4-Methylcatechol inhibits protein oxidation in meat but not disulfide formation

Sisse Jongberg; Marianne Lund Lametsch; Andrew L. Waterhouse; Leif Horsfelt Skibsted

doi:10.1021/jf202268q

4-Methylcatechol inhibits protein oxidation in meat but not disulfide formation

Sisse Jongberg, Marianne Lund Lametsch, Andrew L. Waterhouse, Leif Horsfelt Skibsted

50 Citations (Scopus)

Abstract

The interaction between phenolic compounds and protein thiols was investigated in minced beef with or without 500 ppm 4-methylcatechol (4-MC) that had been stored under oxygen or argon for 7 days (4 °C). Myofibrillar protein isolates were extracted, and the oxidative stability evaluated by the protein radical intensity measured by ESR spectroscopy was found to be improved by 4-MC as well as by storage without oxygen. Significant loss of thiols was found in samples stored under oxygen compared to argon, whereas an additional loss was found in samples with added 4-MC stored under oxygen. In beef with added 4-MC, LC-MS analysis showed formation of thiol-quinone adducts, which may explain the observed additional loss of thiols. Although storage without oxygen inhibited protein cross-link formation as evaluated by SDS-PAGE, both in presence and in the absence of 4-MC, no inhibitory effect of 4-MC was found on the formation of protein disulfide cross-links in beef stored under oxygen.

Original language	English
Journal	Journal of Agricultural and Food Chemistry
Volume	59
Issue number	18
Pages (from-to)	10329-10335
Number of pages	7
ISSN	0021-8561
DOIs	https://doi.org/10.1021/jf202268q
Publication status	Published - 28 Sept 2011

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title = "4-Methylcatechol inhibits protein oxidation in meat but not disulfide formation",

abstract = "The interaction between phenolic compounds and protein thiols was investigated in minced beef with or without 500 ppm 4-methylcatechol (4-MC) that had been stored under oxygen or argon for 7 days (4 °C). Myofibrillar protein isolates were extracted, and the oxidative stability evaluated by the protein radical intensity measured by ESR spectroscopy was found to be improved by 4-MC as well as by storage without oxygen. Significant loss of thiols was found in samples stored under oxygen compared to argon, whereas an additional loss was found in samples with added 4-MC stored under oxygen. In beef with added 4-MC, LC-MS analysis showed formation of thiol-quinone adducts, which may explain the observed additional loss of thiols. Although storage without oxygen inhibited protein cross-link formation as evaluated by SDS-PAGE, both in presence and in the absence of 4-MC, no inhibitory effect of 4-MC was found on the formation of protein disulfide cross-links in beef stored under oxygen.",

author = "Sisse Jongberg and Lametsch, {Marianne Lund} and Waterhouse, {Andrew L.} and Skibsted, {Leif Horsfelt}",

year = "2011",

month = sep,

day = "28",

doi = "10.1021/jf202268q",

language = "English",

volume = "59",

pages = "10329--10335",

journal = "Journal of Agricultural and Food Chemistry",

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TY - JOUR

T1 - 4-Methylcatechol inhibits protein oxidation in meat but not disulfide formation

AU - Jongberg, Sisse

AU - Lametsch, Marianne Lund

AU - Waterhouse, Andrew L.

AU - Skibsted, Leif Horsfelt

PY - 2011/9/28

Y1 - 2011/9/28

N2 - The interaction between phenolic compounds and protein thiols was investigated in minced beef with or without 500 ppm 4-methylcatechol (4-MC) that had been stored under oxygen or argon for 7 days (4 °C). Myofibrillar protein isolates were extracted, and the oxidative stability evaluated by the protein radical intensity measured by ESR spectroscopy was found to be improved by 4-MC as well as by storage without oxygen. Significant loss of thiols was found in samples stored under oxygen compared to argon, whereas an additional loss was found in samples with added 4-MC stored under oxygen. In beef with added 4-MC, LC-MS analysis showed formation of thiol-quinone adducts, which may explain the observed additional loss of thiols. Although storage without oxygen inhibited protein cross-link formation as evaluated by SDS-PAGE, both in presence and in the absence of 4-MC, no inhibitory effect of 4-MC was found on the formation of protein disulfide cross-links in beef stored under oxygen.

AB - The interaction between phenolic compounds and protein thiols was investigated in minced beef with or without 500 ppm 4-methylcatechol (4-MC) that had been stored under oxygen or argon for 7 days (4 °C). Myofibrillar protein isolates were extracted, and the oxidative stability evaluated by the protein radical intensity measured by ESR spectroscopy was found to be improved by 4-MC as well as by storage without oxygen. Significant loss of thiols was found in samples stored under oxygen compared to argon, whereas an additional loss was found in samples with added 4-MC stored under oxygen. In beef with added 4-MC, LC-MS analysis showed formation of thiol-quinone adducts, which may explain the observed additional loss of thiols. Although storage without oxygen inhibited protein cross-link formation as evaluated by SDS-PAGE, both in presence and in the absence of 4-MC, no inhibitory effect of 4-MC was found on the formation of protein disulfide cross-links in beef stored under oxygen.

U2 - 10.1021/jf202268q

DO - 10.1021/jf202268q

M3 - Journal article

SN - 0021-8561

VL - 59

SP - 10329

EP - 10335

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

IS - 18

ER -

4-Methylcatechol inhibits protein oxidation in meat but not disulfide formation

Abstract

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