Iron(II) initiation of lipid and protein oxidation in pork: the role of oxymyoglobin

Feibai Zhou; Sisse Jongberg; Mouming Zhao; Weizheng Sun; Leif Horsfelt Skibsted

doi:10.1021/acs.jafc.6b01168

Iron(II) initiation of lipid and protein oxidation in pork: the role of oxymyoglobin

Feibai Zhou, Sisse Jongberg, Mouming Zhao, Weizheng Sun, Leif Horsfelt Skibsted

9 Citations (Scopus)

Abstract

Iron(II), added as FeSO₄·7H₂O, was found to increase the rate of oxygen depletion as detected electrochemically in a pork homogenate from Longissimus dorsi through an initial increase in metmyoglobin formation from oxymyoglobin and followed by formation of primary and secondary lipid oxidation products and protein oxidation as detected as thiol depletion in myofibrillar proteins. Without added iron(II), under the same conditions at 37 °C, oxygen consumption corresponded solely to the slow oxymyoglobin autoxidation. Long-lived myofibrillar protein radicals as detected by ESR spectroscopy in the presence of iron(II) were formed subsequently to oxymyoglobin oxidation, and their level was increased by lipid oxidation when oxygen was completely depleted. Similarly, the time profile for formation of lipid peroxide indicated that oxymyoglobin oxidation initiates both protein oxidation and lipid oxidation.

Original language	English
Journal	Journal of Agricultural and Food Chemistry
Volume	64
Issue number	22
Pages (from-to)	4618-4626
Number of pages	9
ISSN	0021-8561
DOIs	https://doi.org/10.1021/acs.jafc.6b01168
Publication status	Published - 8 Jun 2016

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title = "Iron(II) initiation of lipid and protein oxidation in pork: the role of oxymyoglobin",

abstract = "Iron(II), added as FeSO4·7H2O, was found to increase the rate of oxygen depletion as detected electrochemically in a pork homogenate from Longissimus dorsi through an initial increase in metmyoglobin formation from oxymyoglobin and followed by formation of primary and secondary lipid oxidation products and protein oxidation as detected as thiol depletion in myofibrillar proteins. Without added iron(II), under the same conditions at 37 °C, oxygen consumption corresponded solely to the slow oxymyoglobin autoxidation. Long-lived myofibrillar protein radicals as detected by ESR spectroscopy in the presence of iron(II) were formed subsequently to oxymyoglobin oxidation, and their level was increased by lipid oxidation when oxygen was completely depleted. Similarly, the time profile for formation of lipid peroxide indicated that oxymyoglobin oxidation initiates both protein oxidation and lipid oxidation.",

author = "Feibai Zhou and Sisse Jongberg and Mouming Zhao and Weizheng Sun and Skibsted, {Leif Horsfelt}",

year = "2016",

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doi = "10.1021/acs.jafc.6b01168",

language = "English",

volume = "64",

pages = "4618--4626",

journal = "Journal of Agricultural and Food Chemistry",

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TY - JOUR

T1 - Iron(II) initiation of lipid and protein oxidation in pork

T2 - the role of oxymyoglobin

AU - Zhou, Feibai

AU - Jongberg, Sisse

AU - Zhao, Mouming

AU - Sun, Weizheng

AU - Skibsted, Leif Horsfelt

PY - 2016/6/8

Y1 - 2016/6/8

N2 - Iron(II), added as FeSO4·7H2O, was found to increase the rate of oxygen depletion as detected electrochemically in a pork homogenate from Longissimus dorsi through an initial increase in metmyoglobin formation from oxymyoglobin and followed by formation of primary and secondary lipid oxidation products and protein oxidation as detected as thiol depletion in myofibrillar proteins. Without added iron(II), under the same conditions at 37 °C, oxygen consumption corresponded solely to the slow oxymyoglobin autoxidation. Long-lived myofibrillar protein radicals as detected by ESR spectroscopy in the presence of iron(II) were formed subsequently to oxymyoglobin oxidation, and their level was increased by lipid oxidation when oxygen was completely depleted. Similarly, the time profile for formation of lipid peroxide indicated that oxymyoglobin oxidation initiates both protein oxidation and lipid oxidation.

AB - Iron(II), added as FeSO4·7H2O, was found to increase the rate of oxygen depletion as detected electrochemically in a pork homogenate from Longissimus dorsi through an initial increase in metmyoglobin formation from oxymyoglobin and followed by formation of primary and secondary lipid oxidation products and protein oxidation as detected as thiol depletion in myofibrillar proteins. Without added iron(II), under the same conditions at 37 °C, oxygen consumption corresponded solely to the slow oxymyoglobin autoxidation. Long-lived myofibrillar protein radicals as detected by ESR spectroscopy in the presence of iron(II) were formed subsequently to oxymyoglobin oxidation, and their level was increased by lipid oxidation when oxygen was completely depleted. Similarly, the time profile for formation of lipid peroxide indicated that oxymyoglobin oxidation initiates both protein oxidation and lipid oxidation.

U2 - 10.1021/acs.jafc.6b01168

DO - 10.1021/acs.jafc.6b01168

M3 - Journal article

C2 - 27217062

SN - 0021-8561

VL - 64

SP - 4618

EP - 4626

JO - Journal of Agricultural and Food Chemistry

JF - Journal of Agricultural and Food Chemistry

IS - 22

ER -

Iron(II) initiation of lipid and protein oxidation in pork: the role of oxymyoglobin

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