International Journal of Gastronomy and Food Science 32 (2023) 100708

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International Journal of Gastronomy and Food Science

journal homepage: www.elsevier.com/locate/ijgfs

Physicochemical, rheological, and textural properties of gelatin extracted

from chicken by-products (feet-heads) blend and application
Omaima Aidat a, Louiza Belkacemi a, b, *, Mahmoud Belalia c, Mohamad khairi Zainol d,
Humam Shaaban Barhoum e
a
Food Technology and Nutrition Laboratory, Abdelhamid Ibn Badis University, Mostaganem, Algeria
b
Higher School of Agronomy, Mostaganem, Algeria
c
Structure, Development and Application of Molecular Materials Laboratory, Abdelhamid Ibn Badis University, Algeria
d
Food Technology Program Laboratory, University of Malaysia, Terengganu, Malaysia
e
Department of Plant Protection, Faculty of Agriculture, Damascus University, Syrian Arab Republic

A R T I C L E I N F O A B S T R A C T

Keywords: The research was carried out to determine the appropriate acetic acid concentrations to extract the gelatin from
Chicken by-products chicken by-products blend (feet and heads) with suitable rheological and textural properties for potential
Feet-heads blend applicability as a gelling agent in the formulation of chocolate custard. Chicken by-products were treated with
Gelatin
two acetic acid concentrations in order to obtain two gelatins: gelatin extracted from chicken by-product treated
TPA
Gel strength
with 3% (CBBG3) or 5% (CBBG5) of acetic acid. Gelatins were analyzed for their proximate composition, color,
Chocolate custard gel strength, textural profile (TPA) and amino acids composition (HPLC). Among the two gelatins, CBGG3 dis­
played the best gel strength (204.91 ± 0.00 bloom), textural parameters such as hardness, adhesiveness, and
gumminess and thus it was used as gelling agents at doses of 3.5, 4.5, and 5% to substitute carrageenan in
chocolate custard preparation. Sensory evaluation by panelists revealed their preference for the chocolate cus­
tard prepared with CBBG3 at 4.5%, over the commercial carrageenan-based-one. Gelatin extracted from chicken
by-products blended with 3% acetic acid represents a potential alternative to the expensive carrageenan additive
in custard preparation and probably other food products.

1. Introduction Regenstein, 2007; Koli et al., 2012).

Gelatin is recognized as an important biopolymer used in various
industries (Schrieber and Gareis, 2007). The rheological and physical
characteristics of gelatin allow it to be used in various fields such as
pharmaceuticals, cosmetics, photography, and mostly in the food in­
dustry (Alipal et al., 2019). Indeed, gelatin is an important food additive
included in numerous food products (Mohos, 2010) according to its
coagulation properties (Ramos et al., 2016), bloom strength, and
thermo-reversibility (Mariod and Adam, 2013). In confectionery, it is
used to provide chewiness, texture, and foam stabilization; while in
gelatin-based desserts, gelatin is incorporated to provide creaminess, fat
reduction, and improved mouthfeel. Gelatin maintains stabilization and
texturization in dairy products and forces binding with water in meat
products (Johnston-Banks, 1990; Schrieber and Gareis, 2007). Finally, it
is notably used in the formulation of water-based dessert gels (Zhou and
The global gelatin market size was esteemed at USD 5.80 billion in
2021 and is expected to expand at a compound annual growth rate
(CAGR) of 9.5% from 2022 to 2030 (Grand View Research, 2023)
because of the growth volume of gelatin-based products. Pig skin and
bovine bones and hide are the principal source providing gelatin to the
international market; however, they remain a real problem for religious
groups such as Jewish, Muslim, and even Buddhists (Zin et al., 2021).
Therefore, gelatin production from alternative sources is receiving
attention from experts in different fields to satisfy their needs (Karim
and Bhat, 2009). It can be obtained from fish, insects (Mariod and Adam,
2013), and different parts of chicken (Alipal et al., 2019).
Chicken by-products are an excellent gelatin source that can be used
for a wide variety of purposes in the industrial sector (Rather et al.,
2022). As an alternative, poultry gelatin is not problematic in terms of
health and religious concerns (Nik, 2014). Furthermore, the valorization

Abbreviations: TPA, Textural Profile Analysis.

* Corresponding author. Food Technology and Nutrition Laboratory, Abdelhamid Ibn Badis University, Mostaganem, Algeria.
E-mail addresses: louiza.belkacemi@univ-mosta.dz, l.belkacemi@esa-mosta.dz (L. Belkacemi).

https://doi.org/10.1016/j.ijgfs.2023.100708
Received 23 January 2023; Received in revised form 24 February 2023; Accepted 8 March 2023
Available online 21 March 2023
1878-450X/© 2023 Elsevier B.V. All rights reserved.
O. Aidat et al.
of poultry by-products into gelatin is an effective way to use chicken
waste (Santana et al., 2020) which can be converted into value-added
products with similar chemical composition to bovine extract and
with better physicochemical properties than fish extract gelatins (Sar­
bon et al., 2013).
Determining texture profile is as well important to define the sensory
and functional properties of gelatin (Chandra and Shamasundar, 2015).
Nevertheless, limited studies focused on the textural profile of gelatin
gels extracted from different sources (Rahman and Al-Mahrouqi, 2009;
Boran and Regenstein, 2010; Chandra and Shamasundar, 2015; Calvarro
et al., 2016; Zhang et al., 2021) including poultry ones. Most studies
dealt with extracted gelatin from either chicken feet or heads mostly
using different extraction protocols probably because of heterogeneity
of their tissues. In fact, chicken feet mostly consist of cartilage and have
small amount of tiny bone (Rahman and Jamalulail, 2012) compared to
chicken head which is a homogenous tissue combination of skin and
bone (Ee et al., 2019; Rahim et al., 2021). Besides, comparing studies
having used relatively the same gelatin extraction procedure reveals
some differences in yield and physicochemical, rheological and even
textural properties of extracted gelatin from chicken heads (Du et al.,
2013; Ee et al., 2019) or feet (Almeida and Lannes, 2013; Chakka et al.,
2017; Choe and Kim, 2018). Using both chicken feet and heads together
as one raw material for gelatin extraction with a same protocol would
not only avoid sorting process for industry but would also result in
gelatin with good properties. To our knowledge, it is the first study
focused on extracting gelatin from chicken by-products blend i.e. feet
and heads blend. So, the present study aimed to characterize gelatin
extracted from the chicken by-products blend (heads and feet) using two
acetic acid concentrations and to incorporate it as a gelling agent in the
formulation of chocolate custard.
2. Materials and methods
2.1. Raw materials
Fresh chicken feet and heads (Arbor Acres broiler) were collected
from the Poultry Group-West Algeria- Mostaganem (GAO-ORAVIO), a
local slaughter and meat processing industry in the west of Algeria. The
samples transferred to the laboratory were cleaned (de-nailed, plucked,
etc.) and washed with tap water. The feet and head samples were then
cut into small pieces (approximately 5 cm) and stored in plastic bags at
− 20 ◦ C in equal amounts (50 g foot pieces + 50 g head pieces) until
gelatin extraction. The chemical manufacturer Sigma-Aldrich provided
food-grade acetic acid. All the reagents and chemicals used were of the
highest quality.
2.2. Gelatin extraction
Gelatin was extracted from the chicken by-products blend (CBB)
using acetic acid, as described by Chakka et al. (2017), with some
modifications. To eliminate non-collagen material, 100 g of thawed
feet-heads blend samples were soaked in 0.5 M NaOH solution in a ratio
of 1/10 (w/v) at room temperature for 18 h under stirring. The samples
were filtered and washed numerous times with distilled water to
neutralize the pH. Following filtration, the residue was treated with
acetic acid at two different concentrations: 3 and 5% to obtain CBBG3
and CBBG5, respectively. The samples were filtered under vacuum after
18 h of acetic acid treatment at +4 ◦ C with constant stirring, and the
gelatin extraction was carried out in warm water at 75 ◦ C for 6 h. Then,
the extracts were agitated for 20 min with activated charcoal (4 g) to
eliminate odors and contaminants (Saenmuang et al., 2020). Finally, the
filtered extracts were poured into Petri plates and dried for 48 h in a
vacuum oven (45 ◦ C). The gelatin sheets were powdered using an
electric grinder.
2
International Journal of Gastronomy and Food Science 32 (2023) 100708
2.3. Physicochemical properties of gelatin
2.3.1. Extraction yield
The gelatin extraction yields obtained from chicken by-products
blend samples were determined by the gravimetric method and calcu­
lated using the following formula:
Yield (%) = (Gelatin dry weight / fresh raw material weight) × 100
2.3.2. Proximate composition of gelatin
The moisture, ash, and fat content of dried gelatin were determined
according to the AOAC (2000) method. Briefly, moisture content was
determined by oven-drying at 105 ◦ C to a constant mass. Ash content
was determined gravimetrically after incineration of the sample at
550 ◦ C in a muffle furnace. Crude fats were determined by Soxhlet
extraction. Protein content was analyzed according to the Kjeldahl
method (AOAC, 2000) by determining the total nitrogen content using
an automatic nitrogen analysis (Gerhardt analytical system, Gerhardt
GmbH & Co. KG, Germany). The crude protein content of gelatin was
obtained by multiplying the nitrogen value by the factor 5.55 (Jones,
1931).
2.3.3. pH determination
Gelatin solution (1%) was prepared in distilled water; then, it was
heated at 45 ◦ C for 5 min to dissolve gelatin. After that, the solution was
cooled at room temperature before pH measurement using a pH meter
AD1200 (ADWA INSTRUMENTS, Hungary).
2.3.4. Color analysis
For color measurement, the samples were prepared by using 6.67%
(w/v) gelatin gels. The color parameters L*, a*, and b* was measured
using a Chroma Meter (CR-400 model, Konica Minolta Sensing, Japan).
2.4. Rheological properties of gelatin
2.4.1. Bloom strength
Bloom strength was determined by the method described by Sarbon
et al. (2013). Gelatin was weighed (7.5 g) and dissolved in deionized
water (105 mL) in a bloom jar, and the solution (6.67%) was covered
and maintained at room temperature for 3 h. After that, the solution was
heated in a water bath at 60 ◦ C for 20 min, then cooled at room tem­
perature and kept at 10 ◦ C for 16 h. The bloom strength was measured by
a texture analyzer (stable micro systems, UK) using a cylinder probe at
speed of 0.5 mm/s to 4 mm depth of the sample. The maximum force (g)
was obtained and translated as the gel bloom value (g).
2.4.2. Texture profile analysis (TPA)
2.4.2.1. Gel preparation. Gelatin gels were made by dissolving the dry
powder in distilled water to a final concentration of 6.67% (w/v). The
solution was then heated for 30 min in a water bath at temperatures
ranging from 50 to 60 ◦ C with occasional stirring. The mixture was then
cooled for 10 min before being placed in a refrigerator (4–6 ◦ C) for 24 h
to allow gel formation. Following that, the gels were removed from the
beaker with a spatula and used for texture analysis.
2.4.2.2. Instrumental texture profile analysis (two-cycle compression test).
The test was performed according to the method described by Chandra
and Shamasundar (2015). The TPA gel’s dimensions were 3.0 cm in
diameter by 4.0 cm in height. TPA was carried out using a TA-TX2
texture analyzer (Stable Micro Systems Ltd., Surrey, UK), attached to a
50-kg load cell. A 75-mm diameter compression platen was used to
compress a cylindrical shape of the gels, which were compressed twice
to 40% of the original height of the gel at a compression rate of 1.0 mm/s
at room temperature. The TPA settings were as follows: pre-test speed:
1.5 mm/s; test speed: 1.0 mm/s; post-test speed: 1.5 mm/s; target mode
O. Aidat et al.
distance: 10 mm; trigger force: 5 g; trigger type: Auto; data acquisition
rate: 200 points per second (pps). The delay between the first and second
compression was 5 s. The TPA analysis was carried out at ambient
temperature (25 ◦ C) and the analysis was completed within 100 s. A
force-time graph was generated and textural parameters, such as hard­
ness, adhesiveness, springiness, cohesiveness, fracturability, resilience,
gumminess, and chewiness, were calculated using the software provided
along with the instrument.
2.5. Amino acid analysis
2.5.1. Preparation of samples and standards
The oxidation process was carried out using performic acid. In a
round bottom flask, a sufficient quantity of the gelatin sample was added
to a mixture of 75 mg of phenol crystals, 1.5 mL of hydrogen peroxide
(30%), and 13.5 mL of formic acid (88%). Afterward, the sample was
rested for 30 min at room temperature at first then placed in a cooler for
another 15 min before allowing its oxidation for another 16 h.
The hydrolysis process was carried out by adding phenol crystals, an
equivalent volume of 50 mL of distilled water, and concentrated hy­
drochloric acid in a 500 mL round bottom flask. The solution was then
heated using a reflux apparatus for 24 h, and the hydrolysates were
partially neutralized with 40 mL of 7.5 M NaOH.
2.5.2. Derivatization of amino acids with phenyl isothiocyanate (PITC)
Each gelatin sample of 30 mg was homogenized for 1 min at medium
speed in 2.0 mL water in a glass tube with a homogenizer equipped with
a 7-mm generator. Five microliters of the mixed sample were transferred
to a glass tube that has been acid-washed with 6 N HCl for 24 h. The
sample was then lyophilized. The samples were hydrolyzed in a vacuum
for 24 h at 110 ◦ C. Samples were vacuum-dried and then put in the
freezer up to derivatization and HPLC analysis. An extra replication was
performed serving as a backup in case the sample tube might have been
contaminated during the hydrolysis process due to HCl condensation. At
the same time, a 10 μL sample of an amino acid standard mixture was
dried in a different acid-washed glass tube.
Phenylthiocarbamyl amino acids of each sample and the standards
were removed from the dried matrix by vortex mixing them with 500 μL
of a 5 mM Na2HPO4 buffer with a pH of 7.4 and 5% acetonitrile. Due to
the PTC amino acid’s sensitivity to light and ambient temperature,
samples were reconstituted one at a time. An HPLC system with a col­
umn heater, autosampler, variable wavelength detector, and data
acquisition software controller was used to analyze 10 μL of samples. A
Pico-Tag dimethyloctadecylsilyl bonded amorphous silica column with
an inline column filter was used as the reverse-phase column. The col­
umn temperature was maintained at 38 ◦ C. The PTC amino acids were
separated and eluted by a gradient resulting from mixing eluents A and
B. Eluent A consisted of 150 mM CH3COONa, 3′′ H" _"2′′ O, 0.05% TEA,
and 6% acetonitrile, pH 6.4. Eluent B consisted of 6:4 acetonitrile: water
(v/v). The flow rate was 1 mL/min throughout, and the gradient con­
sisted of the following profiles: 100% A at the start, 80% A and 20% B at
5.5 min, 54% A and 46% B at 10 min, 100% B at 10.5–12.5 min, 100% A
at 13 min. The PTC amino acids eluted from the column were detected at
254 nm and recorded. The column was regenerated and equilibrated
with eluent A for 10 min. A new and freshly reconstituted sample was
injected and analyzed (Kwanyuen and Burton, 2009).
2.6. Application: gelatin incorporation in chocolate custard
2.6.1. Chocolate custard preparation
Regarding the medium bloom value of CBBG3 and its textural profile
(sections 3.3 and 3.4), this later was incorporated in a dairy product as a
gelling ingredient. The aim was to substitute the carrageenan in a
chocolate custard preparation with a cheaper gelling agent. The prep­
aration of chocolate custard was done in the following step: CBBG3 was
mixed at different doses (3.5, 4.5, or 5%) with the modified starch (5 g),
3
International Journal of Gastronomy and Food Science 32 (2023) 100708
sugar (120 g), cocoa (40 g) salt (1 g) and 1 mL of chocolate flavoring.
Dried ingredients were dissolved in 1 L of milk at 70 ◦ C. The prepara­
tions were then heated at 120 ◦ C for 10 s. The gelatin-based-custard
chocolate preparations CCG 3.5%, CCG 4.5%, and CCG 5% were
poured into individual molds and placed in the refrigerator at 4 ◦ C for
18 h. A like-commercial carrageenan based-chocolate custard (CCC)
prepared according to the described recipe using carrageenan at 3.5%
was considered as control. The different chocolate custrad preparations
are shown in Fig. 1.
It is important to precise that the extraction of the gelatin has been
performed under good hygienic conditions and the mold filling under a
UV hood.
2.6.2. Sensory evaluation
A sensory analysis was conducted to identify the sensory acceptance
of 45 untrained panelists drawn from the Higher School of Agronomy of
Mostaganem and Mostaganem university. The panelists of both genders
(21–32 years) were instructed to score the four chocolate custard
preparations which were randomly presented. The five evaluated attri­
butes included appearance, flavor, mouthfeel texture, taste, and overall
acceptability. The ratings were on a 9-point hedonic scale ranging from
9 (like extremely) to 1 (dislike extremely).
2.7. Statistical analysis
The statistical analyses were performed using a statistical program
Minitab v.18. The data obtained from the sensory evaluation were sta­
tistically compared by one-way variance analysis (one-way ANOVA). A
comparison between the two gelatins was performed using T-test. The
significant level was accepted at p ≤ 0.05.
3. Results and discussion
3.1. Gelatin extraction yield and physico-chemical properties
The yield of CBBG3 and CBBG5 reached 10.49% ± 0.49 and 13.2%
± 0.24, respectively. It seems that higher acetic acid concentration
induced a higher extraction of soluble collagen which consequently
increased gelatin yield extraction. Overall, the yield in the present study
was higher than that obtained from chicken heads (Ee et al., 2019) and
chicken feet (Almeida and Lannes, 2013), but lower compared to the
yield of gelatin extracted by biotechnological procedure from chicken
feet (Mokrejš et al., 2019). The difference in yield is due to the different
compositions of the raw materials, especially the collagen content and
the extraction conditions (Du et al., 2013; Lassoued et al., 2014; Sin­
thusamran et al., 2014).
The proximate composition of gelatin CBBG3 and CBBG5 is reported
in Table 1. Both gelatins had moisture content that met the prescribed
limit (≤16%) (Schrieber and Gareis, 2007; Almeida and Lannes, 2013)
which is important to prevent microbiological development (Sebastian,
2014). The protein content of CBBG3 and CBBG5 were statistically
similar (p > 0.05) and comparable to the results reported for bovine
gelatin (Rahman and Jamalulail, 2012). While the fat and ash contents
of both CBGG3 and CBBG5 were not included in the standard ranges
which are 0% of fat for type A and B, 0.3–2% of ash for type A, and
0.5–2% for type B (Gmia, 2019). High mineral content probably resulted
from head and foot bone demineralization (Chakka et al., 2017). For the
application of gelatin in the food industry, the mineral content must
reach a maximum of 3% (Gál et al., 2020). This limit was not exceeded
for CBBG3. To reduce the undesirable amount of ash in these gelatins, it
is recommended to pass gelatin solutions through ion exchange chro­
matography or an appropriate technique for gelatin demineralization,
such as ultrafiltration or nanofiltration (Sebastian, 2014). Using acti­
vated charcoal to remove undesirable odors and lighten color was
insufficient in reducing excessive amounts of fat as reported by Talap­
phet et al. (2017). Thereby, using solvents like ethanol is recommended
O. Aidat et al. International Journal of Gastronomy and Food Science 32 (2023) 100708

Fig. 1. Appearance of different gelatin chocolate custards (CCC: commercial custard (carrageenan based-chocolate custard), CCG: gelatin based-chocolate custard
prepared at different doses (3.5, 4.5, or 5%)).

The hunter color a* and b* values were affected by acetic acid con­
Table 1
centration (p < 0.001). The a* and b* value of CBBG5 were higher than
Proximate composition of gelatin extracted from chicken by-products (feet-
that of CBBG3. It seems that high acid concentration results in more
heads) blend.
yellowness gelatin.
Parameters (%) Gelatins P-value

CBBG3 CBBG5 3.2. Gel strength

Moisture 7.86 ± 0.37 4.93 ± 0.75 0.333
Fat 2.99 ± 0.50 3.51 ± 0.40 0.100 Bloom value is the key parameter to determine gelatin quality which
Ash 2.40 ± 0.57 4.45 ± 0.69 0.333 in turn determines the commercial value of gelatin products (Schrieber
Protein 86.53 ± 1.02 88.13 ± 0.97 0.333
and Gareis, 2007; Boran and Regenstein, 2010; Sebastian, 2014). The
pH 4.41 ± 0.39 3.81 ± 0.31 0.333
CBBG3 gelatin has an acceptable gel strength (Table 3) since it is within
CBBG3: chicken by-products blend gelatin extracted at 3% of Acetic acid. the range of 150 and 220 g. Gelatin with a bloom value within this range
CBBG5: chicken by-products blend gelatin extracted at 5% of Acetic acid. can be useful as an ingredient in dairy products (Imeson, 1997;
Values represent the mean ± standard error.
Schrieber and Gareis, 2007). The CBBG5 is low-quality gelatin since its
Comparison between the two gelatins was performed using paired samples T-test
bloom strength is less than 150 g (Hanani, 2016). This kind of gelatin
(alpha = 0.05).
can be useful for encapsulation (Johnston-Banks, 1990; Schrieber and
Gareis, 2007; Boran and Regenstein, 2010; Sebastian, 2014; Gmia,
during raw material pretreatment to reduce the lipid content in the
2019). This difference in bloom strength is related to the amino acid
finished product (Chakka et al., 2017; Rahim et al., 2021; Shaari et al.,
composition which in turn is affected by acetic acid concentration as
2021).
reported by Chakka et al. (2017). It is well established that the gel
The pH values of gelatins extracted from CBBG3 and CBBG5 were
strength is related to the gelatin network stability which reduces as the
included in the pH standards of commercial gelatins (3.8–7.6) (Gál et al.,
number of amino residues decreases in gelatin (Liu et al., 2009).
2020). The pH value can be affected by the acetic acid concentration
used during the extraction phase, or by the acidity of the extraction
3.3. Texture profile
water that is slightly acidic. According to some authors (Gudmundsson
and Hafsteinsson, 1997; Songchotikunpan et al., 2008; Chakka et al.,
Texture profile analysis (TPA) is a double compression test deter­
2017), the pH value of gelatin is influenced by the type and strength of
mining the textural properties of food products (Friedman et al., 1963;
the chemical used during the extraction procedure, as well the washing
Rather et al., 2022). The method has been utilized widely for food
process.
characterization and quality control (Tuoc and Glasgow, 2012). The
The results of color analysis are presented in Table 2. The two gel
force-deformation curves of the gelatin samples are given in Fig. 2.
gelatins did not differ from each other in term of lightness (p > 0.05).
The hardness is related to the strength of the gel structure under
Even if both gelatin gels were darker compared to that found in other
compression and corresponds to the maximum force during the first
poultry gelatin extracted from either feet (Chakka et al., 2017) or heads
(Du et al., 2013; Ee et al., 2019), this does not imply poor rheological
Table 3
properties.
Gel strength and texture profile of gelatin extracted from chicken by-product
According to Ockerman and Hansen (2000), although color param­
(feet-heads) blend.
eters may decrease appearance attributes, they do not affect the func­
tional properties of gelatins. Color has aesthetic value because it does TPA Gelatins Mean P-value

not theoretically influence the functional properties of gelatin but only Gel strengh (bloom) CBBG3 204.91 ± 0.00 0.000
serves to satisfy consumer needs (Zarai et al., 2012; Shyni et al., 2014; CBBG5 130.85 ± 0.00
Hardness CBBG3 22.71 ± 0.00 0.000
Mulyani et al., 2017). Besides, the decreased L* value of both gelatins is
CBBG5 16.47 ± 0.00
due to the Maillard reaction induced by the free amino acid released Adhesiveness CBBG3 − 20.68 ± 0.00 0.000
from the acid in contact carbonyl groups present in the gelatin (Mulyani CBBG5 − 56.19 ± 0.00
et al., 2017). Springiness CBBG3 0.96 ± 0.00 0.004
CBBG5 0.92 ± 0.01
Cohesiveness CBBG3 0.88 ± 0.01 0.000
Table 2 CBBG5 0.75 ± 0.00
Color attributes of CBBG3 and CBBG5 gelatins. Gumminess CBBG3 201.27 ± 0.02 0.000
CBBG5 122.32 ± 0.01
CBBG3 CBBG5 P-value
Chewiness CBBG3 191.24 ± 0.00 0.000
L* 61.14 ± 0.31 61.59 ± 0.27 0.28 CBBG5 110.91 ± 0.00
a* − 1.93 ± 0.24 − 2.40 ± 0.04 0.05 Resilience CBBG3 0.89 ± 0.00 0.000
b* 9.76 ± 0.23 11.74 ± 0.37 <0.0001 CBBG5 0.62 ± 0.00

CBBG3: chicken by-products blend gelatin extracted at 3% of Acetic acid. CBBG3: chicken by-products blend gelatin extracted at 3% of Acetic acid.
CBBG5: chicken by-products blend gelatin extracted at 5%of Acetic acid. CBBG5: chicken by-products blend gelatin extracted at 5%of Acetic acid.
* Significance level alpha = 0.05 paired samples T-test. *Significance level alpha = 0.05 paired samples T-test.

4
O. Aidat et al. International Journal of Gastronomy and Food Science 32 (2023) 100708

Fig. 2. Comparison of textural profile between CBBG3 and CBBG5 gelatins CBBG3 and CBBG5: chicken by-products blend gelatin extracted with 3 and 5% of
acetic acid).

cycle of compression (Chandra and Shamasundar, 2015), which corre­ testifies to the ability of elastic recovery which is related to the nature of
sponds to the maximum peak in Fig. 2. The hardness of gel samples the network formed during gelatin gel related in turn to amino residues
prepared with CBBG3 and CBBG5 is considerably different (p < 0.001) (Liu et al., 2009).
(Table 3). Acetic acid treatment with a lower concentration (3%) pro­ On the other hand, no brittleness (Fig. 2) was observed for both
vides a much stronger gel compared to that treated with acetic acid at gelatin gels extracted from the blended chicken by-products (heads and
5%. feet) at 40% compression. This was also the case with fish gelatin
Adhesiveness is the negative surface force for the first bite and rep­ (Rahman and Al-Mahrouqi, 2009) and porcine and bovine ones
resents the work required to overcome the forces of attraction that exist (Almeida and Lannes, 2013).
between a food’s surface and the surfaces of other materials it encoun­ From the results of the textural profile analysis, the textural property
ters (Chandra and Shamasundar, 2015b). The higher value of stickiness of gelatin CBBG3 is better compared to CBBG5. Based on the higher
of CBBG3 compared to CBBG5 implies a soft texture and can be used for values of the texture parameters and gel strength which indicate a better
some dessert preparations (Rather et al., 2022). These results are quality of gelatin (Yang et al., 2007), it can be concluded that CBBG3 is
consistent with those of the Yusof et al. study (2019) which reported that of good quality and can be used in food applications.
high-firmness frosts also have a high adhesion value.
Springiness is the ability of a food product to recover its primary
height after being deformed in the first compression. Higher elasticity 3.4. Amino acid composition
implies more chewing energy in the mouth (Rahman and Al-Farsi,
2005). Both samples showed elasticity values (Table 3) close to the The composition of the two gelatins showed a relatively higher
value of 0.943 obtained with the commercial porcine gelatin (Chandra amino acid content in CBBG3 compared to CBBG5 (Table 4), with
and Shamasundar, 2015).
Cohesiveness indicates the intermolecular strength of the food and Table 4
the degree to which a food can be deformed before breaking (Radočaj Amino acid composition of gelatin extracted from chicken by-products (feet-
et al., 2011). Cohesiveness in Fig. 2 is defined as the ratio of positive heads) blend.
force area under the first and second compression (Lau et al., 2000). The Amino Acids CBBG3 (w/w%) CBBG5 (w/w%)
cohesivity value of CBBG3 is higher than that of CBBG5. From these
Arginine 1.94 2.00
results, it can be concluded that CBBG3 has a higher capacity to resist to Aspartic Acid 3.89 3.79
a second deformation than the first one. Alanine 0.66 0.67
Gum is the energy needed to break down a semi-solid food to swal­ Glutamic Acid 8.04 7.63
Glycine 20.24 17.73
low it (Hwang et al., 2012). Gumminess is calculated by multiplying
Histidine 1.28 1.32
hardness with cohesiveness (Garrido et al., 2015; Kreungngern and Isoleucine 2.24 1.96
Chaikham, 2016). The results show that CBBG3 has a higher gumminess Leucine 0.09 0.05
value than CBBG5 (Table 3). The literature reports that the gumminess Lysine 1.65 1.24
of a product increases when the hardness increases (Mutlu et al., 2018) Methionine 0.18 0.34
Phenylalanine 1.60 1.49
which agrees with the obtained results.
Proline 9.83 9.17
The chewiness is one of the important texture characteristics of a Serine 1.99 1.40
jelly product (Wangtueai and Noomhorm, 2009; Calvarro et al., 2016). Tyrosine 0.19 0.20
The mastication value of CBBG3 was higher than CBBG5. Like the Threonine 4.47 4.09
Valine 1.56 1.34
gumminess parameter, chewiness increases as hardness increases
Tryptophan ND ND
(Chandra and Shamasundar, 2015). Cysteine ND ND
Resilience is a measure of how the sample recovers from deformation
both in terms of speed and strength (Fermin et al., 2006). According to CBBG3: chicken by-products blend gelatin extracted at 3% of acetic acid.
CBBG5: chicken by-products blend gelatin extracted at 5% of acetic acid.
the obtained results, CBBG3 had a higher resilience than CBBG5 which
ND: Not detected.

5
O. Aidat et al. International Journal of Gastronomy and Food Science 32 (2023) 100708

glycine being more dominant followed by proline. Several studies have Table 5
reported similar results regarding the low content of alanine, leucine, Sensory evaluation of chocolate custard prepared with CBBG3 extracted gelatin
methionine, and tyrosine (Raraswati et al., 2013; Pranoto et al., 2016; Ee at different incorporation proportions (mean ± SE).
et al., 2021). The two amino acids tryptophan and cysteine were absent Type Appearance Aroma Texture Taste Acceptability
which is due to their absence in type I collagen (Schrieber and Gareis, Control 6.67 ± 0.34 7.02 ± 6.87 ± 7.44 ± 7.33 ± 0.29 a
2007; Ktari et al., 2014; Lassoued et al., 2014; Jridi et al., 2015). (CCC) b
0.27 ab 0.31 ab 0.27 a
Aspartic and glutamic acid contents were higher than previously re­ CCG 3.5% 6.09 ± 0.15 6.49 ± 6.20 ± 6.09 ± 6.24 ± 0.19 b
b
ported (Sarbon et al., 2013; Ktari et al., 2014), which may be associated 0.17 b 0.18 b 0.20 b
CCG 4.5% 7.42 ± 0.09 7.42 ± 7.31 ± 7.64 ± 7.73 ± 0.15 a
with the acid treatment. The glutamine and asparagine may have been a
0.10 a 0.15 a 0.16 a
converted to their acidic forms during collagen extraction with acetic CCG 5% 4.60 ± 0.27 4.20 ± 4.29 ± 3.44 ± 3.40 ± 0.30 c
acid. This phenomenon was similarly observed for thorny skate skin c
0.22 c 0.31 c 0.31 c
gelatin (Lassoued et al., 2014) and tuna skin gelatin (Gómez-Estaca LSD 0.66 0.56 0.69 0.68 0.68
et al., 2009). CCG: Chocolate Custard Gelatin. LSD: Least Significant Difference. *Different
letters in the same column mean significant differences among treatments (α ≤
3.5. Sensorial evaluation of chocolate custards 0.05).

The scores of sensory evaluation of chocolate custard prepared with
CBBG3 at different incorporation percentages, i.e., 3.5%, 4.5%, and 5%,
are reported in Table 5. Chocolate custard prepared with 4.5% gelatin
(CCG 4.5%) and control one (CCC) showed no difference (p > 0.05) in
likeness scores for taste, aroma, texture, and overall acceptability.
However, in terms of appearance, the panelists attributed a higher score
to CCG 4.5% than to CCC. Similarly, Zare and Lashkari (2019) found
that the most acceptable dairy dessert was produced with 4.36%. At the
highest gelatin incorporation (CCG 5%), the prepared chocolate custard
was disliked by all panelists where all the sensory attributes were under
the score of 5. It seems that a higher concentration of gelatin (>4.5%)
resulted in a more compact texture of chocolate custard altering thereby
both its appearance and mouthfeel over the others.
4. Conclusion
Chicken heads and feet blend as animal by-products obtained from
the poultry industry represents a promising alternative source of gelatin.
Based on our study, it was demonstrated that gelatin extraction with
acetic acid at 3% resulted in gelatin with superior characteristics in term
of textural profile, gel strength, and acceptable ash content. This gelatin
(CBBG3) could be used as an alternative source of mammalian gelatins
in food preparations. For all these reasons, it was selected as a substitute
for carrageenan in chocolate custard preparation. According to the
sensory evaluation, the custard with 4.5% gelatin was more liked than
the carrageenan-based commercial custard. Therefore, gelatin from
chicken by-products blend is a potential alternative to the expensive
carrageenan additive in custard preparation and probably in other food
products.
Implications for gastronomy
Carrageenan has been substituted by poultry gelatin in the prepa­
ration of the custard, a popular type of creamy culinary preparation in
many countries. Carrageenan is used as an important additive in the
formulation of custard in order to reach good eating quality. However,
the desired texture depends on which type of carrageenan is being
applied. Besides, from a cost view, carrageenan is commonly more
expensive than gelatin. Using poultry gelatin as alternative to carra­
geenan would not only overcome the price spikes of this later but also
the health and religious concerns that cause porcine or bovine gelatin to
some consumers.
The results of the present study showed that chicken gelatin substi­
tution to carrageenan in custard preparation provides a very sensory
appreciable custard. Thanks to its textural profile, bloom strength and
other techno-functional properties, chicken gelatin extracted from
poultry by-products blend (feet and heads) can bring a lot of interest for
food manufacturers and consumers.
Author statement
Omaima - Aidat: Methodology, Formal analysis, Writing - Original
draft. Louiza-Belkacemi: Methodology, Conceptualization, Investiga­
tion, Writing - Revision and editing, Supervision. Mahmoud-Belalia:
Revision and editing Mohamed khairi-Zainol: Resources, Investiga­
tion, Data curation. Humam Shaaban- Barhoum: Statistical analysis.
Declaration of competing interest
The authors declare no conflict of interest.
Data availability
No data was used for the research described in the article.
Acknowledgement
The authors would like to express their gratitude to all those who
contributed to this research, in particular the leaders of The Poultry
Group-West Algeria Mostaganem (GAO-ORAVIO). Special thanks to Dr.
Kais Djebali, Chief Engineer (Industrial Chemistry), Laboratory for
Valorization of Useful Materials (LVMU), Centre national de recherche
en science des matériaux (CNRSM) (Tunis, Tunisia). They also wish to
show their appreciation to the laboratory engineers of Milk Trans­
formation Unit S.A.R.L HODNA LAIT (M’sila, Algeria), especially to Mr.
MOUSSOUDE Mohammed, who put the laboratory at their entire
disposal to prepare chocolate cream. Thanks to the UMT for its labora­
tory facilities.
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