Light exposure accelerates oxidative protein polymerization in beef stored in high oxygen atmosphere

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

Standard

Light exposure accelerates oxidative protein polymerization in beef stored in high oxygen atmosphere. / Zainudin, Mohd Asraf Mohd; Poojary, Mahesha M.; Jongberg, Sisse; Lund, Marianne N.

In: Food Chemistry, Vol. 299, 125132, 2019.

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

Harvard

Zainudin, MAM, Poojary, MM, Jongberg, S & Lund, MN 2019, 'Light exposure accelerates oxidative protein polymerization in beef stored in high oxygen atmosphere', Food Chemistry, vol. 299, 125132. https://doi.org/10.1016/j.foodchem.2019.125132

APA

Zainudin, M. A. M., Poojary, M. M., Jongberg, S., & Lund, M. N. (2019). Light exposure accelerates oxidative protein polymerization in beef stored in high oxygen atmosphere. Food Chemistry, 299, [125132]. https://doi.org/10.1016/j.foodchem.2019.125132

Vancouver

Zainudin MAM, Poojary MM, Jongberg S, Lund MN. Light exposure accelerates oxidative protein polymerization in beef stored in high oxygen atmosphere. Food Chemistry. 2019;299. 125132. https://doi.org/10.1016/j.foodchem.2019.125132

Author

Zainudin, Mohd Asraf Mohd ; Poojary, Mahesha M. ; Jongberg, Sisse ; Lund, Marianne N. / Light exposure accelerates oxidative protein polymerization in beef stored in high oxygen atmosphere. In: Food Chemistry. 2019 ; Vol. 299.

Bibtex

@article{3f085f46f7a0484499d32425a39e4167,
title = "Light exposure accelerates oxidative protein polymerization in beef stored in high oxygen atmosphere",
abstract = "Protein oxidation of beef patties stored in high oxygen modified atmosphere packaging for 9 days was investigated. Meat was either stored in the dark, under light, or in the dark with addition of FeCl2/H2O2/myoglobin (forced oxidation). SDS-PAGE analysis showed high degree of protein polymerization for meat exposed to light, compared to the other samples. Light exposure induced reducible (disulfide) and non-reducible cross-links, while mainly disulfides were formed in meat stored in the dark. Light exposure was responsible for 58% loss of free thiols (Cys residues). No significant loss of other amino acid residues was observed and none of the most common oxidation products of tryptophan, tyrosine, and phenylalanine were detected. Intrinsic fluorescence measurements of tryptophan showed 27% loss in samples exposed to light, which was ascribed to loss of protein solubility via protein polymerization rather than tryptophan oxidation. Protein carbonyls were mainly detected in forced oxidized samples at Day 0.",
keywords = "Photo-oxidation, Meat, Protein thiols, Protein cross-linking, Protein oxidation, Tryptophan oxidation, Fluorescence",
author = "Zainudin, {Mohd Asraf Mohd} and Poojary, {Mahesha M.} and Sisse Jongberg and Lund, {Marianne N.}",
year = "2019",
doi = "10.1016/j.foodchem.2019.125132",
language = "English",
volume = "299",
journal = "Food Chemistry",
issn = "0308-8146",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - Light exposure accelerates oxidative protein polymerization in beef stored in high oxygen atmosphere

AU - Zainudin, Mohd Asraf Mohd

AU - Poojary, Mahesha M.

AU - Jongberg, Sisse

AU - Lund, Marianne N.

PY - 2019

Y1 - 2019

N2 - Protein oxidation of beef patties stored in high oxygen modified atmosphere packaging for 9 days was investigated. Meat was either stored in the dark, under light, or in the dark with addition of FeCl2/H2O2/myoglobin (forced oxidation). SDS-PAGE analysis showed high degree of protein polymerization for meat exposed to light, compared to the other samples. Light exposure induced reducible (disulfide) and non-reducible cross-links, while mainly disulfides were formed in meat stored in the dark. Light exposure was responsible for 58% loss of free thiols (Cys residues). No significant loss of other amino acid residues was observed and none of the most common oxidation products of tryptophan, tyrosine, and phenylalanine were detected. Intrinsic fluorescence measurements of tryptophan showed 27% loss in samples exposed to light, which was ascribed to loss of protein solubility via protein polymerization rather than tryptophan oxidation. Protein carbonyls were mainly detected in forced oxidized samples at Day 0.

AB - Protein oxidation of beef patties stored in high oxygen modified atmosphere packaging for 9 days was investigated. Meat was either stored in the dark, under light, or in the dark with addition of FeCl2/H2O2/myoglobin (forced oxidation). SDS-PAGE analysis showed high degree of protein polymerization for meat exposed to light, compared to the other samples. Light exposure induced reducible (disulfide) and non-reducible cross-links, while mainly disulfides were formed in meat stored in the dark. Light exposure was responsible for 58% loss of free thiols (Cys residues). No significant loss of other amino acid residues was observed and none of the most common oxidation products of tryptophan, tyrosine, and phenylalanine were detected. Intrinsic fluorescence measurements of tryptophan showed 27% loss in samples exposed to light, which was ascribed to loss of protein solubility via protein polymerization rather than tryptophan oxidation. Protein carbonyls were mainly detected in forced oxidized samples at Day 0.

KW - Photo-oxidation

KW - Meat

KW - Protein thiols

KW - Protein cross-linking

KW - Protein oxidation

KW - Tryptophan oxidation

KW - Fluorescence

U2 - 10.1016/j.foodchem.2019.125132

DO - 10.1016/j.foodchem.2019.125132

M3 - Journal article

C2 - 31299519

VL - 299

JO - Food Chemistry

JF - Food Chemistry

SN - 0308-8146

M1 - 125132

ER -

ID: 225557630