Non-Invited Review

Antioxidant, angiotensin-converting enzyme inhibitory activity and other

functional properties of egg white proteins and their derived peptides – A
review

E. D. N. S. Abeyrathne,∗ X. Huang,†,‡,1 and D. U. Ahn‡

∗
Department of Animal Science, Uva Wellassa University, Badulla 90000, Sri Lanka; † College of Food Science &
Technology, Huazhong Agricultural University, Egg Processing Technology Local Joint National Engineering
Research Center, National R&D Center for Egg Processing, Wuhan, Hubei 430070, China; and ‡ Department of
Animal Science, Iowa State University, Ames, IA 50010, USA

ABSTRACT Egg white contains many functionally
important proteins: ovalbumin (54%), ovotransferrin
(12%), ovomucoid (11%), ovoglobulin (G2 and G3, 8%),
ovomucin (3.5%), and lysozyme (3.5%) are major pro-
teins, while ovoinhibitors, ovomacroglobulin, ovogly-
coprotein, ovoflavoprotein, thiamine-binding proteins,
and avidin are minor proteins present in egg white.
These proteins, as well as the peptides derived from the
proteins, have been recognized for their functional im-
portance as antioxidant, antimicrobial, metal-chelating,
anti-viral, anti-tumour, and angiotensin-converting en-
zyme (ACE)-inhibitory activities. Among the func-
tional properties of the peptides, antioxidant and an-
timicrobial activities are important characteristics for
Key words: egg white proteins, functional peptides, antioxidant, angiotensin-converting enzyme inhibitory
activity
food processing while other properties such as ACE-
inhibitory activity of the peptides can have important
health-related functionalities. Bioactive peptides can
be produced from egg white proteins by enzyme hy-
drolysis, chemical treatments, or thermal treatments at
different pH conditions. The effective functional pep-
tides produced from egg white proteins are usually
smaller than 2 kDa in molecular size. However, these
peptides are known for their beneficial activities in
vitro only, and little work has been done to prove
their beneficial effects in vivo. Therefore, further stud-
ies are needed to see if the bioactive peptides derived
from egg white proteins are helpful for humans in the
future.
2018 Poultry Science 97:1462–1468
http://dx.doi.org/10.3382/ps/pex399

INTRODUCTION Among these functional properties, antioxidant ca-

Chicken egg consists of three main components, in-
cluding egg white (56%), yolk (33%), and shell (11%).
Egg white is the major component of egg and con-
sists of 88% water and 12% solids, of which over
90% is protein. Ovalbumin, ovotransferrin, and ovo-
mucoid are considered as the major, while ovomucin,
lysozyme, ovoglobulins, ovoinhibitors, ovomacroglobu-
lin, ovoglycoprotein, ovoflavoprotein, thiamine-binding
proteins, ficin/papain inhibitor, avidin, and cystatin
are the minor egg white proteins. These proteins,
as well as their peptides, have been recognized
for their functional importance as antioxidants, an-
timicrobials, metal-chelators, anti-viral, anti-tumor,
and angiotensin-converting enzyme (ACE)-inhibitory
activities.

C 2017 Poultry Science Association Inc.
Received April 27, 2017.
Accepted November 27, 2017.
1
Corresponding author: huangxi@mail.hzau.edu.cn
pacity is an important characteristic for food process-
ing. The production of reactive oxygen species (ROS)
and free radicals is an essential part of the biological
processes that are involved in energy production in all
living organisms. However, the ROS can also enter our
body through the ingestion of foods and from the en-
vironment. Oxidative damage by free radicals may be
related to aging and diseases such as atherosclerosis, di-
abetes, cancer, and cirrhosis. In particular, lipid oxida-
tion in foods is a serious problem for the food industry
because it produces off-flavor, off-odor, discoloration,
and potentially toxic reaction products. Synthetic an-
tioxidants such as butylated hydroxyanisole, and buty-
lated hydroxytoluene are added to food products to re-
tard lipid oxidation. Over the past few decades, how-
ever, the demand for natural antioxidants has increased
dramatically because of the negative consumer percep-
tions and the long-term safety concerns about synthetic
antioxidants. Many natural antioxidants have been iso-
lated from plant sources to replace the synthetic ones to

1462
 EGG WHITE PROTEINS AND ANTIOXIDANT PEPTIDES
improve the flavor and quality of food products, and to
extend the shelf life of foods (Abeyrathne et al., 2014).
Replacing artificial antioxidants with natural antioxi-
dant peptides will be beneficial in the food industry be-
cause they not only control the lipid oxidation in foods
but also supply additional essential amino acids to the
consumers.
Besides antioxidant activity, ACE-inhibitory activity
is another functional property that has been studied
extensively, because high blood pressure has been con-
sidered as a well-defined risk factor for cardiovascular
diseases. As a multifunctional enzyme, ACE is involved
in several systems that are related to the blood pres-
sure through the inactivation of the vasodepressor agent
“Bradykinin” and the generation of the vasopressor
agent angiotensin II. The separation and preparation of
various ACE-inhibitory proteins and peptides from ani-
mal and vegetable sources have been reported. Peptides
are demonstrated to possess higher ACE-inhibitory ac-
tivity than the proteins in vitro (Chen et al., 2012) and
in vivo in hypertensive animals and humans (Mizuno
et al., 2005). Interestingly, it is found that the cardiovas-
cular diseases may also be related to the oxidative stress
in cells caused by excessive production of free radicals
(You et al., 2010). The aim of this article is to review the
research progress of functional proteins and peptides
from egg white on antioxidant, ACE inhibitory activity.
Functional Properties of Egg White Proteins
Ovalbumin, as a major protein in egg white (54%),
demonstrated remarkable antioxidant activity after
binding covalently with galactomannan or dextran by
a controlled Maillard reaction. A Celite powder sys-
tem containing methyllinoleate was used as a simu-
lated dried food model to evaluate lipid oxidation by
measuring peroxide value and thiobarbituric acid val-
ues. The results indicated that the antioxidation activ-
ity of ovalbumin-polysaccharide conjugates were 1.4 to
1.9 times and 1.8 to 2.4 times their mixture by mea-
suring the peroxide value and thiobarbituric acid val-
ues, respectively. (Nakamura et al., 1992). Similarly, the
free-radical scavenging activity, hydroxyl-radical scav-
enging activity and reducing power of selenized oval-
bumin revealed that the antioxidant activity of ovalbu-
min was improved when selenite was conjugated. The
enhanced antioxidant activity of selenized ovalbumin is
ascribed to the conjugated Se and the formation of a
molten globule conformation of protein (Li et al., 2014).
The improvement of antioxidant activity has also been
observed when ovalbumin was combined with buck-
wheat polyphenol rutin (Awatsuhara et al., 2010).
Ovotransferrin (OTf), which accounts for 12% of the
total egg white protein, is known as an iron binder
and transporter in animals, and thus can be used as
an iron supplementing, antimicrobial, or antioxidant
agent. Japanese researchers found that ovotransfer-
rin generates observable thiol-linked self-cleavage in a
1463
redox-dependent process (Ibrahim et al., 2013). OTf
is a superoxide dismutase (SOD)-mimicking protein
r
with a potent superoxide anion (O2 − )-scavenging ac-
tivity and showed dramatically higher scavenging ac-
tivity than some known antioxidants, such as serum al-
bumin or ascorbate. Interestingly, metal-bound OTfs
2+
such as Fe r−
-OTf, Mn2+ -OTf, Cu2+ -OTf exhibited
greater O2 dismutation capacity than the apoprotein
(Ibrahim et al., 2007). Conjugation of OTf with small
molecules such as catechin shows improved antioxidant
activity (You et al., 2014). The research in our labora-
tory found OTf showed certain antioxidant effects dur-
ing in vitro experiments, and its hydrolysates showed
approximately 3.2 to 13.5 times higher superoxide an-
ion scavenging activity and better copper/calcium-
solubililizing activity than OTf (Kim et al., 2012).
Furthermore, autocleaved OTf showed the higher an-
tioxidant activity than the natural OTf, and the hy-
drolysates of autocleaved OTf showed stronger antioxi-
dant activity than those of the autocleaved one (Moon
et al., 2015).
Ovomucoid, which accounts for 11% of total egg
white proteins, is well known as a “trypsin inhibitor”
and is considered as the main food allergen present in
egg (Abeyrathne et al., 2014). It is one of the highly
glycosylated proteins that contains 20 to 25% carbohy-
drates (Nolan, Phillips and Mine, 2005). It has a molec-
ular weight of 28 kDa with an iso-electric point of 4.1,
but it appears in a range between 45 and 50 kDa in
SDS-PAGE. This protein consists of 186 amino acids
that are arranged in three tandem domains (Oliveria et
al., 2009). This protein contains three disulfide bonds,
two tyrosine residues, and one active site (Salahuddin
and Baig, 1985). It is defined as a single headed in-
hibitor of trypsin, meaning each ovomucoid molecule
binds 1:1 with trypsin, and its three-dimensional struc-
ture is secured with the 3 disulfide bonds in it (Oliveria
et al., 2009).
Ovomucin accounts for 2 to 4% of the total egg white
protein (Stadelman and Cotterill, 2001) and is respon-
sible for the gel-like structure in egg white. It consists
of two subunits with a wide range of molecular weight
(220 to 270 kDa) and very high levels of glycosylation
(Omana, Wang and Wu, 2010a). Ovomucin mainly con-
sists of two types of subunits, which are called α and
β . α-Ovomucin is homogeneous whereas β -ovomucin is
heterogeneous in structure. Furthermore, the α-subunit
has two subunits, called α1 and α2, which have fewer
carbohydrate groups than β -ovomucin (Hiidenvoi et al.,
1999). Earlier research of ovomucin was mainly focused
on its effect in the thinning of egg white. Recently,
however, ovomucin was found to possess a variety of
bioactivities such as antibacterial, antiviral, and anti-
tumor activities, and the suppression of cholesterol ab-
sorption (Omana, Wang and Wu, 2010b; Shan, Xu and
Ma, 2014; Nagaoka et al., 2002). Heating ovomucin un-
der alkaline conditions produced many peptides that
have ACE-inhibitory, metal chelating, and antioxidant
activities (Abeyrathne et al., 2016).
1464 ABEYRATHNE ET AL.
Lysozyme is another important protein found in egg
white (3.5% of total egg white proteins) (Ibrahim et al.,
2007). There are many forms of lysozyme found in na-
ture, but the one found in egg is considered as the most
soluble and stable (Benkerroum, 2008). It is a ubiqui-
tous enzyme that can hydrolyze the β -linkage between
N-acetylneuraminic acid and N-acetylglucosamine in
bacterial cell walls. Lysozyme is known for its antibac-
terial property, especially against Gram-positive bac-
teria (Huopalahti et al., 2007). It was found that the
modification of lysozyme exhibited an increased effect
against Gram-negative bacteria such as Pseudomonas
fluorescens compared with natural lysozyme (lysozyme
monomer) (Cegielska-Radziejewska et al., 2009, 2010).
Derde et al. (2013) found that lysozyme rapidly in-
creased the permeability of the outer membrane of Es-
cherichia coli by forming large size pores, which may be
the possible mechanism for its anti-bacterial activity.
In addition to the major proteins in egg white, many
other proteins, including ovoglobulin, ovoinhibitors,
ovomacroglobulin, ovoglycoprotein, ovoflavoprotein,
thiamine-binding proteins, avidin, and ficin/papain in-
hibitor have been identified as functional proteins
(Stadelman and Cotterill, 2001). These proteins, as well
as their peptides, are known to have antioxidant, an-
timicrobial, or anti-enzymatic properties. Among them,
flavoprotein is known as a riboflavin-binding protein
with a single polypeptide chain (Hamazune et al.,
1984). Flavoprotein is composed of 219 amino acids
with several α- and β -helices. Among the helices, 4 α-
helix (A-D) and 4 β -helix make the riboflavin bind-
ing sites. Avidin is an alkaline protein composed of
128 amino acids with the molecular weight of 14.3 kDa
(Stadelman and Cotterill, 2001). Even though the bi-
ological function of avidin is not well understood, it
strongly binds biotin and acts as an antimicrobial agent
(Huopalahti et al., 2007).
There are several proteases found in egg white, but
the identification of these proteins is difficult because
of the presence of numerous anti-proteases (Rawlings
et al., 2006). Two of the proteases identified in egg
white are glutamyl aminopeptidase and aminopeptidase
with a broad specificity (Huopalahti et al., 2007). Sev-
eral proteins in egg white are characterized as “anti-
proteases”. Among them ovostatin, ovoinhibitors, and
cystatin are considered important. Ovostatin is a α2-
macroglobulin with a very high molecular weight with
an isoelectric point of 4.9 (Nagase and Harris, 1983) and
is known to have numerous biological properties includ-
ing anti-bacterial and anti-inflammatory properties and
can be used to treat keratitis (Geng et al., 2013). Ovoin-
hibitors are multiple anti-protease proteins present in
egg white. They are glycoproteins and are heat stable
and inhibit the serine proteases such as trypsin and
chymotrypsin (Huopalahti et al., 2007). Cystatin has
a molecular weight of 13 kDa with two major isoelec-
tric forms differ in the occurrence of phosphorylation
on serine (Huopalahti et al., 2007). These two forms of
cystatin show two different isoelectric point values at
6.5 and 5.6, respectively, depending upon whether it is
non-phosphorylated or phosphorylated (Anastasi et al.,
1983). Cystatin inhibits most of the cysteine proteases,
including papain and fucin (Huopalahti et al., 2007).
Production of Functional Peptides from Egg
White Proteins
Elias et al. (2008) demonstrated that the antioxi-
dant activity of proteins is due to the complex inter-
actions with lipids, oxidation catalysts, and free radi-
cals in food systems. Proteins are somewhat different
from other food antioxidants because they have multi-
ple functions that inhibit various oxidation pathways.
Both proteins and peptides derived from egg are well
known for anti-microbial ant-cancer, metal binding, and
ACE-inhibitory activity properties.
The egg white or the single protein has been used
to produce bioactive peptides. Until recently, however,
most of the functional peptides were produced from
milk and soybean proteins. Peptides produced from
ovalbumin were strongly active agents against Bacil-
lus subtilis but lesser active agents against E. coli,
Candida albicans, and Pseudomonas aeruginosa (Pel-
legrini et al., 2004). Also highly glycosylated ovomucin
peptides are active against one of the most problem-
atic foodborne pathogens E. coli O157:H7 (Kobayashi
et al., 2004). The glycopeptides derived from ovomucin
by pronase digestion showed good antitumor activity
against double-grafted tumors in mice (Watanabe et al.,
1998).
The production of bioactive peptides from egg
proteins was mainly performed using enzyme or heat
treatment. Hydrolysing egg white proteins improves
their functional properties such as antioxidant, antimi-
crobial, metal-binding, and ACE-inhibitory activities
(Moure et al., 2006; Abeyrathne et al., 2015). Chiang
et al. (2006) reported that the peptides produced
from egg white proteins using thermolysin showed
ACE-inhibitory activity in strain spontaneously hyper-
tensive rats. Ding et al. (2014) further demonstrated
that the ACE-inhibitory peptides of egg white have a
cytoprotective effect and could be transported to hu-
man intestinal Caco-2 cell monolayers. Lin et al. (2013)
found that the hydrolysates produced from egg white
proteins using different enzymes (pepsin, alcalase, and
trypsin) showed strong antioxidant activity. Among
the peptides produced, alcalase hydrolysates showed
the highest antioxidant activity, and the fractions
with a strong antioxidant activity had molecular size
smaller than 1 kDa. Chen and Chi (2012) reported
that hydrolysis of egg white proteins with papain
produced two dominant peptides with the amino acid
sequence of Tyr-Leu-Gly-Ala-Lys and Gly-Gly-Leu-
Glu-Pro-Ile-Asn-Phe-Gln, which had strong antioxi-
dant activity in DPPH radical scavenging and lipid
peroxidation inhibition assays. Dávalos et al. (2004)
reported that strong antioxidant peptides with amino
 EGG WHITE PROTEINS AND ANTIOXIDANT PEPTIDES
acid sequences of Tyr-Ala-Glu-Glu-Arg-Tyr-Pro-
Ile, Tyr-Arg-Gly-Gly-Leu-Glu-Pro-Ile-Asn-Phe, and
Tyr-Gln-Ile-Gly-Leu were produced by hydrolysing
egg white proteins with papain. Their antioxidation
was proved by oxygen radical absorbance capacity-
fluorescein (ORAC-FL) assay in vitro. Manso et al.
(2008) also produced peptides with strong antioxidant
activity from egg white proteins using pepsin. These
peptides were effective in preventing or reversing the
abnormalities associated with metabolic syndromes
and their complications such as hypertension, oxida-
tive stress, and hyperlipidemia in hypertensive rats.
Similarly, the hydrolysis of egg white protein powder
with alcalase produced a peptide (His-Cys-Tyr-Tyr-
Phe-Met) with a strong antioxidant activity (2011).
Liu et al. (2015) identified three new peptides with
molecular weights of 628.64, 630.71, and 684.1 Da
from the hydrolysates of egg white proteins. They
found that these peptides had amino acid sequences of
Asp-His-Thr-Glu, Phe-Phe-Glu-Phe-His and Met-Pro-
Ala-His-Leu, and had strong oxygen radical absorbance
capacities. Among the peptides derived from egg white
proteins, the ones with amino acid sequences of
Tyr-Arg-Glu-Glu-Arg-Tyr-Pro-Ile-Leu, Arg-Ala-Asp-
His-Pro-Phe-Ley and Ile-Val-Phe showed positive
actions on hypersensitive rats (Miguel et al., 2004). Yu
et al. (2012) reported that 11 peptides derived from egg
white using alcalase had ACE-inhibitory, antioxidant,
and anticoagulation activities. All 11 bioactive peptides
contained Thr-Asn-Gly-Ile-Arg in their amino acid
sequences, and the primary and secondary structures
of the peptides showed strong ACE-inhibitory activity.
Individual egg white proteins have also been used
to produce functional peptides. Among the egg white
protein OTf, ovalbumin, ovomucin, ovomucoid, and
lysozyme were widely used to produce bioactive pep-
tides. Manso et al. (2008) reported that the peptides
derived from ovalbumin showed a strong inhibitory ac-
tivity against ROS. They reported that oral intake of
these peptides for a short period reduced the blood
pressure in spontaneously hypertensive rats. Free rad-
icals, including ROS, caused lipid oxidation as well as
protein and DNA oxidation. Ibrahim and Kiyono (2009)
demonstrated that OTf auto-cleaved under reducing
conditions exhibited stronger SOD-like activity and an-
ticancer effects against human colon and breast can-
cer cells than the natural OTf. Also, the auto-cleaved
OTf showed stronger Cu2+ - and Ca2+ -binding capac-
ities than the natural OTf (Moon et al., 2015). The
hydrolysis of OTf with the combination of thermolysin,
and pepsin produced 14 peptides with strong antioxi-
dant activity, and the majority of the peptides identified
had high ORAC values. However, peptides with amino
acid sequences of LSKAQSDFG and LVEKGDVAFI
showed pro-oxidant activity (Shen et al., 2010). Kim
et al. (2012) reported that OTf possessed an antiox-
idant effect in a different system, but hydrolysis of
OTf with acid or enzymes improved these abilities.
Also, they found that OTf and its enzyme hydrolysates
1465
showed protective effects against the oxidative stress-
induced DNA damage in human leukocytes.
Lysozyme is considered as one of the most impor-
tant proteins isolated and industrialized from egg white
(Elias et al., 2008). Both lysozyme and its hydrolysates
have been recognized as multifunctional fractions. Pep-
tides derived from egg white lysozyme ROS generation
and protected against acute and chronic oxidant inci-
dence (Liu et al., 2006). It is reported that lysozyme
and the peptides produced by hydrolyzing lysozyme
with 0.5% w/w alcalase at 95◦ C for 10 min showed
significantly higher ORAC-FL activity, which was as
high as that of the synthetic antioxidants like BHA
and BHT in foods (You et al., 2010). Memarpoor-
Yazdi et al. (2012) fractionated a trypsin + papain hy-
drolysate of lysozyme and identified a peptide with the
amino acid sequence of NTDGSTDYGILQINSR (MW:
1,753.98 ± 0.5 Da), which has very high antioxidant
activity. That fraction also had inhibitory effects on
both Gram-negative and Gram-positive bacteria. The
minimal inhibitory concentration values of the peptide
against E. coli and Leuconostoc mesenteroides bacteria
were 355.64 (±2.2) and 442.25 (±2.8) μg/mL, respec-
tively. Another research study demonstrated that the in
vitro digestion product (LPH2) of egg white lysozyme
was found to have potent ACE-inhibitory and antioxi-
dant activities in vitro. Of the fragments in the LPH,
KVF, MKR, AMK, AKF, RGY, WIR, VAW, and GIL
showed great ACE-inhibitory activity. Furthermore, the
peptides RGY, WIR, and VAW showed strong antioxi-
dant activity (Rao et al., 2012).
Recently, a few of the major egg white proteins
(ovalbumin, ovomucoid, and ovomucin) have been
hydrolyzed using combinations of enzymes (trypsin,
pepsin, chymotrypsin, papain, and alcalase) under 37◦ C
to produce bioactive peptides (Abeyrathne, Lee and
Ahn, 2014; Abeyrathne et al., 2015; Abeyrathne et al.,
2016). The combination of pepsin, papain, and alcalase
treatments of those proteins produced peptides with
high antioxidant activity. Among them, ovalbumin hy-
drolyzed with alcalase + trypsin (OAArTr) and pro-
tease + chymotrypsin (OAC), ovomucoid hydrolyzed
with alcalase + trypsin (OMAlTr), and ovomucin dis-
solved at pH 12.0 and heated for 15 min at 100◦ C (OM)
produced peptides with the highest antioxidant activ-
ity. The LC-nano ESI-MS/MS analysis identified sev-
eral tens to hundreds of peptides from each of the hy-
drolysates, and the majority of the peptides had molec-
ular weight <2 kDa (Table 1). The results showed that
the hydrolysates with small peptides showed stronger
functional activity than those with larger peptides,
but purification of individual peptides with a spe-
cific function from the hydrolysates seems not possi-
ble or maybe meaningless. Also, recently Nimalaratne
et al. (2015) produced 16 antioxidant peptides from
ovalbumin, OTf, and cystatin using different proteases
and alcalase, and found that two peptides with the
amino acid sequences of ALs-Glu-Glu-Arg-Tyr-Pro and
Asp-Glu-Asp-Thr-Gln-Ala-Met-Pro showed the highest
1466 ABEYRATHNE ET AL.
Table 1. Effects of enzyme treatment on the size and number of peptides of OAPrTr (ovalbumin treated
with protease and trypsin under ambient conditions), OAC (ovalbumin treated under α-chymotrypsin un-
der optimum conditions), OMAlTr (ovomucoid hydrolysed using alcalase and trypsin under optimum con-
ditions), and OM (ovomucin heat at 100◦ C for 15 minutes) (Abeyrathne et al., 2014; Abeyrathne et al.,
2015; Abeyrathne et al., 2016).
MW of peptides (Da) OAArTr
< 700 10
700 to 1,000 28
1,000 to 1,500 52
1,500 to 2,000 47
2,000 to 3,000 23
3,000 to 5,000 21
Total (Prot. Scores) 181 (64.93)
ORAC. The hydrolyzed peptides from separated ovo-
mucoid showed strong biologically important proper-
ties, including antioxidant, metal-chelating, and ACE-
inhibitory activities (Abeyrathne et al., 2015).
Fertilized chicken eggs and unfertilized duck eggs
were also used to produce functional peptides. Duan
et al. (2014) produced many peptides with antioxi-
dant activity from the fertilized eggs: a peptide with
HLFGPPGKKDPV (MW 1291.51 Da) was identified
in a 15-day-incubated egg and found to have a strong
antioxidant activity. The hydrolysis of duck eggs with
SEEP-Alcalase (HSA21 ) produced 5 oligopeptides with
the molecular weights of 202.1, 294.1, 382.1, 426.3, and
514.4 Da, (Ren et al., 2014). These peptides showed sta-
ble antioxidant activity after in vtiro digestive simula-
tion. The antioxidant activity of the peptides showed a
close relationship with their sizes. Most of the peptides
with a strong antioxidant capacity contained either one
or few of the amino acids, including Cys, Met, Trp, Tyr,
Phe, and His in their peptide sequences. Thus these
amino acids were called as antioxidant amino acids be-
cause they increased the antioxidant activity of the pep-
tides (Elias et al., 2008).
Strategies for the Practical Application of
the Functional Peptides from Egg Proteins
Functional food is an emerging area in the food indus-
try. Functional food sales topped $55.1 billion in 2015,
up 7.7%, and are projected to reach $63.3 billion by
2017 (NBJ, 2016). The derived egg peptides have mul-
tiple functional properties, giving them strong poten-
tial to be used as natural antioxidant, antimicrobial, or
metal-chelating agents because the peptides have multi-
functional properties. The functional peptides from egg
proteins can replace synthetic antioxidants, and there is
no upper limit to the addition of the functional peptides
in the processed foods. Although the industrial appli-
cations of the peptides from egg proteins are limited,
some of the egg white proteins and their peptides are
already used as antimicrobial and antioxidant agents in
some foods, including cheese, wine, and processed meat
(Abeyrathne et al., 2013; Herath et al., 2015). The use
Types of peptides
OAC OMAlTr OM
0 0 0
63 10 4
257 15 24
124 21 33
105 19 33
34 10 55
583 (61.25) 75 (6.90) 149 (0.43)
of different enzymes or enzyme combinations can diver-
sify the sizes, functions, and the amino acid sequences
of the peptides produced.
Over the years, much research has showed strong
antioxidant activity of peptides from various protein
sources, but the use of peptides in real foods or pro-
cessed foods is limited. Some of the bioactive peptides
purified from the enzyme hydrolysates of proteins ex-
hibited potent inhibitory potential, but it is very dif-
ficult to commercialize those peptides because of low
yield, high cost, and difficulties in the separation and
purification processes. Therefore, instead of separating
individual functional peptides from hydrolysates, using
the whole enzyme hydrolysate of a protein with potent
ACE-inhibitory and antioxidant activities in food pro-
cessing would be more desirable because it can directly
add antioxidant, antimicrobial, or ACE-inhibitory func-
tions to the product. For example, nitrite used in cured
meat is considered as a carcinogenic agent but could
be replaced with hydrolysate containing functional egg
white peptides (Demeyer et al., 2008).
Future of the Use of Functional Proteins and
Peptides Derived from Egg White Proteins
Most of the individual egg white proteins separated
and the peptides derived from them are known to have
biomedical importance. The peptides that are known
to reduce ROS activity can be used as a drug or in
therapeutic activities to control the aging process in
humans. Also, the peptides derived from egg proteins
are known to have antioxidant activity, and thus they
can be used as natural antioxidant agents in most of
the processed food products like sausages and cheese.
Some of the proteins and peptides can be used as an-
timicrobial agents since lysozyme, OTf, and the pep-
tides derived from the egg white proteins have shown
strong growth suppressing abilities against E. coli and
other foodborne pathogens (Masschalck and Michiels,
2003). Peptides derived from ovalbumin are known to
have ACE-inhibitory activity, and thus may be used
to lower high blood pressure. Most of the peptides de-
rived from egg white proteins are proven to have strong
 EGG WHITE PROTEINS AND ANTIOXIDANT PEPTIDES
metal-binding capabilities and can be used as good
natural binding agents for iron or calcium. This in-
dicates that functional food industry can use most of
the peptides derived from egg white proteins as health-
promoting food components in the future. Many egg
white proteins and the peptides derived from them
showed antioxidant, antimicrobial, antiviral, antitumor,
and ACE-inhibitory activities, and most of the func-
tional peptides from egg proteins contained amino acids
such as Cys, Met, Trp, Tyr, Phe, and His.
The functional peptides from egg white proteins have
high potential to be used as replacements for the syn-
thetic antioxidants or antimicrobial agents used in pro-
cessed food products. Before this can take place how-
ever, strict vivo experiments need to be performed. The
stability of peptides in the digestive system, the mech-
anism of action, and metabolite of functional peptides
in vivo should be focused on in the future.
ACKNOWLEDGMENTS
This study was supported by the National Institute of
Food and Agriculture/USDA (Award No. 2015–67018-
23081), Washington, DC, and the National Natural Sci-
ence Foundation of China (Project No. 31471602).
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