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Bioactive Peptides: Formation and Impact Mechanisms

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 3rd International Conference on Advanced
Engineering Technologies
19-21 September 2019

Bioactive Peptides: Formation and Impact Mechanisms

Büşra TÜYSÜZ, Enes DERTLİ*, Özlem ÇAKIR, Engin ŞAHİN

Bayburt University, Department of Food Engineering, Bayburt, TURKEY

Keywords: Abstract
Bioactive peptides Bioactive peptides, which are naturally found in foods, have many physiological
Functional features benefits during digestion that are obtained either by fermentation or by enzymatic
Heat treatment hydrolysis. The biological action of these peptides can be registed as antimicrobial
Fermentation effect, lowering cholesterol, lowering blood pressure, antioxidant-antithrombotic
effect, immunomodulator and opioid effects. Foods go through many processes
until they become available to consumers. Frequently preferred processes in food
technology such as heat treatment and fermentation affect bioactive peptide activity
due to protein structure. Many proteins naturally present in foodstuffs show their
physiological activity either directly or indirectly. Dietary protein was found to be a
rich source of bioactive peptide. Foodborne bioactive peptides refer to peptides of
herb and animal root that have regulatory duty in metabolism in usual and adequate
nutrition. These peptides are passive in the protein series in which they are located
and can be activated in three ways: (a) to hydrolysis by the nutritive enzymes, (b)
hydrolysis by proteolytic microorganisms, (c) by the action of proteolytic enzymes
released from microorganisms or herbs. In the fermentation process requires
microorganism which is naturally present in raw material or added later starter
culture. These microorganisms break down sugars and proteins to form peptides
and free amino acids with different amino acid sequences. The degree of
degradation of proteins depends on bacterial species and fermentation conditions.
These peptides and amino acids produced from food by fermentation frequently
alter the functional, sensory, biological and rheological properties of the fermented
product. In this review, the creation of bioactive peptides and their various effects
on health have been explored.

1 INTRODUCTION
Bioactive peptides that are physiologically beneficial, are occurred during digestion of proteins, which are
naturally found in foods, with enzymatic hydrolysis and fermentation [1]. Bioactive peptides are in structurally
long chained form, generally containing 2-20 amino acids residue and also bioactive peptides that contains more
than 20 amino acids are also existing. Caseinomacropeptide (CMP) which contains 64 amino acids can be given
as an example [2]. Because of their small sizes and hydrophobic characteristics, bioactive peptides are absorbed
easier [3].

Biopeptides which organize the body functions and have positive effects are also known as specific protein
fragments. Their biological activity may change due to amino acid composition and amino acid sequence [4]. By
that alteration bioactive peptides may show various activities such as opioid-like (narcotic), immune system
regulator, antioxidant, antimicrobial, antithrombotic, hypocholesterolemic, cancer prevention, mineral binder,
protective against heart attacks and antihypertensive effects. Important sources of various bioactive peptides
include meat, milk and fish [5]. On the other hand, bioactive peptides of plant origin have recently attracted
caution. In agricultural wastes and secondary products, there have been a high amount asset arises of bioactive
peptide. In recent years social and scientific interest have been increasing for the re-evaluation of industrial by-
products [6].

The term food-borne bioactive peptide promotes adequate and balanced nutrition in humans. In addition refers to
peptides of herb or animal root having regulative functions. Bioactive peptides are found naturally in the
structure of food as well as can be released in inactive form by enzymatic hydrolysis in the principal protein.
Bioactive peptides obtained from plant and animal sources also occur in large amounts in fermented foods.

*
edertli@bayburt.edu.tr
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 Bioactive Peptides: Formation and Impact Mechanisms ICADET ‘19

Bioactive peptides may also occur during food processing or maturation with microbial enzymes. For example,
the most basic biochemical reaction during cheese ripening is proteolysis and as a result protein degradation
forms bioactive peptides. In this reaction, plasmin enzyme from milk, pepsin and chymosin enzymes from rennet
and enzymes formed by microorganisms play an important role in bioactive peptide formation [7].

Bioactive peptides is obtained from such products: milk camel milk, cheese, yogurt, sausage, Iberian ham, semi-
dry Cantonese sausage, egg, egg whites, egg membrane, soybeans, soy milk, chia, rice bran, peas, flaxseed,
mushrooms, cauliflower [8].

Sources such as meat, milk and fish are often used in bioactive peptide search, while derived from plants
bioactive peptides are of interest. They are richer in bioactive components such as antioxidants, sterols,
carotenoids, bioactive peptides in agricultural wastes and secondary products [9].

2 BIOACTIVE PEPTIDE PRODUCTION

Many different methods can be used to produce bioactive peptides. Bioactive peptides can be produced
endogenously or by an enzyme used in food processing, microbial fermentation and synthesis of amino acids
(Figure 1).

Proteolysis occurs naturally in large amounts of peptides during food processing. This proteolysis can occur with
the endogenous enzymes during the ripening of foods or by the united effect of both endogenous and exogenous
enzymes during fermentation. On the other hand, food proteins can be isolated, then hydrolyzed by enzymes
(peptidase) and protein hydrolysates are obtained. First, endopeptidases act, followed by exopeptidases (mainly
tri-peptidylpeptidases, di-peptidylpeptidases, aminopeptidases and carboxypeptidases). These peptides can be
further hydrolyzed by the digestive tract. Eventually some of which have bioactive properties different amino
acid sequence and different chain length peptides can be obtained. Commercial proteases used in the production
of bioactive peptides are shown in Table 1 and Table 2 shows the bioactive peptide sources, methods of
obtaining them and their bioactivity.

Food Proteins

Enzymatic Hydrolysis Food Processing Microbial Fermentation

Bioactive Peptides

Peptide Synthesis Expression from the host

Solvent Extraction
from Amino Acids cell via rRNA

Figure 1. Bioactive peptide production ways [10]

Table 1. Classification of Commercial Proteases from Natural Sources [11]

ANIMAL HERBAL MICROBIAL
SOURCES SOURCES SOURCES
PROTEASES

Carboxypeptidase A Ficin Alcalase; B. licheniformis

Carboxypeptidase B Bromelain Collagenase; C. histolyticum
α-chymotrypsin Papain Dipeptidylpeptidase;
Flavourzyme, Aspergillus orizae
Chymotrypsin Proteinase K; Tritirachium album
Pepsin Thermolysis; B. thermoproteolyticus

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 Bioactive Peptides: Formation and Impact Mechanisms ICADET ‘19

Table 2. Bioactive peptide sources, methods of obtaining and bioactivity [12].

PROTEIN SOURCE HYDROLYSIS METHOD BIOACTIVITY
FERMENTATION ENZYMATIC
HYDROLYSIS
Beef Thermolysin, proteinase, Anticarcinogenic activity
tyrosinase, prosthesis,
papain, pepsin
Camel and beef L. plantarum KX881772 Antioxidant activity,
sausage Antihypertensive activity,
Anticancerogenic activity
Geranium flour Bacillus subtilis A26 Cholesterol-lowering
(CTM 50700), activity
Bacillus
amyloliquefaciens An6
Kefir L. acidophilus, Anticarcinogenic activity
B. bifidum
Camel Milk L. plantarum Antimicrobial activity

Goat Milk Trypsin and ficin Antimicrobial activity

Insect (Gryllodes Alkalase Antihypertensive activity,
sigillatus) Antioxidant activity
Micro algae Protease K Antioxidant activity
(Spirulina platensis)
Coconut Alkalase, pepsin, trypsin, Antihypertensive activity
flavourzyme
Pollen Alkalase Antihypertensive activity

Palm Tree Alkalase, pepsin, trypsin, Antihypertensive activity

flavourzyme
Broad beans, quinoa B. animalis, Antihypertensive activity,
and wheat B. longum, Antidiabetic Activity
B. breve
Camu-camu L. helveticus, Antihypertensive activity,
(Myriciaria dubia L. plantarum Antidiabetic Activity
Mc. Vaugh) meyvesi
Fermented soybeans B. subtilis SCK-2, Antimicrobial activity
Lactococcus sp. GM005
Soy milk L. plantarum C2 Antimicrobial activity
Olive seeds Alkalase Cholesterol-lowering
activity

3 THE EFFECTS OF BIOACTIVE PEPTIDES ON HEALTH

Bioactive peptides have different potential health effects such as antioxidant, antihypertensive, antimicrobial,
antithrombotic, opioid and immunomodulatory effects. Some bioactive properties of the peptides are described
in greater detail below.

Antioxidant Effect

Oxidative tension appear as a sequel of the imbalance between reactive oxygen kind production and
antioxidative defenses. Research has shown that many diseases and disorders such as cancer, diabetes, arthritis,
Alzheimer's, schizophrenia are associated with oxidative stress. Oxidative stress can be reduced by consuming
foods rich in antioxidant substances. Antioxidants can delay or prevent oxidation of the substrate [13]. It has
been shown in several studies that peptides from different foods show antioxidant activity [14].

In one study [15] raw extract and peptide fractions won from leavened milk using Lactobacillus plantarum
strains were valued for biological activity. It was concluded that the antioxidant activity of crude extract and
peptide fractions obtained by using L. plantarum 55 strain was much higher than those obtained with other
strains.

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 Bioactive Peptides: Formation and Impact Mechanisms ICADET ‘19

The antioxidant activity properties of the peptides produced in goat and cow tulum cheese produced by
traditional methods were determined. The results determined by DPPH and ABTS method showed that
maturation time increased antioxidant activity. In the ABTS method the top antioxidant action was obtained
from the peptide extracts obtained from cow Tulum cheese, in DPPH method the utmost antioxidant activity was
stated in peptide extracts obtained from goat Tulum cheese [16].

Camel milk casein and camel milk whey proteins were hydrolysed with pepsin enzyme. The peptides obtained
after hydrolysis were distil using opposite phase high pressure liquor chromatography; antioxidant activities of
peptides, superoxide anion-producing xanthine oxidase (XOD) and DPPH radical removal was evaluated using
test systems. The peptides obtained significantly increased the tolerance of yeast cells to oxidative stress caused
by peroxide. Camel milk whey proteins and casein have been noticed to have bioactive peptides with important
antioxidant activities. Thus, they have been shown to be potential peptides for the avoiding and therapy of
oxidative stress-related ailment [17].

In another study, pollen-derived peptides were obtained by using alkalase enzyme. After enzymatic hydrolysis,
the peptides were purified by SEC method and pollen-derived antioxidant activity were fractionated by RP-
HPLC. The antioxidant action of the acquire fractions was found to be 66.61% by DPPH radical removal method
[18].

The peptides of the egg yolk protein were evaluated for various activities and hydrolysis was performed with
pepsin to obtain the peptides. Fractionation was then carried out using ion replacement chromatography and RP-
HPLC. Among the peptides obtained, YINQMPQKSRE has been shown to have very strong antioxidant activity
[19].

Enzymatic hydrolysis was performed to determine the antioxidant peptides from millet by using trypsin enzyme.
Dissimilar antioxidative potential of the insulating peptide was evaluated by ABTS, DPPH and hydroxyl radical
analyzes. The bioactive peptide eluted by gel filtering chromatography showed high antioxidant activity when
tested by dissimilar free radicals [20].

Antimicrobial Effect

Peptides exhibiting antimicrobial activity are obtained in vivo from various sources. They act against bacteria,
moulds and viruses, including parasites.

Properties such as peptide extent, amino acid compound, property to hydrophobic and secondary construction
vary according to the microorganism. Mutual characters of antimicrobial peptides are they 50% are hydrophobic
and that contain less than 50 amino acids. Bioactive peptides with antimicrobial properties breeded by lactic acid
bacteria (LAB) in raised foods have the possible to be used as food contribution. Antimicrobial peptides are
more advantageous than chemical preservatives because they have fewer side effects, require low intensity heat
treatment, and maintain the sensory properties and nutritional values of food [21].

They obtained 30 new peptides from bovine hemoglobin with antimicrobial activity using pepsin enzyme.
Reported that 24 of the peptides are in the α chain and 6 of them are in the β chain [22].

Antimicrobial activities of bioactive peptides obtained by zymosis of soy milk with L. plantarum C2 substrain
were investigated. Antimicrobial action of bioactive peptide fractions was checked by disc distribution method.
Peptides of 5000 Da size were found to exhibit high antimicrobial activity against B. cereus (10 ± 0.57 mm), S.
dysenteriae (11 ± 0.57) , L. monocytogenous (10 ± 0.57) and E. coli (12 ± 0.57) pathogens [23].

In another study, enzymatic hydrolysis was performed from Spirulina platensis using alkaline papain enzyme
and protease to obtain antimicrobial peptide. The minimum inhibition concentration of this peptide was devised
to be 16 mg / mL for S. aureus and 8 mg / mL for E. coli [24].

In a study conducted in 2017, it was determined that Tibetan ox milk protein hydrolysates obtained by pepsin
hydrolysis had antimicrobial activity. Two effective antimicrobial peptide was obtained. These peptides were
detected as the aminoacid series of Arg-Val-Met-PheLys-Trp-Ala and Lys-Val-Ile-Ser-Met-Ile. Arg-Val-
MetPhe-Lys-Trp-Ala showed antimicrobial activity to S. aureus, E. coli, S. paratyphi, L. innocua, E. cloacae and
B. subtilis. The other peptide Lys-Val-Ile-SerMet-Ile inhibited the growth of not only bacteria but also fungi
[25].

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 Bioactive Peptides: Formation and Impact Mechanisms ICADET ‘19

Antihypertensive Effect

Hypertension is a cardiovascular ailment that affects about a quarter of the world's citizenry. Angiotensin I-
converting enzyme (ACE) is a dipeptidyl carboxypeptidase, converts angiotensin I to angiotensin II. Angiotensin
II, which has a vasoconstrictor effect, act apart an prominent physiological role in regulating blood pressure and
fluid-salt stabilize in mammals [2]. Peptides that inhibit ACE enzyme are potential blood pressure lowering
agents [21]. Obtaining antihypertensive activity from cheese, milk, fish, meat, various herb and algae has been
the subject of many studies. Obtaining antihypertensive activity from meat, milk, fish, cheese, various herb and
algae has been the subject of many studies. However, there was no correlation between antihypertensive effects
obtained in vivo and inhibition of ACE enzyme with in vitro results. Therefore, there is no guarantee that the
results of ACE inhibition obtained in vitro will have the same effect in vivo [26].

Since the starter cultures used in the dairy industry have high proteolytic activities, bioactive peptides are formed
in the production of fermented dairy products. There have been many studies on different bioactive peptides
consisting from milk proteins as a result of microbial proteolysis [27]. Ile-ProPro and Val-Pro-Pro tripeptides
insulated from fermented sourish milk with S. cerevisiae and L. helveticus inhibit ACE enzyme. Thus, long-term
use has been observed to prevent the development of high blood pressure in rats [4].

Qula casein from Tibetan cow's milk was hydrolyzed with two different enzyme combinations. The skill of the
obtained hydrolysates to inhibiting ACE enzyme was investigated. The maximum ACE inhibitory effect (<3
kDa) were found in hydrolysates obtained by the combination of alkalase + thermolysin and thermolysin +
proteinase K enzymes. Hypotensive effects in clinical trials a commercial product containing antihypertensive
peptides with proven has been launched [28].

Eggs are important as a resource of many bioactive peptides that can be used in the medical and nutrition
industries [58-60]. Egg ovotransferrin was enzymatically hydrolyzed. In vitro ACE detected three tripeptides
with inhibitory effects. They have the amino acid sequence Ile-Arg-Trp, Leu-Lys-Pro and Ile-Gln-Trp. Oral
administration of IleGln-Trp and Leu-Lys-Pro tripeptides to rats diagnosed with high blood pressure was found
to have both lowered blood pressure [29].

Legumes are imagineed to be a significant source of bioactive peptides with their rich protein content. A study
using dry beans, kidney beans and lentils showed that a heat treatment lasting 50 minutes at 121 ° C increased
ACE inhibitory activity in all three samples [30].

Soybeans are another valuable source of ACE inhibitors. Some ACE inhibitor peptides were isolated from
prepared hydrolyzates and fermented soybean products. ACE inhibitor peptides were isolated from Tofuyo, a
soybean meal fermented with fungi such as Monascus and Aspergillus [31].

Immunomodulator Effect

The basic function of the immune system is to identify and remove pathogens or impurities. Inflammatory
inhibiting cytokines are active in the immune system. Another part of the immune system is the attack of
antigens to the identified pathogen or foreign substances [32]. Immune-regulating peptides can elevate immune
cell functions as mensured by lymphocyte proliferation, cytokine regulation and antibody synthesis [33]. In
addition, immune regulator peptides can decrease allergic reactions in atopic mortal and increased mucosal
immunity exemption in the gastrointestinal tract [34]. Immunopeptides have the ability to regulate the
proliferation of lymphocytes in the human body and increase the phagocytic activity of macrophages [35]. The
peptide found in the 60-70 sequence of β-casein from the milk proteins, has been reported to be
immunomodulatory [36]. Caseinophosphopeptides are thought to enhance the immune system. Phosphoserine
groups, lymphocytes and macrophages of these peptides effect as activating receptors [37]. The
immunomodulatory effect varies depending on the dose. For example; some caseomorphins have been reported
to suppress the proliferation of lymphocyte cells at low concentrations and to promote lymphocyte proliferation
at higher concentrations [33].

Opioid Effect

In the late 1970s, the presence of food-borne peptides with opioid activity was identified [2]. Opioid receptors
(δ- , κ - and µ -type) are found in the neural, endocrine and immunity systems of the mammal, bearing the gastral
tract. This receptors may interact with exogenous opioids and endogenous ligands [38]. These peptides have
been semestered 'exorphins' because of their morphological similarity to endogenous ligands interacting with μ,

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 Bioactive Peptides: Formation and Impact Mechanisms ICADET ‘19

ó or κ-type opioid receptors [39]. Opioid peptides are with a little aminoacid sequence containing 5-10 amino
acids, such as casomorphins and exorphins, which can bind to specific opioid receptors on the intestinal
epithelium and other cells [40]. These receptors are responsible for characteristic physiological functions. Such
as, δ-receptor excited behaviors, µ-receptor excited behaviors and suppression of intestinal motility, κ-receptor
sedative effect and food absorption are responsible from the effect [41]. Opioid peptides are formed by opioid
antagonists (stimulants) and opioid agonists (relaxants). While peptides having a relaxing effect show a
morphine-like drug effect, stimulating peptides have a reducing or inhibiting effect [42]. Kasokines from casein-
derived peptides have a stimulating effect; exorphin, α and β-casomorphine have a relaxing effect [43].

4 CONCLUSION
There is intense interest in the production of proteolytic enzymes and fermentation of biologically active
peptides from plant and animal products. Studies on obtaining bioactive peptides from different origins and
determining their functions are continuing. The relationship between the bioactive properties and compositions
of the peptides has not yet been elucidated. But, in vivo and in vitro studies have shown that peptides obtained
from different resources show antimicrobial, antithrombotic, antihypertensive, cholesterol lowering, antidiabetic,
opioid, anticarcinogenic, immunomodulatory, mineral binding and antioxidative properties. Numerous works
have been conducted on the action mechanisms of bioactive peptides in delaying and treating various diseases. It
is composed of large amounts of fermented foods, especially in the human diet. Fermented dairy products are the
most worked foods for bioactive peptides. However, by hydrolyzing all food-derived proteins with proteolytic
enzymes or fermenting them with special microbial cultures, peptides with different activity, different length and
molecular weight amino acid chains can be produced. Purification and separation of these peptides can also be
applied in the presence of technological advances. Although there are still shortcomings in the transition of some
products to industrial applications and in food applications, many registered bioactive peptides are currently sold
in the market. The production of new value-added products, which have positive effects on health, will also
contribute to the economy of the country, especially by processing protein-rich waste or processing by-products
in this way. Furthermore, further research is demanded on the use of bioactive peptides in the improving of
functional produces.

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