formation in meat added 1500 ppm 4-MC increased significantly (by 50%) when stored under light in oxygen at 4 °C for 7 days as compared to storage in the dark. This was reflected by a significant decrease in thiol concentrations in the same sample. Gel electrophoresis showed loss in myosin heavy chain (MHC), and a resulting increase in cross-linked MHC (CL-MHC) and larger protein polymers in samples added 4MC. Protein blots stained with nitroblue tetrazolium (NBT) showed intensive protein-polyphenol binding in the meat samples added 4MC, but no major differences between storage conditions.

KW - Cysteine-phenol adduct

KW - Meat

KW - Michael addition

KW - Photo-oxidation

KW - Protein cross-linking

KW - Protein oxidation

KW - Thiol-quinone adduct

KW - Thiols

U2 - 10.1016/j.foodchem.2020.127611

DO - 10.1016/j.foodchem.2020.127611

M3 - Journal article

C2 - 32712493

AN - SCOPUS:85088377500

VL - 334

JO - Food Chemistry

JF - Food Chemistry

SN - 0308-8146

M1 - 127611

ER -

ID: 247988397