Review

Lipoxygenase in fruits and vegetables: A review

Taner Baysal a , Aslhan Demirdoven b,
a

Ege University, Engineering Faculty, Food Engineering Department, Izmir 35100, Turkey
b Ege University, Institute of Natural and Applied Sciences, Izmir 35100, Turkey

Abstract
Lipoxygenase (LOX) is one of the most widely studied enzyme in plants and animal kingdom which is found in more than 60 species. Lipoxygenase
catalyses the bioxygenation of polyunsaturated fatty acids (PUFA) containing a cis,cis-1,4-pentadiene unit to form conjugated hydroperoxydienoic
acids. Lipoxygenases have food-related applications in bread making and aroma production; they also have negative implications for the color,
off-avour and antioxidant status of plant-based foods. The signicance of plant lipoxygenase for fruit and vegetables are reviewed with particular
reference to the enzymes from plants. Various aspects of the sources of lipoxygenases, their oxidation mechanism, isozymes and inhibition of
oxidation are discussed.
2006 Elsevier Inc. All rights reserved.
Keywords: Lipoxygenase; Oxidation mechanism; Isozymes; Inhibition

Contents
1.
2.
3.

4.
5.

Introduction . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
Lipoxygenase contents of plants . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
Mechanism of lipoxygenase-catalysed oxidation . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
3.1. Lipoxygenase isozymes . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
3.2. Iron content . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
Inhibition of lipoxygenase oxidation . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
Conclusion . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .
References . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .

1. Introduction
Lipoxygenase (LOX) is an enzyme that is found in many
plants and animals, which catalyses the oxygenation of polyunsaturated fatty acids (PUFA) to form fatty acid hydroperoxides.
They are present in a wide range of biological organs and
tissues, but they are particularly abundant in grain legume
seeds (beans and peas) and potato tubers [1]. Lipoxygenase
from different sources, catalyses oxygenation at different points
along the carbon chain, referred to as positional or regio
specicity, such specicity has signicant implications for the

Corresponding author.
E-mail addresses: taner.baysal@ege.edu.tr (T. Baysal),
ademirdoven@hotmail.com (A. Demirdoven).

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metabolism of the resultant hydroperoxides into a number of

important secondary metabolites [2,3].
Linoleic and linolenic acid are the major polyunsaturated
fatty acids in plant tissues, and insertion of the oxygen takes
place at either the 9 or 12 position to generate the corresponding
9- or 13-hydroperoxides. While most LOXs so far characterized
are soluble cytosolic enzymes, some are chloroplastic, mitochondrial, or located in the vacuoles. In soybean, lipoxygenases
have been identied with involvement in nitrogen and assimilate
partitioning and appear to be regulated in response to plant nitrogen status in both tissue-specic and developmentally controlled
patterns [14]. A key role for some LOX isoforms is in the generation of fatty acid hydroperoxides destined for jasmonic acid
(JA), which triggers gene activation during wound response in
plants. The fatty acid hydroperoxides generated by the activity of LOX are potentially deleterious to membrane function by

causing increased rigidity and would not, therefore, be expected

to accumulate [4].
Lipoxygenase not only has food-related applications in bread
making [5] and aroma production [6]; but also has negative
implications for color, off-avour and antioxidant status of plantbased foods [2]. In many applications it is possible to use crude
plant materials or extracts [6], but such materials usually contain multiple enzymes that may reduce polyunsaturated fatty
acid substrate availability or metabolize the hydroperoxide products, thereby modulating lipoxygenase action, which has led to
understand the activities and properties of plant and other lipoxygenases as food processing additives and to remove selectively
specic lipoxygenase from plants based on such understanding
[2].
The signicance of plant lipoxygenase is reviewed, with particular reference to the enzymes from some fruits and vegetables.
Various aspects of the sources of lipoxygenases, their oxidation
mechanism, isozymes and inhibition of oxidation are discussed.
2. Lipoxygenase contents of plants
There is ample evidence that lipoxygenase is crucial elements of plants defence strategies. Removal of a specic tobacco
leaf lipoxygenase, by genetic engineering, converts a strain
of tobacco that is resistant to Phytophthora parasitica var.
nicotiana to one that is susceptible [7]. Although the mechanism of resistance is unknown, this unambiguously shows that
lipoxygenase is an essential part of the resistance. Many plants
respond to insect damage or wounding by the production of jasmonate (Fig. 1), and the activation of proteinase inhibitor genes
in both wounded and non-wounded leaves [8,9]. Removal of
wound-induced lipoxygenase activity from potato leaves eliminates the production of jasmonate and/or proteinase inhibitor
in response to wounding, which lead to increased susceptibility
to insect attack [9]. Leaves of French beans that are resistant to

Pseudomonas syringae pv phaseolicola show, on infection, an

elevated production of six-carbon aldehydes that are believed to
derive from lipoxygenase-produced hydroperoxides; the aldehydes are produced in bacteriocidal amounts and thus act as a
defence mechanism against Pseudomonas attack [10].
Lipoxygenase in vegetative tissues therefore provide
hydroperoxide substrates that can be metabolized to compounds
that play important roles in plant defence. Although, it is less
clear why seeds and tubers have large amounts of lipoxygenase and in such cases they are possibly dispensable; genetic
removal of specic soybean [11] or pea [12] seed isoforms, for
instance, appears not to compromise plant health. As part of a
drive to understand more fully the roles of various lipoxygenases
in plant biology, many of them have been cloned and produced
as recombinant enzymes [2].
3. Mechanism of lipoxygenase-catalysed oxidation
Various aspects of the sources of the enzymes, their activities,
substrate and product specicities, and co-oxidation potential
are discussed in the context of food quality and shelf life. The
sequences of lipoxygenases, predicted from DNA sequences,
from different plants, are compared and the signicance of
sequence differences assessed in relation to enzyme specicity
and the three-dimensional structure of soybean lipoxygenase1. A novel scheme is proposed for the mechanism of the
lipoxygenase-catalysed dioxygenation of polyunsaturated fatty
acids in which two different pathways are suggested for the
anaerobic and aerobic oxidations (Fig. 2) [13,14].
3.1. Lipoxygenase isozymes
The enzyme lipoxygenase (linoleate oxygen oxidoreductase,
EC 1.13.11.12) is present in a wide variety of plant and animal
tissues [15]. The enzyme in oil-bearing seeds, e.g. soybeans,

Fig. 1. Parts of the pathway of plant oxylipin metabolism leading from linolenic acid to jasmonate and volatile aldehydes [2].

Fig. 2. Pathway of lipoxygenase-catalysed oxidation [14].

can be an important source of hydroperoxides formed in the oil

during extraction. In vegetables, oxidative changes due to the
enzyme may lead to off-avours during storage. The enzyme
does, however, contribute to avor formation in some plant foods
including tomato and cucumber. Lipoxygenase activity requires
the presence of free polyunsaturated fatty acids. Linoleic acid is
the most common substrate in plant-based foods. The enzyme
occurs in a variety of isozymes, which often vary in optimum pH,
as well as product and substrate specicity. Lipoxygenase catalyses the bioxygenation of polyunsaturated fatty acids containing
a cis,cis-1,4-pentadiene unit to form conjugated hydroperoxydienoic acids [16].
Lipoxygenase from soybean seed is the best characterized
among plant LOX, although the physiological roles of these
enzymes are not completely known [17]. Soybean seed lipoxygenase catalyses the hydroperoxidation of polyunsaturated fatty
acids, such as linoleic and linolenic acids, leading to the production of several reactive molecules that account for the grassy
beany taste in soybean processed foods. In soybean leaves, LOX
has been intensively examined [18] but the diversity and characteristics of the different forms of LOX are not yet known. Given
the occurrence of multiple LOX isoenzymes in soybean leaves
and the proposed roles of these enzymes in the plant metabolism,
it is possible that individual isoenzymes play specic functions
[19]. Soybean lipoxygenase is the most extensively studied for
which molecular structure has been reported by Boyington et al.
[20]. Four isozymes have been isolated from soybeans:
(1) Soy isozyme has an optimum pH of 9.0. It only acts on
free polyunsaturated fatty acids and it forms 9- and 13hydroperoxides in the ratio of 1:9 at room temperature
[20]. Some types of lipoxygenases can also catalyse the
co-oxidation of carotenoids in the presence of PUFAs. Soybean lipoxygenase type-1 (LOX-1) has been used for the
bleaching of wheat our and also been shown to act as a

bread improver and a valuable processing aid during dough

development [21].
(2) Soy isozyme has an optimum pH of 6.8, it acts on triglycerides as well as free polyunsaturated fatty acids and it forms
9- and 13-hydroperoxide in the ratio of about 1:1 at room
temperature [20]. A bleached color can also indicate deterioration in either fresh vegetables, such as yellow French beans
or fruits and processed food products, where carotenoids are
important natural colorants and antioxidants. It has been
reported that type-2 lipoxygenases (LOX-2 and -3) of soybean, pea and wheat are pigment bleachers in the presence
of linoleic acid [22], but most of the reported studies for the
co-oxidation of carotenoids have been for soybean LOX-1.
It has been claimed that, under anaerobic conditions, this
enzyme shows strong co-oxidising activities in the presence of PUFA or a corresponding acyl hydroperoxide [23],
whereas, under aerobic conditions, it is not an efcient catalyst for the bleaching reaction [24,13,1,25].
(3) Soy isozyme is similar to isozyme 2, but its activity is inhibited by calcium ions, whereas lipoxygenase-2 is stimulated
by the metal [20].
(4) Lipoxygenase is very similar to isozyme 3, but can be separated by gel chromatography or electrophoresis [20].
Lipoxygenase isozymes are commonly classied as type 1,
which have an optimum pH in the alkaline region and are specic for free fatty acids and type 2, which has optimum activity
at neutral pH and causes co-oxidation of carotenoids. The ability
of lipoxygenase type 2 to bleach carotenoids has found practical
application in the addition of soybean our to wheat our in
order to bleach the our in the manufacture of white bread [16].
For LOX-3 an increase in foaming activity has been reported,
as well as an overall improvement in bread making quality of
wheat our. The bakery yeast Saccharomyces cerevisiae also
contains LOX. Recently, this enzyme was partially puried, but

its potential, if any, on bread making remains to be established.

Nowadays, it is feasible to change the prole and content of LOX
(iso)enzymes in plants either by classical means, or potentially
by genetic modication [7,25]. For example, by appropriate
crosses, near-isogenic soybean seeds have been developed that
lack either isoenzymes L1 and L3, or isoenzymes L2 and L3.
These LOX-minus mutants still grow well in the eld. In principle, transgenic plants lacking or over expressing one or more
LOX isoenzymes could be constructed and tailored to specic
applications [20]. To that end, the heterologous expression of
one or more soybean LOX isoenzymes in wheat could be of
interest. It is interesting to note that the use of soybean lipoxygenase was described in the 1930s as a means to bleach the our
in preparation of white bread. More recent experiments have
shown that carotenoids present in wheat our are destroyed by
co-oxidation. Wheat our itself contains little LOX activity, but
LOX is abundantly present in soybeans [4,11,16]. To that end,
wheat our is often fortied with up to 0.5% enzyme-active
soy our. Other applications of LOX include the bleaching of
noodles, whey products, rice and wheat bran [4].
In plant tissues, various enzymes occur that cause the conversion of hydroperoxides to other products, some of which
are important as avour compounds. These enzymes include
hydroperoxide lyase, which catalyses the formation of aldehydes and oxo acids, hydroperoxide-dependent peroxygenase
and epoxygenase, which catalyse the formation of epoxy and
hydroxy fatty acids, and hydroperoxide isomerase, which catalyses the formation of epoxyhydroxy fatty acids and trihydroxy
fatty acids. Lipoxygenase produces similar avour volatiles
to those produced during autoxidation, although the relative
proportions of the products may vary widely depending on
the specicity of the enzyme and the reaction conditions
[16].
Potato lipoxygenase, although up to date studies have not
well realized, is unusual as it is a plant enzyme, which resembles mammalian lipoxygenase and catalyses the oxidation of
the 20-carbon atom PUFA, arachidonic acid, to form 15hydroperoxyeicosatetraenoic acid as the major product [9,15].
In animals, this hydroperoxide is the precursor of biologically active compounds of considerable pharmaceutical interest.
Thus, potato lipoxygenase is of special interest because of
its greater availability and its potential use as a model and
alternative for the mammalian enzyme. Three isoenzymes of
lipoxygenase have been isolated from potato [26] and dened
as LOX-1, -2 and -3. Linoleic acid has been claimed to be the
preferred substrate for potato LOX-1 and the 9-hydroperoxide
as the dominant product. On the other hand, linolenic acid has
been claimed as the preferred substrate for both potato LOX-2
and -3, which produce the 13-hydroperoxide as the main product. Also potatoes contain different leaf and tuber lipoxygenases
[26] with different regiospecicities; the leaf lipoxygenase that
produces 13-hydroperoxides from linolenic acid is involved in
the synthesis of jasmonate [27,28], an important elicitor of plant
defence gene expression, through the so-called octadecanoid
signalling pathway [8].
Tomato also contain a fruit 9-lipoxygenase activity and a
leaf activity [29,30]. In tomatoes at least two isoenzymes have

been identied different thermal stabilities. Similarly, resistant

and labile lipoxygenase isoenzymes have already been observed
in many vegetable products (potato, wheat germ, green beans,
peas), as well as in tomato [31]. This LOX activity also causes
color degradation for frozen tomato cubes during storage. In
tomato cubes, LOX activity was investigated during frozen storage and it has been observed that LOX activity was increased
during storage. In order to prevent color degradation of tomato
cubes, they were coated by modied starch. The results showed
that LOX activity decreased and the color was found better than
the uncoated samples during frozen storage [32].
The cucumber LOX enzyme was similar to the potato
and tomato enzymes, both in pH characteristics and substrate
specicity [33]. In apples, LOX activity during storage was
investigated in the core, esh and peel. Activity was always highest in the core and peel. On storage, activity was increased in
each part of the fruit but especially in the core and peel. Increase
in LOX preceded the browning of the core. LOX may be responsible for the browning and may be concerned in the induction of
supercial scald [34]. LOX has been reported to be involved in
ripening process in strawberry fruit and thus, albino fruit have
lower LOX activity due to poor color development in them [35].
Pea has a complex lipoxygenase gene family with at least ve
enzymes each in seeds [36] and nodules [37] and yet more in
stems and roots [36]. In some species the leaf enzymes have been
shown to be targeted to the chloroplast [26,28]; such plastidial
enzymes are sufciently different from other lipoxygenases to
be classied as a separate group [38].
3.2. Iron content
Lipoxygenase molecules contain one atom of iron. The iron
atom is in the high spin Fe(II) state in the native resting form
of lipoxygenase, and must be oxidised to Fe(III) by the reaction
product, fatty acid hydroperoxides or hydrogen peroxide before
activating as an oxidation catalyst [1,2]. As a consequence of
this requirement for oxidation of the iron in the enzyme, a lag
period is observed, when the enzyme is used with pure fatty
acid substrates. The active enzyme abstracts a hydrogen atom
stereospecically from the intervening methylene group of a
polyunsaturated fatty acid in a rate limiting step with the iron
being reduced to Fe(II) [3,4]. The enzymealkyl radical complex is then oxidised by molecular oxygen to an enzymeperoxy
radical complex under aerobic conditions, before the transference of electron from the ferrous atom to the peroxy group occurs
[14,17]. Protonation and dissociation from the enzyme allow the
formation of the hydroperoxide. Under anaerobic conditions, the
alkyl radical dissociates from the enzymealkyl radical complex
and then a mixture of products including dimers, ketones and
epoxides is produced by radical reactions [15].
4. Inhibition of lipoxygenase oxidation
Blanching is the inactivation of enzymes that caused
undesirable changes during the processing and subsequent
storage of the products. It has also a number of other advantages
including color stability, improvement in texture and decrease in

microbial population [39]. Heating vegetables to a temperature

high enough to inactivate peroxidase (POD) is generally more
than enough to destroy the undesirable enzymes, since POD
activity has not been shown to be directly responsible for quality
deterioration during frozen storage of vegetables. The use of
LOX as indicator of proper blanching has been recommended
as more signicant in determining storage stability in frozen
vegetables [40,41]. LOX has been associated with quality
deterioration because of its involvement in off-avour and odor
production, loss of pigments such as carotenes and chlorophylls,
and destruction of essential fatty acids [42].
Lipoxygenases can be thermally inactivated above 60 C with
a resulting improvement in the shelf life of foods. However,
heating also increases non-enzymatic oxidation and thus may
exceed the oxidation due to lipoxygenase [43].
Optimum oxidative stability can be achieved by minimizing
exposure of lipids and lipid containing food products to air, light
and higher temperatures during processing and storage. Theoretically, the most convenient way of preserving fatty foods from
oxidative spoilage is to remove all oxygen from the food during
manufacture and from the packaging container. Modern packaging material and equipment allows inert-gas vacuum packaging,
but residual oxygen levels of less than 1% are extremely difcult
to obtain in a production environment. Liquid oils were traditionally packaged in clear glass containers and brown bottles
were sometimes used to protect unstable oils from light oxidation. Glass bottles have now been replaced by plastic containers.
Since it is superior to polyethylene, which is more permeable to
oxygen, polyvinyl chloride is preferred [15].

[4]
[5]

[6]

[7]

[8]

[9]

[10]

[11]
[12]

[13]
[14]

[15]

5. Conclusion
[16]

In order to develop new food products, for achieving higher

rates and levels of extraction, or improve food quality in terms
of, e.g. avour, some enzymes are positively utilized during
food processing for recovery of by-products. On the other hand,
enzymes might also have detrimental effects on food quality.
Food quality defects can be caused by enzymes naturally present
in the food or by enzymes produced by certain microorganisms.
Hence, besides microbial inactivation, preservation technologies
aim at inactivating enzymes with deteriorative action. Owing to
the benecial and/or detrimental effects of enzymes, control of
enzymatic activity is required in many food processing steps.
The use of LOX as indicator of proper blanching has been
recommended, which is more signicant in determining storage stability in frozen vegetables. For industry, rapid detecting
methods of LOX activation must be studied.
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