Oxidation of Food Components
R Mozuraityte and V Kristinova, SINTEF Fisheries and Aquaculture, Trondheim, Norway
T Rustad, Norwegian University of Science and Technology, Trondheim, Norway
ã 2016 Elsevier Ltd. All rights reserved.
Introduction
Originally, oxidation meant a reaction with oxygen to form an
oxide, since oxygen was the first known oxidizing agent. How-
ever, later, the term oxidation has been expanded to include
oxygen-like substances that accomplish parallel chemical reac-
tions. Ultimately, the meaning has been generalized to include
all processes involving loss of electrons.
Oxidation is defined as the loss of electrons or an increase
in oxidation state by a molecule, atom, or ion. However, this
definition is not completely correct, and oxidation should be
referred to as an increase in oxidation state.
Many different components of food, lipids, proteins,
nucleic acids, and different vitamins, are prone to oxidation.
Since lipids and proteins are two of the major components in
food, the focus of this article will therefore be on the oxidation
of these components.
Lipid Oxidation
Lipid oxidation is a highly complex set of free radical reactions
between fatty acids and oxygen, which results in oxidative
degradation of lipids, also known as rancidity. Lipid oxidation
intermediate products (free radicals) and end products (reac-
tive aldehydes) may interact with other food constituents, such
as proteins, sugars, pigments, and vitamins, and negatively
modify their properties. The reaction mechanisms and the
rate of lipid oxidation depend on many factors, such as fatty
acid composition, the presence of prooxidants and antioxi-
dants, type of lipid (triacylglycerols, phospholipids, and
others), and storage conditions, for example, temperature,
light, oxygen availability, and water activity.
Mechanisms of Lipid Oxidation
Lipid oxidation is initiated by the reaction of unsaturated
fatty acid with oxygen (O2) forming a primary oxidation
product – lipid hydroperoxide (LOOH). Thermodynamically,
atmospheric oxygen cannot react directly with double bonds
on a fatty acid, because the spin states are different – the
oxygen is in a triplet state (3O2), whereas the double bond is
in a singlet state. Therefore, the reaction between an unsatu-
rated fatty acid and oxygen (oxidation substrates) can only
occur when one of the oxidation substrates is converted into
an activated form – either a fatty acid radical (L•) or activated
oxygen species – for instance, singlet oxygen (3O2), hydroxyl


radical (•OH), or superoxide radical anion (O• 2 ), the latter
two belonging to a category of reactive oxygen species (ROS).
Based on the reaction mechanism, lipid oxidation can be
classified as
186 Encyclopedia of Food and Health
• enzymatic oxidation,
• singlet oxygen (light-induced) oxidation,
• autoxidation.
Enzymatic Oxidation
Several enzymes can catalyze lipid oxidation:
Lipoxygenases are iron-containing enzymes present, for
example, in fish gill and skin tissues, beans, or grains. The
enzymes catalyze the insertion of O2 into an unsaturated fatty
acid producing lipid hydroperoxides (LOOH).
Myeloperoxidases can initiate lipid oxidation in the presence
of hydrogen peroxide and halides, such as bromides and
iodides, and can be critical during the processing of meat/
muscle tissues, when interaction between air (oxygen), blood,
and lipids (oxidation substrates) is increased.
Singlet Oxygen (Light-Induced) Oxidation
In the presence of photosensitizers (porphyrins and riboflavins)
and under exposure to light, the nonreactive triplet oxygen can
be converted into reactive singlet oxygen (1O2). In addition,
singlet oxygen can be formed chemically and enzymatically.
Singlet oxygen can directly attack the dC]Cd double bond
on a fatty acid and thereby initiate photooxidation. Singlet
oxygen-induced oxidation leads to the formation of both con-
jugated and nonconjugated hydroperoxides, which further
decompose by the same mechanisms as peroxides formed
from triplet oxygen in autoxidation (described in the succeeding
text). The rate of lipid oxidation mediated by singlet oxygen is
much higher than the rates in autoxidation, resulting in drasti-
cally increased rates of oxidation even at very low temperatures,
which lowers the quality of foods during processing and storage.
Autoxidation
The most important mechanism in lipid oxidation is
autoxidation, which occurs via free radical chain mechanism
in an autocatalytic manner. It involves the reaction of unsatu-
rated fatty acids with atmospheric oxygen and occurs in three
phases: initiation, propagation, and termination.
In the initiation step, lipid radicals may be formed by
thermal cleavage, by reactions with chemical oxidizers (acti-
vated oxygen species), or by interactions with transition metals
or enzymes. Once an initial lipid radical is formed, it reacts
with atmospheric triplet oxygen, generating peroxyl radicals.
These act as chemical oxidizers and react with a new unsatu-
rated fatty acid, thereby propagating the chain of autoxidation
(Figure 1), which leads to branching reactions. The chain
is terminated once the free radical is reacted into a stable
molecule.
http://dx.doi.org/10.1016/B978-0-12-384947-2.00508-0
 Oxidation of Food Components 187

Primary Oxidation Products of double bonds, the mixture of volatile secondary oxidation
products formed after the breakdown of hydroperoxides is very
The primary product of the autoxidation cascade is LOOH;
complex. Volatile decomposition products from long-chain
each peroxide group is accompanied by the formation of con-
n
3 PUFAs from marine organisms have extremely low flavor
jugated diene structure on the fatty acid. The chain also pro-
threshold values and have readily detectable odors at very low
duces intermediate and short-lived lipid radicals, such as L•
levels of oxidation. During homolytic b-cleavage of the perox-
and LOO•. As the number of double bonds in polyunsaturated
ides, aldehydes are left on the triacylglycerol or phospholipid
fatty acid (PUFA) increases, more complex mixtures of LOOH
molecule, and these aldehydes are called core aldehydes.
are produced. Lipid hydroperoxides are tasteless and odorless
(Figure 2).

Tertiary Oxidation Products

Secondary Oxidation Products
In the presence of metals and nonheme iron and at high
temperatures, lipid hydroperoxides break down to an array of
nonvolatile and volatile secondary oxidation products. As a
result of this breakdown, new radicals are formed (•OH,
LO•, and LOO•) that can reinitiate and branch the autoxida-
tion reactions. LO• can also be cleaved in a b-scission reaction
into various nonvolatile and volatile secondary oxidation
products. Peroxyl radicals (LOO•) of fatty acids or esters that
contain three or more methylene-interrupted double bonds
can be oxidized by cyclization into hydroperoxy epidioxides
and bicycloendoperoxides, which then may be broken down
into malondialdehyde.
Due to the variety of lipid hydroperoxides that can be
formed during autoxidation and the type of oxidative cleavage
In the final termination stage, relatively unreactive tertiary
oxidation products are formed, including hydrocarbons, alde-
hydes, and ketones. However, unsaturated aldehydes and
ketones may also undergo further oxidation forming volatile
oxidation products. Additionally, hydroperoxy radicals formed
during the propagation stage may react with triacylglycerols
forming dimeric and trimeric triacylglycerols linked via
peroxidic-type bonds.
Factors Influencing the Oxidation Rate and Mechanism
As the degree of unsaturation of fatty acid increases, the sus-
ceptibility to oxidation of fatty increases (Table 1).

Initiation
Fatty acid

OOH Lipid radical

O23
Lipid
hydroperoxide propagation

OO
Fatty acid
peroxy radical
Figure 1 Autoxidation of fatty acids. Reproduced from Frankel, E. N. (2005). Lipid oxidation. Bridgewater: Oily Press.

Oxygen consumption
Intensity or acumulation

Hydroperoxides (PV)
Nonvolatiles (AV)

Volatiles

Oxidation time

Figure 2 The kinetic curve of autoxidation of polyunsaturated fatty acids. PV, peroxide value; AV, anisidine value. Adapted from Kamal-Eldin, A. (2003).
Lipid oxidation pathways. Champaign, IL: AOCS Press.
188 Oxidation of Food Components
Table 1 Relative oxidation rates of unsaturated fatty acids subjected
to photooxidation and autoxidation
Degree of unsaturation
Oxidation mechanism C18:1 C18:2 C18:3
Autoxidation 1 27 77
Photooxidation 3  104 4  104 7  104
Oxygen
Oxidation of oils also increases with an increased amount of
dissolved oxygen. The concentration of dissolved oxygen in the
oil is dependent on the oxygen partial pressure in the
headspace of the oil. Therefore, in order to stabilize unsatu-
rated oils, oxygen should be omitted during processing and
storage of unsaturated oils. Due to this, tall and narrow tanks
are suggested for the storage of oils. Air-filled headspace in
storage tanks should be held at a minimum, and all pipelines
are recommended to be filled with inert gas.
Light
Photochemically induced oxidative changes are directly related
to the light source, wavelength, light intensity, exposure time,
and temperature. UV light was observed to be more harmful
than visible light. Packaging of oils into colored (dark) glass
containers or plastic vessels with UV absorbers efficiently
reduces light-induced oxidation.
Temperature
Autoxidation of oils and decomposition of LOOH increase as
the temperature increases. As a rule of thumb, autoxidation
rates double for each increase in temperature by 10  C. There-
fore, variations in storage temperature will lead to significant
reduction in shelf life.
Prooxidants and Antioxidants
Prooxidants
Prooxidants are compounds that initiate, facilitate, or acceler-
ate lipid oxidation. Prooxidants are considered ubiquitous and
are efficient in catalyzing lipid oxidation even at trace
concentrations.
Transition Metals
Transition metals, such as low-molecular (free) iron and
copper ions, are common catalysts of lipid oxidation. Iron is
normally found in greater concentrations than copper, but
copper is a stronger prooxidant than iron. Oxidizing metals
(M(nþ1)þ) decompose LOOH at rates several orders of magni-
tude slower than reducing metals (Mnþ). Iron catalyzes lipid
oxidation via the decomposition of LOOH into free radicals
through redox cycling pathways. In the absence of oxygen,
metal ions can still cause the breakdown of already formed
hydroperoxides, facilitating the formation of secondary oxida-
tion products (via b-scission), such as aldehydes.
Hemoproteins
Hemoproteins, that is, proteins containing a porphyrin struc-
ture with embedded iron atom, are known to catalyze lipid
oxidation at much higher rates than low molecular weight
iron. The most common heme compounds are derivatives of
hemoglobin, myoglobin, catalase, and peroxidase. Hemoglo-
bin and myoglobin are typically present in meat tissues and
tissues rich in blood, such as organs.
In living tissues, hemoglobin exists in the reduced form (Fe2þ),
either saturated with an oxygen molecule (oxyhemoglobin) or
devoid of oxygen (deoxyhemoglobin). After death (postmortem),
the concentration of oxy- and deoxyhemoglobin progressively
decreases as it is converted (oxidized) to brown-colored methe-
moglobin (metHb) that does not have the ability to bind oxygen.
It is believed that intact porphyrin–Fe structure inside a
pocket formed by surrounding proteins is an absolute require-
ment for heme-catalyzed lipid oxidation and that hypervalent
iron complexes – mainly ferryl iron complexes (Fe4þ ¼O and
Fe4þ(OH)) – are responsible for the rapid catalysis. The basic
reaction mechanism involves binding of preformed LOOH to
Fe3þ-heme, which generates the ferryl iron complex in a very
fast reaction (K  109 M
1 s
1). The LOOH is then decom-
posed either heterolytically or homolytically inside the heme
pocket, producing lipid alcohols (R–OH) or LO•, respectively.
The resulting ferryl iron complex is an extremely strong oxidant
and rapidly abstracts H from either a new LOOH or the fatty
acid directly, which generates lipid radicals for autoxidation
reactions. The hypervalent iron complexes can be maintained
by electron transfers, thus keeping their oxidizing power. Even-
tually, they are reduced back to Fe3þ-hemes.
The composition and arrangements of amino acids in the
heme pocket, as well as heme pocket size and orientation,
affect lipid binding and proton abstraction, while the protein
structure and ligands influence electron transfer processes and
stabilization of the ferryl iron complex. The reaction environ-
ment influences whether the LOOH cleavage is homolytic or
heterolytic. Therefore, variable catalytic activity between differ-
ent heme compounds and the same heme compounds from
different animals has been observed.
Antioxidants
Antioxidants are compounds that prevent or delay lipid perox-
idation. Antioxidants are usually classified into primary and
secondary.
Primary antioxidants act as free radical scavengers via their
ability to donate electron/hydrogen to peroxyl or alkoxy radicals,
preventing them from reacting with a new fatty acid, thereby
blocking the branching reactions in autoxidation. Tocopherols
(vitamin E), ascorbic acid (vitamin C), and carotenoids (vitamin
A) are common antioxidants in plants. Plant extracts are rich
sources of natural antioxidants that contain compounds with
multiple OH groups (phenolic acids, flavonoids, and anthocya-
nins), which act as hydrogen donors. Examples of these are
rosemary extract where the active compounds are carnosol,
carnosic acid, and rosmarinic acid or flavonoids found in green
tea (catechins), red wine, seeds, and spices.
Secondary antioxidants act by a number of different mecha-
nisms including metal chelation and scavenging of singlet
oxygen and ROS. Examples are ethylene-diamine-tetraacetic

acid and citric acid, which complex iron and copper ions and
thereby prevent metal-catalyzed lipid oxidation. Carotenoids
absorb energy from singlet oxygen, transferring it to triplet
oxygen, without changing their chemical structure (quench-
ing) and therefore protect oil against light-induced oxidation.
Antioxidants assist to maintain low oxidative status of oils
when added after an effective refining process, when most
oxidation products and prooxidants have been removed from
the oil. If the oxidation process in the oil is already started,
addition of an antioxidant may only to some extent slow down
oxidation or even have no effect.
Oxidation of Proteins
Oxidation of food proteins has received less attention than
oxidation of lipids and the studies of oxidation of proteins
have mainly been focused on the role of protein oxidation in
age-related diseases.
The discovery that myofibrillar proteins in beef were
oxidized led to many studies of protein oxidation in muscle
foods. Early studies on protein oxidation in food showed that
oxidation of food proteins could lead to significant losses in
the functionality of proteins. Oxidation may lead to changes in
both the primary and the secondary structures of proteins.
Protein oxidation may lead to loss of solubility, changes in
surface hydrophobicity, and changes in texture and affect water
binding and also how susceptible proteins are toward proteo-
lytic degradation. It has also been shown that some of the
changes occurring during frozen storage of fish can be
explained by protein oxidation.
The reactions between proteins and radicals in the presence
of oxygen lead to changes both in the amino acid side chains
and in the backbone of the proteins. The amino acids that are
most often affected are cysteine, tyrosine, lysine, arginine, and
histidine. The amino acids may be oxidized both as free amino
acids and as part of the protein backbone.
The oxidation of proteins is believed to occur via a free
radical chain reaction that is similar to the mechanism of
lipid oxidation. However, there is an even higher complexity
of pathways and therefore also a larger variation in reaction
products. Reaction between a protein and a ROS leads to the
formation of protein-centered radicals (called P•). In the pres-
ence of oxygen, this is converted to a peroxyl radical (POO•),
and by abstracting a hydrogen atom from another molecule, it
is converted to an alkyl peroxide (POOH). Further reactions
can lead to the formation of alkoxy radicals (PO•) and hydroxy
compounds. Protein radicals may react with other macromol-
ecules in food like DNA, starch, lipids, and other proteins.
The thiol group in cysteine is highly susceptible to
oxidation, and this may lead to the formation of sulfenic
acid, sulfinic acid, and disulfide bonds. Oxidation of tyrosine
may lead to the formation of dityrosine cross-linkages. The
formation of disulfide and dityrosine cross-linkages may lead
to both textural changes and reduced solubility. Oxidation of
lysine, arginine, and histidine may lead to the formation of
carbonyl groups. In addition to changes in the amino acid side
chains, protein oxidation may also lead to breakage of the
protein backbone.
Oxidation may change hydrophobicity, conformation,
solubility, and susceptibility toward digestive enzymes – the
latter may reduce nutritional value.
Oxidation of Food Components 189
Some proteins are more susceptible toward oxidation than
others and studies have shown that large proteins are more
prone to oxidation than proteins with lower molecular weight.
There are several methods to determine protein oxidation,
by detection of carbonyl groups, determination of changes in
sulfhydryl groups, and formation of dityrosine. In addition,
advanced methods like electron spin resonance, fluorescence
spectroscopy, and high pressure liquid chromatography
coupled with fluorescence detection as well as mass spectrom-
etry have been used to increase the understanding of the mech-
anisms of protein oxidation.
As already mentioned, protein oxidation affects food
properties, both texture and water-holding capacity. It has
also been found that protein oxidation affected the gel strength
of transglutaminase (TG)-mediated restructured meat. The
combination of oxidation and high-salt content increased the
TG-mediated cross-linking of myofibrillar proteins, probably
because TG had increased accessibility to glutamine and lysine
residues. A study on pork meat showed that mild oxidation of
myofibrillar proteins improved gelling properties probably
due to the formation of disulfide bonds; however, a negative
effect was found on the water-holding capacity of the gels.
Oxidizing agents are also used to improve baking properties
of wheat (gluten) due to the importance of disulfide inter-
change for dough strength. Other studies have, however,
shown negative effects of protein oxidation on the gel-forming
properties of proteins showing that more studies are needed.
Several enzyme systems, the main ones are the calpains and
the cathepsins, influence the tenderness of muscle foods. The
only endogenous meat enzyme system that has been evaluated
with regard to oxidation in meat is the calpain. The decrease in
tenderness due to protein oxidation has been ascribed to either
inactivation of m-calpain or cross-linking of myosin resulting in
strengthening of the myofibrillar structure.
Studies of lipid and protein oxidation in rainbow trout have
shown that protein and lipid oxidation followed the same
trend and that protein carbonyls developed together with
the formation of LOOH indicating that these two processes
occur simultaneously.
Protein oxidation has been studied during different food
processing operations. For salted herring, cross-linking of myo-
sin was found to be responsible for changes in texture, and an
increase in protein carbonyls with increased ripening period
was also found.
Storage of processed food such as pâtés and cooked sausages
was also found to result in increased hardness; this has been
ascribed to onset of protein oxidation, especially to the forma-
tion of cross-linkages between myofibrillar proteins. A relation-
ship between protein carbonyls and instrumental hardness of
sausages and packaging of beef in high-oxygen atmosphere has
been found to have a negative effect on meat tenderness.
In rainbow trout stored at different storage temperatures,
no protein oxidation was detected while storage at
20  C
resulted in the formation of protein carbonyls.
Controlling Protein Oxidation
The use of antioxidants – for instance, as part of the feed of the
animals – has been found to increase oxidative stability of the
food products. Reducing the PUFA/FA in animal tissues and
supplementing the feed with antioxidants have also been
190 Oxidation of Food Components
suggested as strategies to control protein oxidation. Different
results have been found with regard to the effect of modifica-
tion of the fatty acid composition in the muscle; some studies
show only minor effect while the results of other studies indi-
cate positive correlations between the ratio between PUFA and
tocopherol as antioxidant. Therefore, controlling the protein
oxidation by managing the feed composition seems to be a
promising possibility. In a study on chilled mackerel, catechin
was found to inhibit both lipid oxidation and protein
oxidation; however, the antioxidative effect varied for the dif-
ferent myofibrillar proteins. It is also important to bear in
mind that protein oxidation may lead to desired changes in
food and might enable the production of foods with new and
desirable textural properties.
Several recent studies on protein oxidation in food have led
to increased understanding of both the mechanisms and the
effect of protein oxidation on food quality. However, the exist-
ing methods for detection of protein oxidation are not suffi-
ciently sensitive. There is therefore a need to develop new and
sensitive methods to characterize the oxidation products gen-
erated during oxidation of proteins in food.
See also: Antioxidants: Characterization and Analysis; Fish Oils:
Production and Properties; Fish: Processing; Phospholipids:
Properties and Occurrence; Proteins: Chemistry, Characterization, and
Quality; Vegetable Oils: Oil Production and Processing.
Further Reading
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Raton, FL: CRC Press/Taylor & Francis Group.
Baron CP, Kjærsgård IVH, Jessen F, and Jacobsen C (2007) Protein and lipid oxidation
during frozen storage of rainbow trout (Oncorhynchus mykiss). Journal of
Agricultural and Food Chemistry 55: 8118–8125.
Carlsen CU, Møller JKS, and Skibsted LH (2005) Heme-iron in lipid oxidation.
Coordination Chemistry Reviews 249: 485–498.
Chaiyasit W, Elias RJ, McClements DJ, and Decker EA (2007) Role of physical
structures in bulk oils on lipid oxidation. Critical Reviews in Food Science and
Nutrition 47: 299–317.
Chen B, McClements DJ, and Decker EA (2011) Minor components in food oils: a
critical review of their roles on lipid oxidation chemistry in bulk oils and emulsions.
Critical Reviews in Food Science and Nutrition 51: 901–916.
Choe E and Min DB (2005) Chemistry and reactions of reactive oxygen species in
foods. Journal of Food Science 70: R142–R159.
Choe E and Min DB (2009) Mechanisms of antioxidants in the oxidation of foods.
Comprehensive Reviews in Food Science and Food Safety 8: 345–358.
Frankel EN (1985) Chemistry of autoxidation: mechanism, products and flavor
significance. In: Min DB and Smouse TH (eds.) Flavor chemistry of fats and oils,
pp. 1–34. Champaign, IL: American Oil Chemists’ Society.
Frankel EN (2005) Lipid oxidation. Bridgewater: Oily Press.
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polyunsaturated lipids: a comparative evaluation. Trends in Food Science &
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Kamal-Eldin A (2003) Lipid oxidation pathways. Champaign, IL: AOCS Press.
Kamal-Eldin A and Min DB (2008) Lipid oxidation pathways. Urbana, IL: AOCS Press,
vol. 2.
Liu Z, Xiong YL, and Chen J (2010) Protein oxidation enhances hydration but
suppresses water-holding capacity in porcine longissimus muscle. Journal of
Agricultural and Food Chemistry 58: 10697–10704.
Lund MN, Heinonen M, Baron CP, and Estévez M (2011) Protein oxidation in muscle
foods: a review. Molecular Nutrition & Food Research 55: 83–95.
Mozuraityte R, Rustad T, and Storro I (2008) The role of iron in peroxidation of
polyunsaturated fatty acids in liposomes. Journal of Agricultural and Food
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Perron N and Brumaghim J (2009) A review of the antioxidant mechanisms of
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food dispersions. Trends in Food Science & Technology 22: 3–13.