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A Comprehensive Review on Function and Application of Plant Peroxidases

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DOI: 10.4172/2161-1009.1000308

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 nalytica

Biochemistry &
ry &A l Pandey et al., Biochem Anal Biochem 2017, 6:1

Bi
DOI: 10.4172/2161-1009.1000308
chemist

och
emistry
Analytical Biochemistry
Bio

ISSN: 2161-1009

Research Article OMICS International

A Comprehensive Review on Function and Application of Plant

Peroxidases
Veda P Pandey, Manika Awasthi, Swati Singh, Sameeksha Tiwari and Upendra N Dwivedi*
Bioinformatics Infrastructure Facility, Center of Excellence in Bioinformatics, Department of Biochemistry, University of Lucknow, Uttar Pradesh, India

Abstract
Peroxidases, one of the key antioxidant enzymes, are widely distributed in nature and catalyze oxidation of various
electron donor substrates concomitant with the decomposition of H2O2. The non-animal plant peroxidases (class III
peroxidase) are involved in various essential physiological processes of plant growth and development throughout
their life cycle. In view of the capability of peroxidases to catalyze the redox reaction for a wide range of substrates,
they are considered as one of the important enzyme from the point of view of their various medicinal, biochemical,
immunological, biotechnological and industrial applications. They have been successfully used for biopulping and bio-
bleaching in the paper and textile industries. Peroxidases have also been used in organic synthesis, bioremediation,
as well as various analytical applications in diagnostic kits, ELISA. Peroxidase based biosensors find application in
analytical systems for determination of hydrogen peroxide, glucose, alcohols, glutamate, and choline etc. Thus, in
view of array of physiological functions as well as industrial applications, the peroxidases have conquered a dominant
position in research groups and become one of the most extensively studied enzymes. In this direction, the present
review embodies the classification, mechanism of action, major physiological functions as well as industrial applications
of plant peroxidases.

Keywords: Heme peroxidase; Analytical applications; Biosensor Classification of peroxidases

development; Class III peroxidase; Dye decolorization
On the basis of presence or absence of heme, the peroxidases have
Introduction been classified into heme and non-heme peroxidases [1]. According to
PeroxiBase database, >80% of known peroxidase genes are reported to
Development of environmentally sustainable processes is a code for heme-containing peroxidases. On the other hand, the non-
challengeable task for the current bioeconomy. In this direction, the heme peroxidases such as thiol peroxidase, alkylhydroperoxidase,
use of biocatalysts, enzymes, in various processes is considered as an NADH peroxidase constitute only a small proportion. Since majority
ecofriendly approach. The stability, activity and specificity of enzymes of the peroxidase sequences are reported to be heme peroxidases, thus
are the fundamental parameters that are required to develop enzymes they are described in detail.
for their optimal applications in various industrial processes. Therefore,
identification of newer sources for such novel enzymes with desired Heme peroxidases have further been assigned to two superfamilies,
properties is important. Furthermore, modern approaches such as in- namely peroxidase-cyclooxygenase superfamily (PCOXS) and the
silico molecular modeling concomitant with site directed mutagenesis peroxidase-catalase superfamily (PCATS) [2,3]. Description of
to develop such novel enzymes with improved attributes are also in these peroxidase superfamilies are presented as follows. A schematic
great demand. The present thesis is an effort in this direction. classification of peroxidases is presented in Figure 1.

Peroxidases (EC.1.11.1.x) are hydrogen peroxide (H2O2) The Peroxidase-Cyclooxygenase Superfamily (PCOXS): The
decomposing enzymes concomitant with the oxidation of wide range peroxidases of PCOXS superfamily exclusively contain animal
of phenolic as well as non- phenolic substrates (RH) peroxidases which have been suggested to be involved in the innate
immunity, defense responses etc. [4,5]. The myeloperoxidase (MPO),
2RH + H2O2 → 2R° + 2H2O eosinophil peroxidase (EPO), lactoperoxidase (LPO), thyroid
They are ubiquitous in nature being found in bacteria, fungi, peroxidase (TPO) are belonging to this family. In this superfamily, the
algae, plants and animals. The plant peroxidases, belonging to Class prosthetic heme group is covalently linked with the apoprotein.
III peroxidase, are implicated in various vital processes of plant The Peroxidase-Catalase Superfamily (PCATS): The PCATS is the
growth and development throughout the plant life cycle including cell most intensively studied superfamily of non-animal heme peroxidases.
wall metabolism, lignification, suberization, reactive oxygen species
(ROS) metabolism, auxin metabolism, fruit growth and ripening,
defense against pathogens etc. Due to versatility in reaction catalyzed
by peroxidases, and their ubiquitous nature, they have immense *Corresponding author: Upendra N Dwivedi, Department of Biochemistry, University
potential to be an industrial enzyme with application in various of Lucknow, Lucknow 226007, Uttar Pradesh, India, Tel: +91-522-2740132; E-mail:
[email protected]
medicinal, immunological, biotechnological and industrial sectors.
The peroxidases find applications in bioremediation, textile synthetic Received: November 03, 2016; Accepted: January 21, 2017; Published January
24, 2017
dye decolorization, polymer synthesis, paper and pulp industry,
in development of biosensor, diagnosis kits etc. In view of various Citation: Pandey VP, Awasthi M, Singh S, Tiwari S, Dwivedi UN (2017) A
Comprehensive Review on Function and Application of Plant Peroxidases.
applications, the identification of newer sources of novel peroxidase
Biochem Anal Biochem 6: 308. doi: 10.4172/2161-1009.1000308
offering resistance towards temperature, pH, salts, heavy metals,
organic solvents etc. is highly desirable. Thus, the present review is an Copyright: © 2017 Pandey VP, et al. This is an open-access article distributed
under the terms of the Creative Commons Attribution License, which permits
attempt to summarize various physiological functions as well as the unrestricted use, distribution, and reproduction in any medium, provided the
industrial applications of plant peroxidases. original author and source are credited.

Biochem Anal Biochem, an open access journal

ISSN: 2161-1009 Volume 6 • Issue 1 • 1000308
Citation: Pandey VP, Awasthi M, Singh S, Tiwari S, Dwivedi UN (2017) A Comprehensive Review on Function and Application of Plant Peroxidases.
Biochem Anal Biochem 6: 308. doi: 10.4172/2161-1009.1000308

Page 2 of 16

Figure 1: Schematic representation of classification of peroxidases.

Initially, the superfamily was named as the plant, fungal and bacterial [14]. In the PeroxiBase database, 609 sequences of class II peroxidases
heme peroxidase superfamily depending upon the sources of the are reported till date. White-rot fungal lignin peroxidases (LiPs; EC
peroxidases. Later on, due to emergence of new cnidarians peroxidase, 1.11.1.14) are secretary in nature and catalyze depolymerization of
the name of this superfamily was changed as peroxidase-catalase lignin as well as possess immense potentials for waste disposal of a
superfamily. number of phenolic as well as non-phenolic compounds. Manganese
peroxidases (MnP; EC 1.11.1.13), are also secreted by lignin-degrading
The non-animal peroxidases have further been sub-divided into
white-rot fungi. They catalyze the peroxide-dependent oxidation of Mn
three classes namely, class I, II and III peroxidases as described in
(II) to Mn (III) and the Mn (III) is released from the enzyme as oxalate-
following sections.
Mn (III) complex that serve as diffusible redox mediator having ability
(a) Class I Peroxidases: The class I peroxidases include both to oxidize lignin. Versatile peroxidases (VP; EC 1.11.1.16) exhibited
prokaryotic and eukaryotic peroxidases belonging to non-animal a hybrid molecular architecture between LiPs and MnPs [15]. They
sources. Currently, 1839 sequences of this class are reported in are not only specific for Mn (II) as in 3MnPs, but also catalyze the
PeroxiBase database. They exhibited major role in oxidative stress oxidation of phenolic and non-phenolic substrates like LiPs, in the
i.e., detoxification of ROS (H2O2) [6-8]. They include cytochrome absence of manganese [16]. In contrary to class I peroxidases, the
c peroxidase (CCP; EC 1.11.1.5), ascorbate peroxidase (APX; EC class II peroxidases have N-terminal signal peptides, four conserved
1.11.1.11) and catalase ­peroxidase (CP; EC 1.11.1.6). The cytochrome disulphide bridges (differently located to those of class III) and calcium
c peroxidase (CCP), uses reducing equivalents from cytochrome c and in their structure.
reduces hydrogen peroxide to water. Ascorbate peroxidases (APx)
(c) Class III Peroxidases: The class III peroxidases are widely
are involved in hydrogen peroxide detoxification using ascorbate as
distributed in plant kingdom [17,18]. In the PeroxiBase database [1],
reducing equivalents as well as in photo-protection of the chloroplasts
5692 sequences of class III peroxidases (~ 70% of total non-animal heme
and cytosol in higher plants [9,10]. The catalase-peroxidases (CPs),
peroxidases) are reported till date. They include horseradish peroxidases
predominantly reported in bacteria, are bi-functional antioxidant
(HRP), peanut peroxidase (PNP), soybean peroxidase (SBP), etc. and
enzymes that exhibit both catalase and peroxidase enzyme activity.
they are reported to play crucial roles in the plant life cycle [19]. Thus,
Due to their unique catalytic capacity to dismutate hydrogen peroxide
they are involved in wide range of physiological processes such as
and ability to evolve molecular oxygen (O2) by oxidation of H2O2,
cell wall metabolism [20], lignification [21], suberization [22], auxins
they prevent bacteria from oxidative stress [11]. Evolutionary they are
metabolism [23], wound healing [24], reactive oxygen species (ROS)
closely related to ascorbate peroxidases and cytochrome c-peroxidases
and reactive nitrogen species (RNS) metabolism [25,26], fruit growth
[12,13]. At the structural level, the class I peroxidases lack disulphide
and ripening [27] defense against pathogens [28] etc. These peroxidases
bridges, calcium and an endoplasmic reticulum signal sequence.
exist as multigene family as evident by 73 and 138 peroxidase genes in
(b) Class II Peroxidases: The class II peroxidases, exclusively the genomic sequences of Arabidopsis (Arabidopsis Genome Initiative,
containing fungal peroxidases, have major role in lignin biodegradation 2000) and rice (International Rice Genome Sequencing Project, 2005),

Biochem Anal Biochem, an open access journal

ISSN: 2161-1009 Volume 6 • Issue 1 • 1000308
Citation: Pandey VP, Awasthi M, Singh S, Tiwari S, Dwivedi UN (2017) A Comprehensive Review on Function and Application of Plant Peroxidases.
Biochem Anal Biochem 6: 308. doi: 10.4172/2161-1009.1000308

Page 3 of 16

Figure 2: Catalytic cycle of heme peroxidases showing catalytic events (oxidation-reduction) occur at heme (Fe+ porphyrin IX) center of the enzyme. At the end of the
reaction, H2O2 is degraded to H2O and reducing equivalent (RH) is polymerized.

respectively [17,29,30]. Similar to class II peroxidases, in the structural coordinated peroxide undergoes rapid heterolytic cleavage, producing
fold, the class III peroxidases also contain N-terminal signal peptides, a molecule of water and the semi-stable intermediate referred to as
four conserved disulphide bridges and calcium. In the present review, compound I (green in color, and also referred as oxyferryl porphyrin π
the class III plant peroxidases are detailed below. cation radical). The reaction involves transfer of a proton from peroxide
O1 to O2, followed by breaking of O-O bond. Departure of O2 as water
Evolutionary relationship between heme peroxidases molecule leaves O1 that is already coordinated to the heme with only
The heme peroxidases of non-animal origin show low amino six electrons. It completes its octate by abstracting the two most readily
acid sequence identity (less than 20%) but, share similar helical folds available electrons from the enzyme. One electron is removed from the
independent to the presence (in plant and fungal peroxidases) and iron, creating an oxy-ferryl (Fe=O) center. Generally, in case of most
absence (in bacterial peroxidases) of disulfide bridges and structural of the peroxidases, the second electron is removed from the porphyrin
calcium ions. Recently [31] have also studied the comparative account ring, creating a porphyrin pi-cation radical.
of non-animal heme peroxidases and reported that the peroxidases are
This porphyrin radical accepts one electron from an electron
clustered into three major classes. In addition, [6] have suggested that
the class I peroxidases are the origin point for the other two classes of donor substrate, yielding a substrate free radical and compound II
peroxidases. (red in color and referred as oxyferryl heme intermediate). In the next
one-electron reduction step from a second molecule of the substrate
Mechanism of action reduces compound II to the resting ferric peroxidase [34,35].
Peroxidases share a common catalytic mechanism for the Another intermediate namely the compound III, in which the iron
degradation of hydrogen peroxide [32]. The peroxidase reaction is a is in the ferrous state, is usually formed when there is a large excess of
two-electron oxidation-reduction with three distinct steps [33] : H2O2. It is likely that this intermediate is largely formed by combination
Peroxidase + H2O2 → Compound I + H2O ……………… …. .(1) of superoxide, generated by the oxidation of H2O2, with the ferric
Compound I + RH → Compound II + R° ……………………. (2)
enzyme, although superoxide could also be generated by electron
Compound II + RH → Peroxidase + R ° + H2O……………….. . (3 )
transfer from oxidized substrates to molecular oxygen. Compound III
______________________________________________________________
is not a catalytically active intermediate.
2RH + H2O2 → 2R ° + 2H2O Physiological roles of plant peroxidases
___________________________________________________________
Where, RH is a peroxidase substrate and R° is a free-radical product Class III plant peroxidases have been reported to play diverse
derived from it. functions in the plant life cycle such as in cell wall metabolism,
lignification, suberization, ROS metabolism, wound healing, fruit
The catalytic cycle of heme peroxidases specific to plants begins growth and ripening, seed germination etc. [36]. A schematic
with the coordination of peroxide to the ferric heme (Figure 2). The representation of diverse functions of class III peroxidases is presented

Biochem Anal Biochem, an open access journal

ISSN: 2161-1009 Volume 6 • Issue 1 • 1000308
Citation: Pandey VP, Awasthi M, Singh S, Tiwari S, Dwivedi UN (2017) A Comprehensive Review on Function and Application of Plant Peroxidases.
Biochem Anal Biochem 6: 308. doi: 10.4172/2161-1009.1000308

Page 4 of 16

Figure 3: A schematic representation of various roles of plant peroxidases.

Figure 4: Generalized lignin biosynthesis pathway indicating the role of peroxidases.

Biochem Anal Biochem, an open access journal

ISSN: 2161-1009 Volume 6 • Issue 1 • 1000308
Citation: Pandey VP, Awasthi M, Singh S, Tiwari S, Dwivedi UN (2017) A Comprehensive Review on Function and Application of Plant Peroxidases.
Biochem Anal Biochem 6: 308. doi: 10.4172/2161-1009.1000308

Page 5 of 16

in Figure 3. Some major roles of peroxidases are described in following and highly differentiated plant cells capable of forming secondary cell
sections: walls. The cell wall peroxidases polymerize the hydroxycinnamic acid
and their derivatives by converting them into phenoxy radicals that are
Lignification and suberization then deposited on the extracellular surface. The accumulation of these
Lignification occurs during normal growth and defense responses polymers strengthens the cell wall, thereby restricting cell expansion
in plants and is one of the classical functions attributed to Class III and pathogen invasion, and confers structural strength to the plant
peroxidases [37]. Lignin, a phenolic heteropolymer, present in the cell body, which is especially important for trees and construction of xylem
wall of plants and provides rigidity, strength, and resistance to chemical, vessels.
physical as well as biological attacks. Lignin which contributes about
Plant defense against pathogen infection
25% of the plant biomass is considered as one of the greatest obstacle
towards the optimal utilization of the plant biomass for various Plants protect themselves, after pathogen attack, through
purposes such as paper manufacturing, production of highly palatable the passive and active defense mechanisms. The passive defense
forage and bagasse utilization. mechanisms involve structural barriers or existing anti-microbial
compounds which prevent colonization in the tissue, while, the active
Chemically, lignin is made up of mainly three types of monolignols,
or induced defense responses include the hypersensitive response (HR)
namely p-coumaryl alcohol, sinapyl alcohol and coniferyl alcohol.
and systemic acquired resistance (SAR) i.e., production of phytoalexins
These monolignols are synthesized via phenyl propanoid (PP) and pathogenesis-related (PR) proteins, reactive oxygen species (ROS)
pathway which starts with deamination of phenylalanine, followed by and reactive nitrogen species (RNS) (oxidative bursts), ion fluxes across
successive hydroxylations, methylations, thiol ester formation and two the plasma membrane, lignification and the reinforcement of the cell
reduction reactions leading to the formation of the three major kinds of wall through both the cross-linking of cell wall structural proteins.
monolignols. These monolignols are transported to cell wall in the form The active defense responses are regulated through a complex and
of glycosides and there glucosidase enzyme release the monolignols. interconnected network of signaling pathways mediated by salicylic
The polymerization of the monolignols, into lignin involves an acid (SA), jasmonic acid (JA) and ethylene (ET).
oxidative mechanism with the consequent formation of phenoxy Among the proteins induced during the plant defense, the class
radicals, through the action of oxidative enzymes, such as peroxidases. III plant peroxidases are well known and they play roles through (1)
The schematic representation of lignin biosynthesis pathway along reinforcement of cell wall physical barriers comprising lignin, suberin,
with the role of peroxidase is represented in Figure 4. feruloylated polysaccharides and hydroxyproline-rich glycoproteins
There are several reports suggesting higher expression of peroxidase [46,47] ; (2) enhanced production of reactive oxygen species as
genes in the tissues undergoing lignification [38]. Thus, Mader and signal mediators and antimicrobial agents [48-50] ; and (3) enhanced
Amberg- Fisher [39] have reported that the peroxidases have ability production of phytoalexin [51].
to polymerize cinnamylalcohols in the presence of hydrogen peroxide. Peroxidases have been reported to be induced by fungal infection
Furthermore, based on experimental study, Andrews et al. [40] have [52,53], bacterial infection [54,55], infection caused by viruses
demonstrated the link between peroxidase isoenzymes and the cross and viroids etc. [56-59]. In tobacco, a positive correlation between
linking of cell wall components and the deposition of lignin-like peroxidase activity and resistance to tobacco wildfire disease was
phenolics in the epidermis of the tomato fruits. Christensen et al. reported [60,61]. Furthermore, [54] have reported a rapid induction of
[38] have purified and characterized five peroxidases in poplar xylem a cationic peroxidase in rice plants, infected with Xanthomonas oryzae
and also analyzed their correlation with lignification via oxidation of pv. oryzae.
syringaldazine (a lignin monomer analogue). The recombinant papaya
peroxidase was also reported to be involved in defense response and Wound healing
lignification via qRTPCR and activity measurement with coniferyl Plants respond to wounding by activating self-defense systems to
alcohol [41]. In addition, Ostergaard et al. [42] have reported an restore damaged tissues or to defend against attacks by pathogens and
extracellular peroxidase from lignifying Arabidopsis thaliana cell herbivores. Among the large number of wound-inducible proteins,
suspension cultures. The authors have also done mutational studied peroxidase have been shown to express upon mechanical wounding
and proposed a possible correlation between the enzyme and the in various plants, including tobacco [57,58], tomato [62], potato [62],
increased levels of lignin in a mutant Arabidopsis. The evidence for a cucumber [63], azuki bean [64], rice [65], horseradish [66] and sweet
role of peroxidases in lignification has also been supported by studies potato [67].
on transgenic plants with altered peroxidase activity. For example,
Quiroga et al. [43] showed that expression of a tomato peroxidase Reactive Oxygen Species (ROS) metabolism
gene, in transgenic tobacco resulted in an increase in lignin content.
The Reactive Oxygen Species (ROS) are partially reduced forms of
Lagrimini et al. [44] have also found higher levels of lignin in transgenic
atmospheric oxygen (O2) and produced by the excitation of oxygen to
tobacco with over-expressed peroxidase than the wild type plants.
form a singlet oxygen (O21) or from the transfer of electrons to O2, to
Suberization has been believed to play a role in the defensive form superoxide radical in the case of one electron; hydrogen peroxide
responses against the entry of pathogenic micro-organisms through (H2O2) if two electrons are transferred; or hydroxyl radical (OH-) when
a wounded part by developing physical barrier [43,45]. This protects three electrons have been transferred to oxygen. These reduced species
tissue from water loss and pathogen invasion. Suberized tissues are of oxygen are highly reactive and are capable of oxidizing various
found in various underground organs like roots, stolon and tuber as cellular components leading to the oxidative damage of the plant cell
well as in periderm layer. They are formed as a part of wound and that is associated with the peroxidation of membrane lipids, protein
pathogen induced defenses of specific organs and cell types, perhaps oxidation, enzyme inhibition and DNA damage that ultimately leads
the most familiar example being the browning of sliced potato tubers. to Programmed Cell Death (PCD) [68-70]. In plant cells, ROS are
Lignification and suberization are terminal processes of determinate produced in cell walls, chloroplasts, mitochondria, plasma membrane,

Biochem Anal Biochem, an open access journal

ISSN: 2161-1009 Volume 6 • Issue 1 • 1000308
Citation: Pandey VP, Awasthi M, Singh S, Tiwari S, Dwivedi UN (2017) A Comprehensive Review on Function and Application of Plant Peroxidases.
Biochem Anal Biochem 6: 308. doi: 10.4172/2161-1009.1000308

Page 6 of 16

endoplasmic reticulum, and apoplastic space [68,71]. In plants, the Stress tolerance
cellular level of H2O2 is mostly regulated by enzymatic actions of
catalases and peroxidases. In addition to scavenging H2O2, the cell wall Peroxidases are considered as one of the stress indicators of plants
peroxidases have been considered to catalyze O2- and H2O2 formation because their level considerably increases after stress stimulation.
through oxidation of substrates such as NADH and IAA, in the absence Lignification also occurs due to stress responses [73].
of exogenous H2O2 [71]. The role of peroxidases and other antioxidant enzymes on heat stress
Auxin catabolism have been documented by various researchers. Thus, Larkindale and
Huang [90] have demonstrated that the expression level of peroxidases
Peroxidases play an important role in auxin catabolism through and superoxide dismutase increased, while those of catalase decreased
the oxidative carboxylation of indole-3-acetic acid (IAA) [72]. IAA, after heat treatment of creeping bentgrass plants. Similarly, Edreva et
one of the most studied plant growth regulators, is found throughout
al. [91] have also investigated the role of peroxidases in bean plants and
the plant, but is at highest concentrations in the apical and other
they found that peroxidase activity is increased after heat treatment.
meristematic regions. Auxin affects the plant development through
apical dominance, cell elongation, ethylene formation and adventitious Salinity stress is caused by accumulation of dissolved salts in soil
root formation. Plant peroxidases are involved in the oxidation of auxin water either through natural process or due to human induced activity
either through the conventional H2O2-dependent pathway or through and the high salt accumulation in the soil can affect the growth of the
a H2O2-independent and O2-dependent pathway. As specific IAA plants [92,93]. Amaya et al. [94] have investigated the role of a cell
oxygenases, the peroxidases have domains, similar to auxin-binding
wall peroxidase in the response to salt stress. They have observed the
proteins, which are missing in non-plant peroxidases [23].
increased rates of seed germination in transgenic tobacco with over-
Gazaryan et al. [23] have also reported that over-expressing expressed peroxidase under both osmotic and salt stress. They have also
peroxidase in tobacco plants showed depressed IAA levels with suggested that enhancement of peroxidase activity stabilizes the cell
decreased root branching and closed stomata. On the other hand, plants wall structure and higher germination rate might be due to the better
with suppressed peroxidase showed increased levels of IAA and rapid capacity to retain water that reduces the effect of water deficit caused
shoot growth, fused leaves and early flowering. Based on experimental by the salinity. Pujari and Chanda [95] have also studied the effect of
study, Jansen et al. [73] have reported the transgenic tobacco with over-
high salinity on the levels of peroxidase expression in vigna seedlings
expressed peroxidase exhibited increased UV tolerance and decreased
and have reported higher activity of peroxidases in salt treated plants.
IAA levels, suggesting the contribution of the peroxidases in UV
tolerance and auxin catabolism. Furthermore, Schopfer [74] have also Metals such as manganese (Mn), zinc (Zn), copper (Cu) etc. are
reported the involvement of plant peroxidases in cell elongation via necessary for the plant development in trace amounts but in excess
IAA catabolism. they become toxic for the plant [96]. In general, increase in peroxidase
Seed germination expression in response to various metals are reported and it is suggested
that this increase could be a kind of defensive response for scavenging
The seed occupies a unique position and has fundamental the H2O2 generated due to metal toxicity [97]. Assche and Clijsters
importance in plant physiology because most of the known physiological [98] have reported the induction in peroxidase activity in leaves and
processes are concentrated in the growth and development of the seed.
roots treated with toxic doses of Zn, Cd, Ni and Pb. In addition, Fang
The exact reaction between activation of essential enzymes, sequential
and Kao [99] have also reported the increase in peroxidases activity
release of hormones and the energy relations of the process during
the germination of seed are still unknown. An increase in peroxidase as well as changes in the isozyme patterns after exposure to iron,
activity during seed germination has been reported [75]. Fridovich copper and zinc in rice leaves and have suggested that the toxic levels
[76] and Gasper et al. [77] have suggested that the peroxidase removes of the metals could be responsible for both quantitative and qualitative
various toxic products from the seeds as a natural scavenger for seeds. changes in the peroxidase. Abercrombie et al. [100] have also reported
After 4 days of germination in mung bean seedlings. Dendsay and that in response to metals such as aluminum, arsenic, etc. the class III
Sachar [78] have observed a 30-fold activation of peroxidase activity. peroxidase genes are over expressed.
In cotton plants, increase in peroxidase activity is also correlated with
auxin induced ethylene biosynthesis [79,80]. Ultraviolet-B radiation is reported to influence the plant
metabolism, growth and development leading to affecting
Fruit ripening photosynthesis, flowering, pollination and transpiration by altering
gene expression [101]. Jansen et al. [102-120] have analyzed various
Ethylene has been demonstrated as an essential plant hormone
involved in initiation of fruit ripening as well as promotion of tobacco lines with altered peroxidase expression and suggested a clear
maturation and abscission of fruits and in the regulation of senescence link between peroxidase activity and UV tolerance. UV tolerance has
and fading of flowers [81]. Peroxidases also contribute to the synthesis been reported to be linked with levels of peroxidases in plant. Thus,
of ethylene. L- methionine is the precursor for ethylene in tissues Jansen et al. [73] demonstrated that UV-tolerant plants exhibited more
of higher plants. Three enzymes are involved in this methionine- peroxidase expression than the sensitive type.
methional-ethylene pathway with peroxidase being most limiting
Isolation, purification, and characterization of some peroxi-
enzyme in ethylene biosynthesis. Zymograms of peroxidase show
change in activity pattern during initial stages fruit ripening [82]. Both
dases
positive and negative correlations between peroxidase activity and fruit Plant peroxidases from various sources such as Eruca vesicaria,
ripening have been reported in literature. Thus, peroxidase activities in tea, Ficus, lettuce, citrus, broccoli, royal palm, soybean, Leucaena
mango, apples, banana fruits etc. have been reported to increase with leucocephala, papaya, wheat grasss, Solanum melongena, lemon etc.
ripening [83-85] while, those of tomato, strawberry, capsicum, papaya have been isolated, purified and characterized. A brief description of
fruits etc. decrease with ripening [86-89]. physicochemical properties of some of them is presented in Table 1.

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ISSN: 2161-1009 Volume 6 • Issue 1 • 1000308
Citation: Pandey VP, Awasthi M, Singh S, Tiwari S, Dwivedi UN (2017) A Comprehensive Review on Function and Application of Plant Peroxidases.
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Page 7 of 16

pH Temperature Km/affinity for Effect of metal/

S. No. Source Mol. Weight Thermostability References
optimum optimum substrates organic solvent
Guaiacol> Retained 20-30% activity at 50,
Inhibited by Li+, Zn2+ Mohamed, et
1 Citrus jambhiri 56 kDa 5.5 40°C O-dianisidine> 60, and 70°C after 15, 10, and
and Hg2+ al. (2008)
pyrogallol 5 min of incubation
Not affected by Zn2+,
o-dianisidine: 9.35 mM Lost 55% activity at 65°C within
2 Prunus persica 29 kDa 5 40°C Cu2+, Mg2+, Mn2+, NH4+ Neves (2002)
H2O2: 15.38 mM 1 min
(1.5-6.0 µM)
• Inhibited by Fe3+,
Zn2+, Ca2+, Cu2+, Mn2+
Lactuca sativa Guaiacol: 4.74 mM Retained 55% activity at 60°C • 40-70% loss of Hu et al.,
3 35 kDa 5.0 45°C activity in presence of
L. pyrogallol: 1.96 mM after 1 hr (2012)
25% propylene glycol,
ethanol, acetone and
methanol
Guaiacol: 0.8 mM
Mg2+ as a potent
O-dianisidine: 0.125 Retained 80% activity at 60°C Pandey et
4 Carica papaya 240 kDa 7.0 40°C activator and Ca2+ as a
mM ascorbic acid: 5.2 upto 1 Hr al., (2012)
weak activator
mM H2O2: 0.25 mM
Roystonea 51 kDa o-dianisidine: 9.35 mM Stable at 70°C after 1 h Sakharov et
5 4-11 - -
regia H2O2: 15.38 mM incubation al. (2001)
Guaiacol: 9.5 mM • Activated by Ca2+,
Ficus O-dianisidine: 16.6 mM Ni+2 and Mg2+ Mohamed et
6 43 kDa 5.5-7.0 5°C to 40°C -
sycomorus pyrogallol: 26 mM, • inhibited by Mn2+, al. (2011)
H2O2 : 1.2 mM Fe3+ Zn2+ and Hg2+
• Activated by Pandey and
Leucaena Guaiacol: 2.9 mM,
7 200 kDa 5.0 55°C Fully active at 65°C for 20 min Ca2+, Mn2+, Na+ Azide Dwivedi,
leucocephala H2O2: 5.6 mM
insensitive 2011
• Activated by Ni2+,
Eruca vesicaria Guaiacol: 375.74 mM Retained 50% activity at 80°C Co2+, Cu2+ Nadaroglu, et
8 34 kDa 6.0 40°C
sbsp. Sativa pyrogallol: 510.14 mM after 30 min incubation • Inhibited by Mn2+, al., (2013)
Hg2+, Zn2+, K+, Ca2+, Fe2+
• Activated by Cu2+,
Guaiacol: 8 mM Co2+, Mg2+, K+ and Ca2+ Mall et al.
9 Citrus medica 32 kDa 6.0 50°C o-dianisidine : 1.8 mM Stable at 60°C and 65°C
• Inhibited by Hg2+, (2013)
H2O2: 0.66 mM
Fe2+, Mn2+ and Zn2+
Fragaria
Complete loss of activity> 60°C Civello et al.
10 ananassa 56 kDa 6.0 30°C - -
within 5 min (1995)
Duch.
Guaiacol: 0.305 mM
Brassica Neutral and Neutral and Thongsook
(acidic), 8.789 mM Stable at 80°C activity after 1hr
11 oleracea Var. basic: 43 kDa basic : 6.0 - - and Barrett,
(basic), 0.711 mM incubation
Italica Acidic: 48 kDa Acidic: 4.0 (2005)
(neutral)
• Activated by Na+,
Zn2+, Mg2+, Ca2+ and
Mn2+
• tolerance towards
Guaiacol: 0.7 mM Retained 92% activity at 80°C Cd2+, Cs2+ and Ni2+ Pandey, et
12 Citrus limon 200 kDa 5.0 40°C
H2O2: 1.09 mM for 1 h • Retained 30- al., (2016)
50% activity in the
presence of 50%
ethanol, methanol and
isopropanol
Actinidia Guaiacol: 7.4 mM H2O2: Soda et al.,
29 kDa 5.5 50°C -
deliciosa 1.3 mM (1991)
Camellia Pyrogallol > ascorbate Kvaratskhelia
14 34.5 kDa 4.5 to 5.0 - - -
sinensis > guaiacol et al. (1997)
Solanum 45.8 kDa Bernards et
15 4.5 40°C -60°C - - -
tuberosum al. (1999)
Trachyca-rpus Inhibited by Na+, Ca++, Caramyshve
16 50 kDa 3.0 61−67°C - Moderate stable
fortunei and Mg++ et al., (2006)
Solanum Guaiacol: 6.5 mM Vernwal et al.
17 - 5.5 84°C - -
melongena H2O2 : 0.33 mM (2006)
POX I-
Guaiacol: 0.288 mM,
46.1 kDa o-dianisidine: 0.229
30°C (POX
Fagopyrum (POX I) and 8.0 (POX I) mM, Ascorbate: Suzuki et al.
18 I) and 10°C - -
esculentum 58.1 kDa 4.5 (POX II) 0.043 mM POX II- (2006)
(POX II)
(POX II). o-dianisidine: 0.137
mM, Ascorbate: 0.029
mM

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Citation: Pandey VP, Awasthi M, Singh S, Tiwari S, Dwivedi UN (2017) A Comprehensive Review on Function and Application of Plant Peroxidases.
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Page 8 of 16

• Activated by Al3+,
Gossyp-ium 39.1 and 64 Fe3+, Ca2+, and Ni2+ Kouakou et
19 5.0 and 6.0 25°C. - -
hirsutum kDa • Inhibited by Mn2+, al., (2009)
K+, Zn2+ and Hg2+
Retained 33%, 66% and 3.4%
o-dianisidine: 1.55-2.24 Yves et al.
20 Vigna species - - - activity at 70°C, 75°C and -
mM (2011)
80°C, for 1 h
Brassica Retained <10% activity after 5 Fortea, et al.,
21 - 4.0 - - -
oleracea min at 76.6°C (2012)
Luffa aegyptia- Guaiacol: 2.0 mM Yadav et al.,
22 - 6.5 60°C - -
ca H2O2: 0.2 mM (2011)
Table 1: Physicochemical properties of some purified plant peroxidases.

Applications of peroxidases over HRP for the biosensor manufacturing. The first SBP biosensor
was reported by Vreeke et al. [143] as a thermostable-wired enzyme
Peroxidases are important from the point of view of their industrial electrode. Spring cabbage peroxidase (SCP), has been reported to
applications by virtue of their ability to catalyze the oxidation- provide a good bioelectrocatalytic system due to its good affinity for
reduction reaction of a wide range of phenolic as well as non-phenolic various substrates, stability towards temperature and pH and ability to
substrates in the presence of hydrogen peroxide. A number of bind to polyanionic matrices and low costs of extraction and purification
industrial applications of peroxidases have been reported in the area [144]. Due to efficient bioelectrocatalysis of lignin peroxidases (LiP),
of agriculture, analytical, environmental, medical sectors etc. Thus, the LiP–graphite electrode biosensor systems have been developed for
peroxidases have been used in bioremediation of contaminating detection of recalcitrant aromatic compounds [145].
environmental pollutants such as phenols, delignification in paper
and pulp industry, diagnosis kit development, immunoassay, organic Application in analytical and diagnostic kits
and polymer synthesis as well as in and biosensor technology. They
are also used for developing convenient and quick methods for the Peroxidases are widely used in the development of analytical as
determination and quantification of hydrogen peroxide in both the well as diagnostic kits. Among peroxidases, horseradish peroxidases
biological and industrial samples [121,122]. Additional applications of are most commonly used for the analytical purposes [146]. However,
peroxidases include determination of extent of lipid peroxidation in other plant peroxidases having wide pH and temperature stability are
meat food products, in polymerization and precipitation of aqueous emerging as option for HRP. Since, the peroxidase has capability to
phenols as well as in decolorization of industrial effluents [123]. Some produce stable chromogenic products, thus, they are suitable candidate
of the important applications of peroxidases are described in detail in enzyme for the manufacturing of various diagnostic kits based on
following sections. enzyme conjugated antibody technology [147]. Uric acid detection kits
have been developed using turnip root peroxidases [148].
Application as biosensor
In combination with cholesterol oxidase and cholesterol esterase,
Biosensors have significance in medicine, quality control, food peroxidases have also been exploited for developing cholesterol
and environmental monitoring as well as in research. Enzyme based detection kits that help in quantification and monitoring of human
biosensors have advantageous over other analytical techniques with serum cholesterol [149,150]. Peroxidases have been used in developing
regards to high selectivity and high sensitivity. The performance of kits for the diagnosis of bladder and prostate cancers through the
these biosensors depends upon the amount and bioactivity of enzyme detection of 8-hydroxydeoxyguanosine and its analogs in urine [151].
immobilized onto the electrodes. Peroxidases have immense potential The monitoring of glucose for diabetes mellitus and of lactate in
and wide spread application as biosensors [123]. hypoxia and ischemia, are of great significance in patient management
Horse radish peroxidase has widely been used in development of [152] and it would be highly desirable to develop such a sensitive
biosensors [124-126]. HRP biosensors are made by applying various biosensor for the detection of H2O2, which would be stable at 37°C
detection methods including an amperometric immunosensor, mass and higher temperatures for sustained periods of time. Lactose content
balance, potentiometric methods, photovoltaic spectroscopy, optical monitoring strips have been developed using the combination of
and chemiluminescent methods etc. [127-132]. Potentiometric based immobilized β-galactosidase, galactose oxidase and HRP enzymes
biosensors are developed by combination of an enzyme (eg. peroxidase) [153]. In biomedical sectors, for cancer treatment gene-directed
and a transducer that can detect the variation in protons. Glucose, enzyme/prodrug therapy, (GDEPT) have been extensively and
maltose or lactate are reported to be detected by peroxidase based successfully used. Greco et al. [154] proposed a prompt and efficient
biosensor using potentiometric methods [133]. HRP-based biosensors peroxidase-IAA based GDEPT system for cancer treatment. This
for antioxidant monitoring have been applied in the detection of enzyme–prodrug system has been found to be effective against hypoxic
superoxide radical [134], nitric oxide [135], glutathione [134,136], uric and anoxic tumor cells and also has potential to be used in other
acid [137,138] and phenolic compounds [139-141]. Besides HRP, other anti-cancer strategies. Besides GDEPT, in antibody-directed enzyme/
plant peroxidases such as sweet potato, tobacco, peanut, soybean etc. prodrug therapy (ADEPT), specific HRP-conjugated antibodies are
have been also explored for their applications as biosensors. The sweet used [155,156]. Influenza virus was reported to detect using ultra-
potato peroxidase, due to its easy availability, high specific activity and sensitive colorimetric immunoassay with peroxidase-mimic of gold
superior electrochemical characteristics, is considered as advantageous
nanoparticles [157].
for application as biosensor [126]. A recombinant tobacco peroxidase
immobilized to graphite electrodes were reported to be advantageous Application in de-colorization of industrial dyes
for detection of aromatic phenols and amines [142].
Dyes are used extensively for paper printing, color photography
Soybean peroxidase (SBP) has been reported to be advantageous and as additive in petroleum products. These are synthetic aromatic

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Citation: Pandey VP, Awasthi M, Singh S, Tiwari S, Dwivedi UN (2017) A Comprehensive Review on Function and Application of Plant Peroxidases.
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Page 9 of 16

compounds having complex structures, biologically un-degradable potential of peroxidase for soil and water detoxification constitute a
and causing environmental problems. For the degradation of theses possible basis for the development of bioremediation technologies.
synthetic industrial dyes, the currently available methods such as
chemical oxidation, reverse osmosis, and adsorption, are highly efficient, Application in pulp and paper industry
but they suffer with some disadvantages. Now- a-days the interest is Lignin, a phenolic heteropolymer, shows negative impact on the
towards the use of microbial degradation of dyes, because this process is proper exploitation of plant biomass for the pulp and paper industry.
less expensive and ecofriendly alternative [158]. Enzymes such as lignin Thus, the lignin should be removed prior to the production of good
peroxidases (LiPs) and manganese peroxidases (MnPs), are involved in quality paper. The chemical delignification leads to production of
the decolorization of synthetic azo dyes such as orange II, and others various pollutants. Thus, the enzymatic degradation of lignin is
[159]. Horseradish peroxidase (HRP) is reported to degrade phenol and suggested as a better alternative. Lignin peroxidase (LiP) and manganese
substituted phenols via a free radical polymerization mechanism and peroxidase (MnP) are successfully used for biopulping, biobleaching
can be effective in degrading and precipitating industrially important as well as selective delignification in the paper industry and selective
azo dyes, such as Remazol [160,161]. The properties of white-rot fungi delignification helps in the production of cellulosic materials that can
to oxidize various recalcitrant xenobiotics released to the environment be used as efficient feed and biofuel [188,189].
are thought to result from the activities of LiP, MnP, and laccases
[162]. A purified peroxidase produced by Geotrichum candidum dec Hair dyeing
1, was involved in decolorization of dyes [163]. Pandey et al. [164,165] Traditionally the hair coloring dyes are synthesized via oxidative
have also reported that the purified lemon peroxidase was found to polymerization of dye precursors (phenols or aminophenols, and
be oxidized the industrial dyes in the order of aniline blue>methyl couplers). For this process, the hydrogen peroxide (3%) is used that
orange>indigo carmine >trypan blue>crystal violet. initiates the polymerization reaction but it bleaches the natural
The textile industry, being one of the traditional industrial hair pigment melanin. These concentrations of H2O2, when applied
segments, consume large quantities of water, chemical products and repeatedly, can cause hair damage. To achieve a gentler dyeing with
synthetic dyes and generate large volumes of wastewater that contain milder oxidation process, the enzymes such as oxidases, peroxidases
a high organic load that are responsible for acute or chronic toxicity etc. have been proposed as better options [190].
on the ecosystems. Thus, the wastewater from textile industries is
Analytical applications
considered as one of the most polluting among all industrial wastes,
thereby requiring appropriate treatment technologies. Peroxidases Enzyme Linked Immunosorbent Assays (ELISA) has advantages
have been shown to have great potential in the decolorization process over other immunoassays in simplicity, low cost, reliability, simple
to decrease textile industry pollutant residues [166,167]. Uses of equipment requirement etc. ELISA is usually developed to detect
peroxidases, such as horseradish, Brassica campestres turnip, tomato, antigens or antibodies by producing an enzyme such as peroxidase
bitter gourd, soybean, Ipomea palmata and Saccharum spontaneum catalyzed color changes. In these assays an enzyme-linked antibody
peroxidases, for degrading and detoxifying polyaromatic hydrocarbons, specific to the antigen is required along with a chromogenic substrate,
polychlorinated biphenyls, and other synthetic industrial dyes have which give colored product in the presence of the enzyme and the
been reported [168-178]. color of the product is proportional to the amount antigen/antibody
of interest. For such type of assays HRPs are the most commonly
Application in bioremediation of phenolic compounds used enzymes as linked with antibody. They are used to screen the
Aromatic compounds such as phenols and its derivatives are a monoclonal antibodies against dangerous mycotoxins of various
major class of pollutants in wastewater from a number of food and fungal species like Aspergillus, Penicillium (ochratoxins), Fusarium
chemical industries [179]. Phenols are known to be toxic and also (T-2 toxin, trichothecenes) etc [191-193]. A large number of reports
hazardous carcinogens that can accumulate in the food chain. Being regarding the development of enzyme immunoassays using peroxidase
highly toxic their discharge into the environment should be highly as reporter enzyme to detect toxins, pathogens, and other analyses are
regulated [180]. The polymerization using redox enzymes is one of the available. For example, in detection of Goynyautoxins, Chlamydia,
phenol removal methods. The enzyme treatment offers a high degree Fusarium toxin, Dengue virus proteins, Hepatitis-E virus peroxidases
of specificity, operation under mild conditions and high reaction are used [194-199]. HRP-based immunoassays for the detection of
velocity [180] concomitant with an ecofriendly approach. The ability undeclared milk proteins (eg. bovine b-lactoglobulin) in foods has also
of peroxidases to catalyze the formation of free-radical from various been developed [200].
aromatic pollutants and their polymerization can be potentially
exploited in bioremediation and wastewater treatment. Thus, The DNA detection using complementary DNA probes is of
peroxidases have been reported for removal of phenolic compounds significance in diagnostics and research. The non-radioactive DNA
from synthetic model effluents and also from real industrial effluents probes associated with peroxidases, such as HRP have become safer than
[160,161,181-183]. There are a number of reports in literature on radioactive probes [201]. Peroxidases have been reported to become
detoxification of wastewater contaminated with phenols, cresols, and suitable for microarray analyses because it catalyses a large number of
chlorinated phenols using HRP. Using HRP, Bewtra et al. [184] have electron-transfer reactions with natural and synthetic substrates. It can
determined the optimum pH for removal of 2, 4-dichlorophenol as be used either directly immobilized on the microarray [202], or as a
6.5. The removal efficiency is also affected by the hydrogen peroxide labeling agent for nucleic acids, antibodies and other proteins [203,204].
concentration. Soybean and turnip peroxidases have also been shown The HRP-based or associated microarrays (biochips) have been used in
to have good potential for removal of phenolics compounds [185,171]. various applications such as expression analysis, recombination and
Additives, such as PEG or gelatin, usually improve removal efficiency gene mapping, mutation analysis etc [205,206].
by protecting the enzyme [186]. The addition of PEG-3350 or PEG-
8000 to soybean peroxidase, increased the removal efficiency of 2, Application in organic polymer synthesis and grafting
4-dichlorophenol by a factor of 10 or 50, respectively [187]. Thus, the The importance of heme peroxidases in polymer chemistry is

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Page 10 of 16

based on their ability to oxidize a variety of phenolic molecules thereby The chemical synthesis of conducting polymers such as polyaniline,
generating reactive species (phenoxy radicals) which provide ideal sites the most extensively studied conducting polymers having high
for cross-linking (coupling) leading to polymerization reactions. The environmental stability and promising electronic application including
grafting application of peroxidase is one of the important industrial electronic equipment, photovoltaic cells, plastic batteries, polymer
applications of heme peroxidases. The free radicals generated from light-emitting diodes, and optical displays, is not eco-friendly, thus
the reactions catalyzed by peroxidases, can induce formation of HRP have been tried as an alternative for the synthesis [227-234]. But
other new functional polymers such as phenolic resins [207,208]. The due to low activity of HRP towards the synthesis of Polyaniline, the
broad spectrum of peroxidase applications in organic synthesis is due other anionic peroxidase purified from soybean, african oil palm tree is
to their ability to catalyze different types of reactions as 1) oxidative developed as better substitute of HRP [235].
dehydrogenations (2RH + H2O2 → 2R° + 2 H2O), 2) oxygen transfer
Peroxidase catalyzed polymerization of substituted and un-
reactions (R + H2O2 → RO + H2O), 3) oxidative halogenations (RH +
substituted phenols and anilines have also been reported as better
H2O2 + HX → RX + 2H2O) and 4) H2O2 dismutation (2 H2O2 → 2H2O +
and striking alternative to the conventional chemical (formaldehyde)
O2) [209,210]. The peroxidases have been used in the development of
polymerization method [236-238]. Peroxidases also catalyze the stereo-
hybrid resins from renewable sources to replace phenol–formaldehyde
specific oxygen transfer reactions such as heteroatom oxidations,
based resins that are widely used in surface coatings, adhesives,
oxidation of C-H bonds in allylic/benzylic compounds, alcohols and
laminates, molding, friction materials, abrasives, flame retardants,
indoles that yield various synthetic compounds of significance [210].
carbon membranes, glass fiber laminates, fiberboards, and protein-
The plant peroxidases have also been shown to have application in
based wood adhesives etc [211].
the synthesis of α- 3’, 4’-anhydrovinblastine, by the coupling reaction
Blinkovsky and Dordick [212] have demonstrated the HRP of catharanthine and vindoline. The α-3’, 4’-anhydrovinblastine is a
mediated polymerization of phenolics and incorporation of phenols metabolic precursor of vinblastine and vincristine which are used in
into lignin leading to the formation of polymers of great potential cancer chemotherapy [238,239,240].
as phenolic resins [213]. For example, enzymatically synthesized
poly (p-phenylphenol) and poly (p-cresol) were reported to have Conclusion
high melting points, whereas, the poly (p-phenyl-phenol) exhibited Peroxidases catalyze oxidation of a wide range of phenolic as well
higher electrical conductivity than that of phenol-formaldehyde as non-phenolic compounds. Plant peroxidases, belonging to class
based resins. The incorporation of cresol into lignin by peroxidase III peroxidases, have been implicated in various plant growth and
provides a platform for using lignin as a raw material for grafting developmental processes such as cell wall metabolism, fruit growth
molecules to obtain new functional polymers [214]. Thus, the ability and ripening, metabolism of reactive oxygen species (ROS), defense
of peroxidases to modify lignin and develop new functional polymers against pathogens etc. In view of the wide applications of peroxidases
with excellent properties leads to the progress in lignin applications in key areas such as clinical biochemistry, immunology, biotechnology,
such as in development of polymer adhesives, biodegradable plastics, environment and industry, they are considered as one of the important
polyurethane copolymers, paints, dispersants in dyes, in pesticides, and industrial enzyme. Thus, peroxidases have been used in bioremediation
printed circuit boards [207,215-217]. Using Soybean peroxidase (SBP), of contaminating environmental pollutants such as phenolic
Ikeda et al. [218] successfully developed polyphenol resins without compounds, delignification in paper and pulp industry, diagnosis kit
involvement of formaldehyde, which exhibited better properties than development, immunoassay, organic and polymer synthesis as well as
that of conventionally polymerized resins. in ELISA and biosensor technology. Furthermore, with the potentials
Kim et al. [219] have used SBP to catalyze the oxidative of nano-based biosensor applications, in recent years, peroxidases have
polymerization of cardanol to polycardanol. Cardanol is an excellent gained more prominence. The use of immobilized enzymes, in various
raw material for the preparation of high grade insulating varnishes, industrial processes, is one of the advancement in their application.
paints, enamels, laminating resins, and rubber. Thus, the cardanol- For all such applications of peroxidases there is a need for search of
based resins show resistance towards softening action of mineral oils, novel peroxidases offering tolerance towards the factors / ingredients
acids and alkaline conditions, termite, and insects and have coefficient of the reaction environment such as temperature, pH, salts, metals and
of friction less sensitive to temperature changes than phenol– organic solvents etc.
formaldehyde based resins. Acknowledgements
The free radical polymerization of methyl methacrylate (MMA) Financial assistances from Department of Biotechnology (DBT), New Delhi
catalyzed by peroxidase (such as HRP) was developed by Karla and under Bioinformatics Infrastructure Facility; Department of Higher Education,
Gross [220]. Poly (methyl methacrylate) (PMMA) is a colorless Government of U.P., Lucknow under Centre of Excellence Grant and Department of
Science and Technology, New Delhi under Promotion of University Research and
polymer used extensively for the production of scratch resistance Scientific Excellence (DST-PURSE) programme for infrastructure development are
optical products, plastics, and PVCs. In addition, peroxidase mediated gratefully acknowledged.
polymerization of acrylamide in to poly-acrylamide with good thermal
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Citation: Pandey VP, Awasthi M, Singh S, Tiwari S, Dwivedi UN (2017) A Comprehensive Review on Function and Application of Plant Peroxidases.
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Citation: Pandey VP, Awasthi M, Singh S, Tiwari S, Dwivedi UN (2017) A Comprehensive Review on Function and Application of Plant Peroxidases.
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