Trends in Food Science & Technology

Trends in Food Science & Technology 104 (2020) 14–26
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Trends in Food Science & Technology

journal homepage: www.elsevier.com/locate/tifs
Poultry gelatin: Characteristics, developments, challenges, and future

outlooks as a sustainable alternative for mammalian gelatin
Ahmadreza Abedinia a, Abdorreza Mohammadi Nafchi b, Mohammad Sharifi c,
Pantea Ghalambor d, Nazila Oladzadabbasabadi b, Fazilah Ariffin b, *, Nurul Huda e
a
Food Biopolymer Research Group, Food Science and Technology Department, Damghan Branch, Islamic Azad University, Damghan, Iran
b
Food Biopolymer Research Group, Food Technology Division, School of Industrial Technology, Universiti Sains Malaysia, Minden, 11800, Penang, Malaysia
c
Department of Food Science and Technology, Sabzevar Branch, Islamic Azad University, Sabzevar, Iran
d
Department of Food Science and Technology, Science and Research Branch, Islamic Azad University, Tehran, Iran
e
Faculty of Food Science and Nutrition, Universiti Malaysia Sabah, 88400, Kota Kinabalu, Sabah, Malaysia
A R T I C L E I N F O A B S T R A C T
Keywords: Background: Studies indicate a 30% increase in demand for all types of food and non-food grade gelatins in the
Barrier properties world. The largest volume of gelatin production comes from mammal sources (cows and pigs). Nowadays, health,
Functional properties cultural, and religious concerns have arisen due to consumption of mammalian gelatin. This has prompted
Non-mammalian gelatin
scientists to look for non-mammal sources that closely resembles the desirable physicochemical, functional, and
Poultry gelatin
Rheological properties
sensory characteristics of mammalian gelatins. Non-mammalian gelatin from poultry and fish by-products are
also gaining importance in food industry. Over the past decade, poultry production has increased by about
37.34%. Poultry by-products have good potential for replacing mammalian sources for gelatin extraction.
Scope and approach: This paper reviews in detail the fundamental properties of poultry gelatins (PG), including
rheological, functional and physicochemical properties. This study provides a perspective on their potential food,
pharmaceutical, medical and industrial applications.
Key findings and conclusions: The highest quality PG was extracted through acid treatments. PG extracted in this
way exhibited favorable rheological, fat replacement, film formation, foaming, emulsifying and sensory prop
erties, and nutritional quality. PG films showed better barrier properties than mammal-origin gelatin, making
them ideal for food and medical applications. The amino acids composition of PG, especially the imino acid and
hydrophobic amino acids, which determine the physicochemical and functional properties of gelatin, are higher
than gelatin obtained from mammals and fish that classifies them in the upper Bloom category.
1. Introduction Selvamurugan, 2019), nanoparticles as drug and gene delivery systems

(Mahmoudi Saber, 2019), a matrix for implants, in injectable drug de
Gelatin, a partially hydrolysed of collagen, is biodegradable and livery microspheres, as alive attenuated viral vaccines stabilizer agent,
exhibits good applicability in food as a texture, water-binding and in intravenous infusions, for the production of hard and soft capsules,
creamy provider, foaming, emulsifier and fining agent, colloid stabilizer plasma expanders, wound care and cosmetic fields and etc.
(Karim & Bhat, 2009), biodegradable packaging material, vehicle for Sheela (2014) suggests an increase of about 30% in global demand
encapsulating probiotic living cells (Soukoulis, Behboudi-Jobbehdar, for food and non-food grade gelatin, as was expected, it rose from 348.9
Yonekura, Parmenter, & Fisk, 2014) and micro-encapsulating agents kilo tons in 2011 to 450.7 kilo tons in 2018, where 40% of the gelatin
(M. C. Gómez-Guillén, Giménez, López-Caballero, & Montero, 2011). It output in 2011 was derived from pig skin. In the past, gelatin was
is low in calories and is used as a supplier of protein in body-building extracted from the skin and cartilage of pigs (46%) output, bovine hides
foods and as carbohydrate reducer in diabetes patients’ diets. In medi (29.4%), bones (23.1%), and other sources (1.5%) (GME, 2020).
cine, it is used in composites utilized to repair bone defects or for bone Nowadays, owing to bovine spongiform encephalopathy (BSE) and
tissue engineering (BTE) (Ranganathan, Balagangadharan, & foot-and-mouth disease (FMD) concerns, other safer sources are also
* Corresponding author. School of Industrial Technology, Universiti Sains Malaysia, 11800, Penang, Malaysia.
E-mail address: [email protected] (F. Ariffin).
https://doi.org/10.1016/j.tifs.2020.08.001
Received 27 March 2020; Received in revised form 26 July 2020; Accepted 1 August 2020
Available online 7 August 2020
0924-2244/© 2020 Elsevier Ltd. All rights reserved.
A. Abedinia et al. Trends in Food Science & Technology 104 (2020) 14–26
used for gelatin extraction. Consuming the pig skin gelatin is considered important repeating strand of Gly–X–Y triplets, where X is originally
unlawful in Judaism and Islam and beef gelatin is acceptable only if it proline, and Y is mainly hydroxyproline which stabilizes collagen
has been prepared according to the religious dietary law. World’s pop structure or in other words are Gly-Pro-Y, Gly-X-Hyp, and Gly-Pro-Hyp,
ulation of Muslims, Jews and Hindus is expected to increase about 53% with the transition temperature of the (Gly-X-Hyp)n being higher than
in the next 20 years to around 3.7 billion (PRC, 2019). These concerns that of (Gly-Pro-Y)n (Schrieber & Gareis, 2007).
have even led scientists to look for analytical methods to find ways to The quality of the amino acids in gelatin determines the unique
recognize the source of the gelatin species such as chromatographic, properties and functionality of gelatin. Therefore, this parameter gua
chemisorption, mass spectrometric, spectroscopic, immunochemical, rantees many physicochemical properties and causes to make differ
halal authenticity applying species-specific PCR (Shabani et al., 2015), ences between gelatins which are mainly owe to different amino acid
molecular techniques and proteomic methods like electrospray ioniza composition as well as proline and hydroxyproline contents (imino
tion quadrupole time-of-flight mass spectrometry (nano acid). Hydroxyproline is a derivative of proline and both are responsible
UPLCESI-q-TOF-MSE) (Yilmaz et al., 2013) which are expensive and for the stability of collagen structure by forming hydrogen bonds in its
time-consuming. Therefore, developing and offering gelatin alternatives structure. Imino acid contents are also responsible for the melting and
to nearly more than a third of world population is highly desirable for gelling temperatures of gelatin. The lower the imino acid contents, the
food industries as the global market for halal foods is growing rapidly lower the melting and gelling temperatures of gelatin, so the amount of
(Badii & Howell, 2006; Oladzadabbasabadi, Ebadi, Mohammadi Nafchi, the amino acid content distinguishes and identifies different types of
Karim, & Kiahosseini, 2017). gelatin sources (Haug, Draget, & Smidsrød, 2004). The amount of imino
According to Cheow, Norizah, Kyaw, and Howell (2007), the gelatin acid in gelatin derived from poultry skin (Mhd Sarbon, Badii, & Howell,
quality depends on its physical and chemical specifications, which are 2013) is higher than that of mammals (Eysturskarð, Haug, Elharfaoui,
strongly associated with animal species and the tissue types they are Djabourov, & Draget, 2009) and fish (Wang et al., 2015; Lin, Regenstein,
extracted from. During the past decade, there has been an intensive Lv, Lu, & Jiang, 2017). Different types of gelatin have different physi
trend in gelatin derived from non-mammalian sources, especially fish cochemical characteristics that affect the thermal and rheological
and poultry. So far, the gelatin’s yield from poultry by-products (skin, properties, including melting and gelling temperatures and Bloom
bone, scale, mechanically deboned residue, and feet) has been so low strength (Cheow et al., 2007).
that it has not reached a commercial scale (Schrieber & Gareis, 2007; FAOSTAT (2019) have reported that worldwide poultry meat pro
Araghi et al., 2015; Hazaveh, Mohammadi Nafchi, & Abbaspour, 2015). duction grew from about 92.68 million tons in 2008 (of which the share
Researchers in both industrial and academic fields have attempted to of the chicken, duck, goose and guinea fowl, and turkey were 80.84,
develop alternative routes to produce non-mammalian gelatin resem 3.83, 2.27 and 5.7 million tons, respectively) to around 127.29 million
bling unique functional properties of the mammalian ones. tons in 2018 with the share of the chicken, duck, goose and guinea fowl,
Most of the studies in the past to find novel sources for gelatin pro and turkey values of 114.26, 4.46, 2.64 and 5.9 million tonnes,
duction have been focused on fish. The effects of various extraction respectively (Table 1). The growth of the poultry industry has led to an
methods on properties of the gelatin obtained from different fish species, increase in large quantities of poultry slaughterhouse by-products and
such as black and red tilapia skin (Jamilah & Harvinder, 2002), hake and wastes. Among poultry by-products produced in the slaughtering, pro
cod skin (M. Gómez-Guillén et al., 2002), haddock and pollock (Zhou, cessing and without commercial targets, skin, feet, bone, and blood,
Mulvaney, & Regenstein, 2006), and ribbon (Norziah, Kee, & Norita, which are considered waste, are utilized to manufacture meals. Several
2014) have been thoroughly studied. Gelatin from fish has limited use by-products previously considered as waste, such as skin, feet, bones,
because of its weaker gel strength and lower stability of its gel structure blood, among others, now are recycled and used in pet foods (Padilha,
as compared with mammalian gelatin. The fishy odor is also one of the Silva, & Sampaio, 2006). Poultry slaughter waste contains about 34.2%
major drawbacks of the fish gelatin (Rafieian, Keramat, & Kadivar, dry matter which contains 51.8% crude protein, 41.0% fat and 6.3% ash
2013). Fish-sourced gelatin accounts for only 1% of the world’s annual (Kobya, Senturk, & Bayramoglu, 2006), therefore, it can possibly
gelatin production (Jan Arnesen & Gildberg, 2002). replace mammalian resources to produce gelatin. About 375,000-400,
Some studies have investigated gelatin production from poultry by- 000 tons of gelatin is produced annually worldwide (Meky, Fujii, Ibra
products. However, there is limited information on detailed character him, & Tawfik, 2019), of which only 2% (about 8 tons) extracted from
ization of physicochemical and structural properties of these types of non-mammalian sources. It is estimated that the cut components and
gelatin. Therefore, this review study aims to provide an insight into bones of the carcass make up about 7–8% of the live weight of the broiler
other aspects of PG as a suitable alternative to mammalian gelatin, with (Salminen & Rintala, 2002), which is about 9.5 million tons of suitable
an emphasis on the properties of the tissues and methods used for gelatin poultry by-product as an alternative to mammals to extract gelatin. The
extraction and the physico-chemical, functional and sensory properties PG has been shown to contain amino acids, secondary structure, and
of PG. Also, the potential difficulties and possibilities for increasing the molecular weight similar to those of mammalian gelatin. Moreover, this
industrial use of PG and further research pathway strategies are novel source would further encourage efforts to exploit untapped
discussed. available resources and recycle industrial waste (Mhd Sarbon et al.,
2. Poultry gelatin
Table 1
According to the Schrieber and Gareis (2007) collagen classification, Production of poultry worldwide and its portion (FAOSTAT, 2019).
about 27 types of collagen have been identified so far. Type I collagen is Livestock primary Production value Period of Production
derived from connective tissue such as bone, skin, and tendons. Collagen (million tonnes) years changes (%)
of type II occurs practically and widely in cartilage tissue. Type III Meat, chicken 80.84 to 114.26 2008 to 41.34
collagen is strongly related to age whereas very young skin contains up 2018
to 50% and sometime reduces to 5–10%). Other types of collagen are Meat, duck 3.83 to 4.46 2008 to 16.48
2018
available in limited amounts, which is only and often organ-specific.
Meat, goose and 2.27 to 2.64 2008 to 16.26
Gelatin is a water soluble material obtained from the fibrous protein guinea fowl 2018
collagen, which is the main component of animal bone, skin and con Meat, turkey 5.7 to 5.9 2008 to 3.38
nective tissues. Therefore, the source, collagen type and age of the an 2018
imal species are the factors that affect gelatin properties. Partial Meat, Poultry 92.68 to 127.29 2008 to 37.34
(Total) 2018
hydrolysis of native collagen forms gelatin, which is combined of an
15
2013). Table 3
Generally, gelatin can be extracted from various parts of poultry that Selected reports on extraction and characterization of alternative gelatin.
contain significant amounts of protein, including the heads and feet with Sources Reference
protein levels of 16% (Okanović, Ristić, Kormanjoš, Filipović, &
Poultry:
Živković, 2009) and bones (Cheng, Liu, Wan, Lin, & Sakata, 2008; H.; Turkey and chicken heads Du et al. (2013)
Cheng, Zhu, et al., 2008) with 23–24%. D. Liu, Lin, and Chen (2001) and Chicken heads (Gál et al., 2020), (Ee et al., 2019)
Huda, Seow, Normawati, and Aisyah (2013) reported that the collagen Chicken deboned residue (Masood & Chen, 1995), (Rammaya et al., 2012), (
contents in the chicken and duck feet were 30.74% and 28.37% (wet Rafieian et al., 2013), (Rafieian et al., 2015), (Erge
& Zorba, 2018)
basis), respectively, which are comparable to that extracted from fish Turkey deboned residue Fonkwe and Singh (1997)
waste material include skin, bone and fins with average of 50% (dry Chicken feet (Jun et al., 2000), (Almeida et al., 2012), (Rahman
basis or 33.3% wet basis) reported by Nagai and Suzuki (2000). Jun, Lee, & Jamalulail, 2012), (Almeida et al., 2013), (
Lee, and Kim (2000) studied the feasibility of using chicken feet to Almeida et al., 2013), (Choe & Kim, 2018) (
Saenmuang et al., 2019), (Santana et al., 2020)
replace cow hides, moreover, a number of studies were focused on
Duck feet (Yeo et al., 2013), (Park et al., 2013), (Y. H. Kuan,
poultry skins (Cliche, Amiot, Avezard, & Gariepy, 2003; Mhd Sarbon Nafchi, Huda, Ariffin, & Karim, 2017), (Abedinia
et al., 2013; Bichukale et al., 2018; T.-K.; Kim et al., 2020), feet et al., 2017), (Nik Muhammad et al., 2018)
(Almeida, da Silva Lannes, Calarge, de Brito Farias, & Santana, 2012; Chicken skin (Mhd Sarbon et al., 2013), (Bichukale et al., 2018), (
Yeo, Song, Ham, He, & Kim, 2013; Widyasari & Rawdkuen, 2014; Y.-H.; Aykın-Dinçer et al., 2017), (Saenmuang et al., 2019)
Duck skin (S.-J. Lee, Kim, Kim, et al., 2012), (T.-K. Kim et al.,
Kuan, Nafchi, Huda, Ariffin, & Karim, 2016; Abedinia, Ariffin, Huda, & 2020)
Nafchi, 2017), bones (Haroun, Beherei, & El-Ghaffar, 2010; Bichukale Poultry bones (Dewi Yuliani, Awalsasi, & Jannah, 2019), (Dewi
et al., 2018; Dewi; Yuliani, Awalsasi, & Jannah, 2019; D; Yuliani, Yuliani, Awalsasi, & Jannah, 2019), (Bichukale
Maunatin, Jannah, & Fauziyyah, 2019), mechanically deboned residue et al., 2018), (Haroun et al., 2010)
Marine:
(Fonkwe & Singh, 1997; Rammaya, Ying, & Babji, 2012; Rafieian et al.,
Nile perch (Lates niloticus) Muyonga, Cole, and Duodu (2004)
2013; Rafieian, Keramat, & Shahedi, 2015) and processing by-product skins and bones
(Almeida, da Silva, da Silva Lannes, de Brito Farias, & Santana, 2013; Yellowfin tuna (Thunnus (S. M. Cho et al., 2005)
Gál et al., 2020) to develop gelatin as an alternative source for albacares) skins
mammalian gelatin. Bigeye snapper skins Nalinanon et al. (2008)
Lizardfish (Saurida spp.) Wangtueai and Noomhorm (2009)
It is worth mentioning that in the year of 2017 world poultry meat
scales
had about 27.5 million tonnes of production more than 2009 (FAOSTAT, Hoki (Macruronus Mohtar, Perera, and Quek (2010)
2019), resulting in significant volume of organic waste generation in novaezelandiae) skins
different production stages. Due to the high content of organic materials, Mackerel (Scomber scombrus) Khiari, Rico, Martin-Diana, and Barry-Ryan (2011)
heads
these wastes can be hosted microorganisms’ proliferation and environ
Marine snail (Hexaplex Zarai, Balti, Mejdoub, Gargouri, and Sayari (2012)
mental problems are raised by inadequate treatment of this industrial trunculus) meat
solid waste (Alireza Seidavi, 2019; Pelizer, Pontieri, & Moraes, 2007). Cobia (Rachycentron Silva, Bandeira, and Pinto (2014)
canadum) skins
Skin of octopus (Octopus Jridi et al. (2015)
2.2. Materials and methods used for gelatin extraction vulgaris)
Comparative studies:
Tuna, frog and chicken skins Aksun Tümerkan, Cansu, Boran, Regenstein, and
Depending on the pre-treatment procedure, under acid and alkaline Özoğul (2019)
pre-treatment conditions, two types of gelatin are obtainable that are
commercially known as type-A (isoelectric point at pH ~ 8–9) and type-
B (isoelectric point at pH ~ 4–5) (M. C. Gómez-Guillén et al., 2011). Raw salts (Schrieber & Gareis, 2007). The PG has been extracted using
materials derived from fish and poultry are still new to the market. different methods, which are summarized in Table 4.
Therefore, gelatin manufacturers must precisely adjust the process and
extraction parameters to obtain a product with maximum desired 2.2.1. Acid treatment
properties (see Table 2). In the acidic process, an acid solution is used to collagen hydrolysis,
Table 3 lists the various available reports on extraction and charac which is product of this process called type A gelatin. Pigskins are the
terization of poultry and marine gelatin as alternative sources. most commonly used raw material for this process, which are treated
For PG, as the normally young poultry are slaughtered, the material over a period of 10–45 h. Acidic treatment causes collagen swelling to
can be pre-treated using the acid process. The poultry skins contain a increase the efficiency of gelatin extraction throughout thermal hydro
large volume of fat and low concentration of collagen and it is preferred lysis (Damrongsakkul, Ratanathammapan, Komolpis, & Tanthapa
to use other organs such as feet. The poultry bone is not demineralized nichakoon, 2008). To ensure the warm-water solubility of the collagen,
before conditioning, so during the extraction concentration of salts is hand-sized pieces of skin should be soaked in 2–4% dilute sulphuric or
high and a precipitation step after extraction is necessary. Additional hydrochloric acid at room temperature for 24 h. Due to the mechanical
steps, such as ultrafiltration and deionization, also help remove excess agitation involved in this process, the fat is separated and is easily
removed as it floats onto the surface (Schrieber & Gareis, 2007).
Swelling attributes and further solubilisation of collagen are intensely
Table 2
Raw material conditioning (Schrieber & Gareis, 2007). affected by the type and concentration of acid used according to the
durability of some of inter-relations between collagen chains, which
Raw material type Raw material conditioning
causes the variance in the distribution of molecular weight in the
Acid Alkali resulting gelatin.
Bones * * Phosphoric and organic acids are additionally reasonable for this
Cattle hide splits * * preparation step, yet they are increasingly costly and adversely influ
Pigskin splits * * ence the smell and the flavour of the final product. However, Dewi
Pigskin *
Fish skin *
Yuliani, Maunatin, Jannah, and Fauziyyah (2019) obtained gelatin with
Poultry skin * favorable physicochemical properties from broiler chicken bones using
Poultry feet * different concentrations and treatment times of 8–10% phosphoric acid.
16
Table 4 Table 4 (continued )

Procedures used to extract poultry gelatin. Poultry gelatin Preparation and pre- Extraction Reference
Poultry gelatin Preparation and pre- Extraction Reference treatment procedure
treatment procedure
water (1:6, w/v) at NaOH in ratio of
Chicken feet Washing whit Extracting in 4% (Almeida et al., 30 ◦ C for 10 min, 3 1:6, w/v for 3 h,
gelatin (CFG) chlorine (2 ppm of acetic acid 2013), (Almeida times washing until
active Cl2) water solution at 60 ◦ C et al., 2012) neutralize pH,
for 4 h extracting in DW
CFG Washing, soaking in Neutralizing by (H. Y. Kim, Song, for 12 h at 65 ◦ C
0.1 N HCl at 18 ◦ C washing, then et al., 2012), ( with a ratio of 1:2
for 24 h with a ratio samples were Choe & Kim, (w/v). Enzymatic
of 1/10 (v/w) of placed in 2018) procedure were
tissue/solution polyethylene started with 0.2
bags, vacuum- M acetic acid
packaged and containing pepsin
heating in water 15 units/g in 1:10
bath at 75 ◦ C or (w/v), then
65, 75, 85, and stirring at 4 ◦ C for
95 ◦ C for 2 3 adjusting pH to
CFG Washing, soaking in Rinsing in tap (Almeida et al., 7.5, then heating
4.0% and 0.318%– water and 2013), (Santana for 12 h at 65 ◦ C.
3.682% acetic acid extracting with et al., 2020) All obtained
for 16 h and 1–8.4 h DW (1:2 w/v) for gelatin were
6 h at 55C and filtered and
43.3 ◦ C–76.8 ◦ C. freeze-dried.
CFG Cleaning at 100 ◦ C Soaking in HCl (Bichukale et al., Chicken skin Defatted dried Rinsing with DW (Said & Sarbon,
for 40 min to remove 4% with ratio 1:6 2018), (Rahman gelatin (CSG), samples soaked in and treating with 2020), (N
skin, fat and cuticles, with changing & Jamalulail, black-bone NaOH (0.15% w/v) 0.15% (v/v) Suderman &
then drying at 50 ◦ C every three days 2012) chicken feet for 40 min then H2SO4 and 0.7% Sarbon, 2019), (
for 18 h for 9–12 days, and skin mixture was (w/v) citric acid Bichukale et al.,
soaking osein in gelatin (CSG, centrifuged at room solution, washing 2018), (
0.2 M NaOH BCFG and temperature. with DW and Saenmuang
(1:10 w/v) for 20 BCSG), broiler centrifuging, et al., 2019), (
days with skin gelatin then extracting in Aykın-Dinçer
changing every 3 (BSG) DW at (45 ◦ C) et al., 2017) (
days, then overnight Mhd Sarbon
soaking in DW for et al., 2013)
24–48 h until pH Chicken deboned Drying at 39 ◦ C in Washing, soaking (Rafieian et al.,
= 5–7 and residue gelatin oven, then defatting in 1% (w/v) 2013), (Fonkwe
heating at 60 ◦ C (CDRG) using hexane NaCl, treating & Singh, 1997)
for 5 h (HCl (1:2) (w/v)
Duck skin gelatin Washing, soaking in Washing until the (S.-J. Lee, Kim, for 24 h), rinsing
(DSG) 2% NaOH or 0.1 M pH ~ 7 and Kim, et al., 2012) until pH ~ 7;
acetic acid with a extracting with then extracting at
skin/solution of 1:7 distilled water varying
(w/v) (DW) for 3 h at temperatures and
65 ◦ C; skin/water times
1:5 (w/v) Mechanically Washing, defatting, Washing, Rammaya et al.
DSG Washing, adjusting Extracting using (T.-K. Kim et al., deboned washing, extracting in DW (2012)
pH 1 to 14 with 0.1 N the following 4 2020) chicken meat demineralizing (3% at pH 4 under
HCl, 0.1 N NaOH, extraction gelatin HCl for 24 h), constant shaking
and DW for 24 h, methods for 10 (MDCMG) washing until the for 120 min at 25
washing for 48 h and min: water bath pH ~ 4, then soaking ◦
C with ratio
sample pH 1 was (60 ◦ C), in 4% NaOH (1:5 w/ (2.5:1) solution/
used for extraction sonication (60 ◦ C v) for 72 h MDCM residue
because of highest with 40 kHz), MDCMG Cutting, grounding, Using RSM with Erge and Zorba
rate of swelling. superheated defatting with DW at these raging of (2018)
steam (steam 35 ◦ C for 1 h, parameters:
temperature of washing, filtering, NaOH
150 ◦ C), and demineralization in (1.8–4.2%),
microwave 3 g/100 mL HCl extraction
(2450 MHz and solution for 24 h at temperature
200 W power), 10 ◦ C, washing 3 (58–82 ◦ C) and
then filtering and times and then extraction time
coagulating at 4 filtering (30–250 min)
◦
C for 12 h and Chicken head Mincing, frizzing, Dried matter was Gál et al. (2020)
freeze drying gelatin (CHG) thawing, soaking in ground and
Duck feet gelatin Washing and soaking Neutralizing by Yeo et al. (2013) 0.1% NaOH by conditioned by
(DFG) in 0.1 N HCl in 5 washing for 48 h shaking for 45 min proteolytic
times (v/w) for 24 h (pH 5.5), then (4 times), rinsing, enzyme: mixing
extracting by the drying at 35 ◦ C, with DW for 15
ratio of 1:1 of defatting (petroleum min, adjusting
(duck feet: DW) ether and ethanol pH, adding
at 75 ◦ C for 6 h (1:1)), then filtering proteolytic
DFG Thawing, cleaning, Treating with Abedinia et al. and purified collagen enzyme of 0.4%
mincing and then 0.05 M acetic (2017) material left to dry or 1.6%, shaking
washing with tap acid or 0.1 M for 24 or 72 h,
then, filtering,
(continued on next page)
17
Table 4 (continued ) acids for treatment, electrolytes affect the biophysical properties
Poultry gelatin Preparation and pre- Extraction Reference (swelling, solubility, gelatin, viscosity and water-binding capacity) of a
treatment procedure protein at various ionic qualities and pH amounts. Saline particles may
rinsing, mixing
either tie straightforwardly to the peptide spine of collagen, or influence
with DW, heating collagen collapsing in a roundabout way by collaborating with struc
to 80 ◦ C, turally bound-water molecules. ‘Lyotropic hydration’ is described as a
inactivating hydration arising from the disruption neutral salt ions with non-ionic
enzyme, then
bonds such as hydrogen bonds of collagen. Therefore, lyotropic agents
extracting at 95
◦
C, then drying at can modify the structure of water about collagen molecules, interrupt
45 ◦ C for 48 h internal hydrogen bonds, or interact with internal hydrophobic bonds by
Mechanically Treating with 1% Washing in Fonkwe and direct binding at similar destinations of the protein chains (Giménez,
deboned NaCl at pH of 10.7 running tap Singh (1997) Turnay, Lizarbe, Montero, & Gómez-Guillén, 2005). For example, the
turkey residue for 30 min, then water for 15 min,
gelatin pretreating by 5% then extracting in
use of NaCl (1.5% w/w) in fish gelatin extraction (Sow & Yang, 2015)
(MDTRG) H2SO4 for 24 h DW with 1:3 (v/ was reduced textural properties and gel strength and adding (NH4)2SO4
w) at 55 ◦ C for 5, and NaH2PO4 to gelatin (Sarabia, Gómez-Guillén, & Montero, 2000) was
extracting the improved the melting point. They was reported that the reasons for these
residue at 70 ◦ C
changes are due to the effect of salts on the change, loss of molecular
with 1:3 (v/w)
DW for another 5 order or modification of gelatin structure.
h, then heating T.-K. Kim et al. (2020) by examining the swelling rate of duck skin
the residue at 85 samples exposed to different pH levels, from 1 to 14, concluded that pH
◦
C 1 is the most appropriate treatment for extracting DSG due to the high
Bird bones Cleaning, Treating with Haroun et al.
gelatin (BBG) demineralizing using H2SO4 to a pH of (2010)
level of collagen type A in the duck’s skin. The remarkable result was
3% HCl at room 2.5–3.0 for 16 h, that there was no significant difference between skin swelling between
temperature for heating, then pH 1 and 11 treatments. Yeo et al. (2013) conducted a study to evaluate
9–12 days, with the filtering using the effects of DFG, as a fat alternative, on the quality of low-fat sausages.
liquor changing of activated carbon
Extraction was conducted by soaking in 0.1 N HCl solutions for 24 h.
every 3 days column, pH
adjusting to 5.0 Extraction was conducted at 75 ◦ C for 6 h. The addition of DFG improves
and drying cooking properties of low-fat sausages. Almeida et al. (2012) and San
extracted gelatin tana et al. (2020) characterized the CFG by FTIR spectroscopy. They
at 40 ◦ C demonstrated that CFG type A has very good nutritional quality
Chicken bone Soaking in NaOH 5% The osein was (Dewi Yuliani,
compared to the commercial gelatin. H. Y. Kim, Lee, and Kim (2012)
gelatin (CBG) for 2 days 1:4 (v/v). extracted by Awalsasi, &
Osein was water in 55, 65, Jannah, 2019) have observed the positive effect of CFG and wheat fibre content on the
neutralized by tap and 75 ◦ C for 4 h, quality of semi-dried chicken Jerky (an old meat product which pre
water and acetic acid then drying, pared with drying in the steps of 55, 60, 73 and 75 ◦ C for 30, 150, 90 and
5%. gelatin
10 min, respectively). The CFG was obtained by 0.1 N HCl, pH = 1.31
purification by
ammonium treatment. Choe and Kim (2018) extracted CFG at four different tem
sulphate peratures using HCl at pH 2 and compared the physicochemical prop
(40–70%) erties of their gels with a mixture of wheat fiber (WF). They suggested
precipitation, applying of CFG blending with WF in meat products. Almeida et al.
centrifuging then
(2013) proved that the extraction of CFG is economically feasible using
dialysis.
CBG Washing, grounding, Extraction was (Dewi Yuliani, 4% acetic acid at 60 ◦ C, and it has very good nutritional and sensorial
degreasing (water: conducted in DW Awalsasi, & qualities. Sompie, Siswosubroto, Rembet, and Ponto (2019) studied the
30 min at 70 ◦ C), (1:4 (w/v) at 55 Jannah, 2019) rheological properties and total bacteria of chicken leg skin gelatin
washing, drying (25 C–75 ◦ C).
(CLSG) extracted using HCl and acetic acid. Their findings showed that
◦
◦
C), soaking Treated bones
(phosphoric acid were extracted at
applying acids could reduce total bacteria in the final product (1.6–3.4
8–10% (w/v) 1:4 55 ◦ C for 4 h, × 10 4 comparing other results 5.7 and 4.0 × 10 9 CFU/g).
(w/v) for 12 h and then filtering.
24 h, washing and The procedure 2.2.2. Alkali treatment
drying at 25 ◦ C was repeated to
In the alkaline media, gelatin is prepared from boned materials,
the remained
bones at 65 ◦ C treated with alkali, with or without agitation. The conditioning process
and 75 ◦ C for 4 h. takes quite long times depending on the temperatures and concentra
All of the filtrates tion. For example, using sodium hydroxide solution at 25 ◦ C takes
were mixed, then
several weeks to form supersaturated milk of lime (GME, 2020). Agita
filtering and
drying.
tion consistently accelerates the conditioning process. The most
important qualitative factors of gelatin, including Bloom and viscosity,
are directly influenced by the concentration, time and duration of
Bovine hide splits are ordinarily treated with acid for 48–72 h. It must be exposure to alkaline treatment. Tougher conditions result in higher
noticed that ensuing the acid conditioning, the extraction, likewise, is viscosity gelatin production (Mad-Ali, Benjakul, Prodpran, & Maqsood,
completed in an acid condition. After this treatment, pH is expanded to 2016). Although the process with lime milk would seem inefficient at
2–4 by including alkali. As a result of the reactions, salts are formed first glance, it shows various technological advantages. During the
which are then cleaned out over a time of 24 h using water. During the treatment, which may last for several months, mucopolysaccharides,
extraction, the firmness to viscosity proportion is balanced by the pH, sulphur-containing compounds which are non-protein materials and
extraction time, temperature just and speed. The producer must alter the non-collagenous proteins, are dissolved (D.-C. Liu, 2002). For example,
ideal proportion between the ideal quick extraction and undesired when using calcium hydroxide for treatment, this mild treatment also
chemical/thermal hydrolysis of the gelatin (Almeida et al., 2013). purifies the raw material while preventing loss of efficiency. If treated
According to Asghar and Henrickson (1982), when using organic with too much alkali, the collagen dissolves in cold water. Thus, by
18
washing off the raw materials, the collagen is also washed off, reducing categories with their recommended level and Bloom strength. These
gelatin efficiency (Schrieber & Gareis, 2007). important attributes are influenced by several parameters such as mo
Abedinia et al. (2017) investigated the effects of different pre lecular weight and distribution, gelatin solution concentration, gel cure
treatments on yield and composition of extraction, physicochemical, time and temperature, concentration of H+ ions and salt content.
and rheological properties of DFG. Rheological analysis of alkaline So far, several studies have been conducted to extract and evaluate
gelatin indicated that almost the same elastic modulus and loss modulus the collagen and gelatin characteristics of poultry. These studies focus
with commercial bovine gelatin. Dewi Yuliani, Awalsasi, and Jannah on certain purposes such as the feasibility of collagen and gelatin
(2019) extracted CBG by NaOH and characterized it. Although alkaline extraction from poultry and determination of physicochemical proper
extraction and subsequent purification and dialysis treatment was not ties (Almeida et al., 2013; Huda et al., 2013; Rafieian et al., 2015; Dewi;
successful in comparison with other methods due to the amount of Yuliani, Awalsasi, & Jannah, 2019; Gál et al., 2020; T.-K.; Kim et al.,
protein extracted, but, the accompanying purification step in this extract 2020), rheological properties of PG (Mhd Sarbon et al., 2013; Abedinia
can eliminate large quantities of small peptide fragments and leave a et al., 2017; Yasin, Babji, & Norrakiah, 2017; Santana et al., 2020), as
large amount of α- and β-chains in the product. The RSM study of Erge well as its emulsifying and foaming properties (H. Y. Kim, Song, et al.,
and Zorba (2018) showed that the most effective parameters on yield 2012; Du, Khiari, Pietrasik, & Betti, 2013; Rasli & Sarbon, 2015; Chakka,
extraction and gel strength were extraction temperature and time. Their Muhammed, Sakhare, & Bhaskar, 2017), bioactive activity (S.-J. Lee,
results indicated the optimum condition of the parameters were defined Kim, Kim, et al., 2012; S.-J. Lee, Kim, Kim, et al., 2012; Wan Omar &
as NaOH concentration of 2.9–3.4%, extraction temperature ranging Sarbon, 2016; Said & Sarbon, 2020), fat replacement ability (Yeo et al.,
from 76 to 82 ◦ C and 105–183 min of extraction time. Saenmuang, 2013; Almeida & Lannes, 2017), sensory quality properties (H.-W. Kim
Phothiset, and Chumnanka (2019) characterized the BCFG and BCSG et al., 2014; Nik Muhammad, Huda, Karim, & Mohammadi Nafchi,
extracted using NaOH treatment and compared with commercial bovine 2018) and film-forming ability (Haroun, Beherei, & El-Ghaffar, 2010;
gelatin (BG). Results indicated that obtained gelatins had two distinct J.-H.; Lee, Lee, & Song, 2015; Nazmi, Isa, & Sarbon, 2017; Abedinia,
α-chains and high Bloom values along with lower color properties. Ariffin, Huda, & Mohammadi Nafchi, 2018).
2.2.3. Enzyme aid treatment

Use of proteolytic enzymes is an alternative approach to acid 2.2.1. Chemical and structural properties
method. As demonstrated by Abedinia et al. (2017) on poultry source
and Abdelmalek et al. (2016) on marine source, using 15 Units pepsin/g The twenty types of amino acids found in nature can be divided into
tissue in gelatin extraction increases the yield of gelatin, but, SDS-PAGE three groups:
evaluation indicated high band intensity for α- and β-components, so
that, the major components were α1-and α2-chain bands (≈100 kDa each a) Hydrophobic or non-polar, including glycine, alanine, valine,
one). Low-molecular-weight peptides were obtained in this extraction, leucine, isoleucine, methionine, phenylalanine, tryptophan and
caused by the ample cleavage of peptides via enzyme during gelatin proline.
preparation. Thus, the size of the polypeptide chains was influenced by b) Hydrophilic or polar including serine, threonine, cysteine, tyrosine,
enzyme, which is the most important factor affecting rheological asparagine and glutamine.
properties. c) Hydrophilic electrically charged:
Pepsin has been mostly applied in studies to isolate collagens from o Positive-charged (histidine, arginine and lysine).
many tissues (J. Cao, Duan, Liu, Shen, & Li, 2019; Hamdan & Sarbon, o Negative-charged (glutamic acid and aspartic acid).
2019; S. Cao, Wang, Xing, Zhang, & Zhou, 2020). In specified condi
tions, it can extract a fairly high amount of the triple-helical molecule Imino acid contains both carboxyl and imino (CNH) functional
intact shape of collagenous material. For example, depending on pepsin groups and proline is classified as an imino acid. (Hanani, 2016). Table 6
concentration and substrate ratio/enzyme, up to 80%–90% of bovine gives a brief of the amino acid composition of different kinds of PG.
tendons collagens can be extracted (Ju, Liu, Zhang, Liu, & Yang, 2020). Generally, collagens in poultry sources show a wider variety in amino
Ye et al. (2020) evaluated the physicochemical composition of gelatin acid compositions than those of mammalian collagens. Their hydroxy
obtained from collagen hydrolysis of chicken bones at different tem proline and proline contents are higher than those in mammalian col
peratures and times. The results of hydrolysis degree and SDS-PAGE lagens, as well as, glycine. In general, the imino acid content of PG is
analysis showed that the average molecular weight of collagen hydro comparable to that in mammal’s gelatin. The raw material from which
lyzes at 50 and 70 ◦ C were higher than hydrolysates at 90 ◦ C, which gelatin is extracted determines the amount and sequence of amino acids
indicates the re-formation of the three helix protein structures in their in the final product. Hydroxyproline amino acid content represents the
transport on chains. FTIR analysis confirmed that β-sheet decreased and percentage of gelatin extraction in the process (Nalinanon, Benjakul,
random coil increased significantly (P < 0.05). Gelatin hydrolysates Visessanguan, & Kishimura, 2008). The results showed that alcoholic
obtained at 90 ◦ C for 30 min showed better properties (melting point, polar amino acids (serine, threonine and tyrosine) play an important
textural and microstructural properties) compared to samples treated at role in determining the gel strength. Serine amino acid content (with a
50 and 70 ◦ C. Enzymes can be used to prepare active gelatin hydroly
sates as antioxidant activity agent (Ketnawa, Martínez-Alvarez, Benja Table 5
kul, & Rawdkuen, 2016). The mechanism of gelatin radical scavenging The multifunctionality of gelatin in food production (Schrieber & Gareis, 2007;
is due to the presence of residual free amino groups (NH2) in its struc Ahmad et al., 2017).
ture that form a stable macromolecule with ambient free radicals and Application Concentration and function Bloom
form ammonium groups by adsorption of hydrogen ions (N Suderman & strength (g)
Sarbon, 2019). Gelatin desserts and gummy 7–9% as gel formation 175–275
bears
Meat products, sausages, broths 1–5% as emulsion stabilizer 175–275
2.3. Chemical, physicochemical, and functional properties of poultry
and canned meats and binding agent
gelatin Dairy products 0.2–1.0% as syneresis stabilizer 150–250
Frozen foods 0.1–0.5% reducing water loss 200–250
In terms of gelatin application in food industry, the most important agent
properties of gelatin are strength of gel, viscosity, setting and melting Beverage industry 0.002–0.015% as clarifying 100–200
agent
temperatures. Table 5 shows the uses of gelatin in different food
19
Table 6 of the gelatin. Over time, this network becomes an infinite network
Amino acid content of poultry gelatins compared to mammalian gelatins (%). (Bohidar & Jena, 1993). Since the bonds involved in the gelation process
Amino Porcine Duck b
Chicken Turkey Duck Chicken are physical (hydrogen bonds and van der Waals) they give this process
acids a c d
feet e feet f the nature of thermal reversibility. The source, breed and age of animals;
Ala 8.3 9.84 10.08 12.99 8.12 10.11 size, number, molecular weight and breakdown position of peptide
Arg 8.5 7.87 5.57 5.74 5.67 ND chains; the number, type and concentration of amino acid residues
Asp 6.0 4.81 g 2.11 5.82 2.72 i 4.24 present in gelatin are important factors in the rheological properties of
Cys 0.2 0.02 0.16 ND ND ND gelatin. Gel strength and melting point are a direct function of the mo
Glu 10.5 10.63 5.84 8.66 5.53 j 3.13
h lecular weight as well as the complex interactions that are determined
Gly 20.2 26.04 33.70 35.14 29.81 31.51 by the amino acid composition and the ratio of α/β chains present in
His 0.8 0.97 0.30 0.58 0.7 ND gelatin (S. Cho et al., 2004). According to Schrieber and Gareis (2007),
Hyl 1.2 ND ND ND ND 2.25 strength of gel is largely dependent on the fraction with a molecular
Hyp 10.8 12.78 12.13 ND k 10.7 9.24
weight of approximately 100,000 g mol− 1. With the same reasoning
Ile 1.3 1.10 1.15 2.35 1.14 ND
Leu 2.9 2.70 2.63 1.36 2.5 3.47 Aykın-Dinçer, Koç, and Erbaş (2017) proved that the broiler skin gelatin
Lys 4.0 2.88 4.66 2.99 1.75 2.41 (BSG) had low viscosity (1.35 cP) as well as low gel strength (166.6 g)
Met 1.1 1.34 0.07 0.89 1.47 1.12 values. H. Liu, Li, and Guo (2008) demonstrated that the gelatin gel
Phe 2.1 2.19 1.77 1.65 1.84 3.16 strength characteristic was strongly dependent on the amount of α-chain
Pro 13.4 8.84 13.42 13.87 10.68 17.6
Ser 3.6 2.50 2.20 2.57 3.75 1.43
in gelatin. Given that a high proportion of peptides with molecular
Thr 1.9 2.94 1.01 2.10 2.37 ND weights higher or lower than α-chains can decrease gel strength, it can
Trp ND ND 0.04 ND ND 1.23 be concluded that the higher the α-chains in the gelatin protein pattern,
Tyr 0.8 0.72 1.22 0.43 0.46 0.96 the higher the gel strength. The amount of Bloom used to express the gel
Val 2.4 1.85 1.94 2.24 2 1.38
strength of commercial gelatin which is the amount of weight (in grams)
Imino 24.2 21.62 25.55 ND 21.39 26.5
acid required to compress the surface of a thermo stated standard under
a
standard conditions by a specified plunger to a specified depth
Porcine skin gelatin (type A commercial) (Eysturskarð et al., 2009).
b
(Schrieber & Gareis, 2007). The Bloom for commercial gelatin ranges
DSG extracted by 0.1 M (0.6%) acetic acid (S.-J. Lee, Kim, Kim, et al., 2012).
c from 100 to 300, whereas the range between 200 and 250 is most
CSG extracted using NaOH (0.15% w/v) then 0.15% (v/v) H2SO4 (Mhd
favorable.
Sarbon et al., 2013).
d
MDTRG extracted by 5% HCL at 70 ◦ C (Fonkwe & Singh, 1997). Table 7 shows rheological properties (Bloom number, melting, gel
e
DFG extracted using (4%) acetic acid (Y. H. Kuan et al., 2017). ling point and viscosity) of various PG as reported in the literature. PG
f
DFG extracted using 1.5% acetic acid (Chakka et al., 2017). typically has a Bloom value ranging from 120 to 831 (tested under the
g
Aspartic acid. conditions of the standard Bloom test) which is categorized in term of
h
Glutamic acid. high (>200 g) Bloom, while a ranging from as low as zero to 270 has
i
Asp + Asn. been reported for fish gelatins and typical Bloom values ranging from 70
j
Glu + Gln. to 110 for cold-water gelatins (Karim & Bhat, 2009) of course, with an
k
Du et al. (2013) reported the amount of 11.2% for hydroxyproline content in exception of Bloom value as high as 426 has been reported for a
type B gelatin extracted from turkey head.
warm-water yellowfin tuna skin (S. M. Cho, Gu, & Kim, 2005),
compared to the Bloom values for bovine or porcine gelatin, which have
free hydroxyl group) was higher in non-gelling gelatin and threonine Bloom values of 200–240. Gelatins extracted from mechanically
and tyrosine content in gelatin with good gel forming properties were deboned chicken or turkey residue have been reported to exhibit highest
higher than non-gelling gelatin. This is due to the presence of free hy Bloom value in PG (Fonkwe & Singh, 1997; Rafieian et al., 2013;
droxyl groups that can bond with water molecules and negatively affect Rafieian et al., 2015). Such high gel strength characterizes only those
the strength of the gel (Jan Arnesen & Gildberg, 2002). gelatins extracted from mechanically deboned poultry residues. For
Overall, in conducted studies, gelatins from chicken have higher example, Bloom values 260, 294, 338, 355, 439, 520 and 831 have been
concentrations of imino acids compared to mammalian gelatins and reported for duck skin, chicken by-products gelatin, mechanically
duck gelatins (such as Pekin duck), among which, hydroxyproline con separated turkey meat gelatin, chicken head gelatin, chicken bone
tent of duck gelatins is higher than mammalian and chicken gelatins, gelatin, chicken deboned residue gelatin, and mechanically deboned
but, proline content of chicken gelatins is higher than mammalian and turkey residue gelatin respectively (Almeida et al., 2013; Du, Keplová,
duck gelatins. The proline and hydroxyproline contents are approxi Khiari, & Betti, 2014; Rafieian et al., 2015; Ee et al., 2019; Dewi; Yuliani,
mately 21–28% for CFG (Chakka et al., 2017), 22–30% for mammalian Awalsasi, & Jannah, 2019; T.-K.; Kim et al., 2020).
gelatins (Haug et al., 2004), 22–25% for warm-water fish gelatins Studies have shown that the most important difference in the gel
(tilapia and Nile perch) (Jamilah & Harvinder, 2002; Weng, Zheng, & strength of different gelatins is their diversity in the amount of imino
Su, 2014), and 17% for cold-water fish gelatin (cod) (M. Gómez-Guillén acids, which are influenced by their amount in collagen present in
et al., 2002). different species as well as the extraction conditions. Studies by Badii
and Howell (2006) and Montero and Gómez-Guillén (2000) conclude
2.2.2. Rheological properties that another factor that even plays an important role in the development
Gelatin’s rheological and mechanical attributes play a significant of physical properties, especially gel strength, is the amount of hydro
role in the development of the product and product specifications in the phobic amino acids (Ala, Val, Leu, Ile, Pro, Phe, and Met). The results
food, medicinal and biomedical industries. Gelatin is categorized as a showed that the amount of these amino acids in the non-gelling gelatin
physical gel, i.e., the interactions or bonds between the chains that make (cod gelatin) was low. Thus, the hypothesis of a direct relationship be
up the material are physical in nature (van der Waal’s interactions and tween the amount of hydrophobic amino acids and the gel strength is
hydrogen bonds, with an E ≈ 2 kcal/mol). If we cool a homogeneous confirmed. The extraction conditions may influence the distribution and
gelatin solution (gelatin in the range of one to fifty percent constitute composition of hydrophobic amino acids which markedly affect the
homogeneous gel) to below the sol-gel transition point, the collagen-like temperature of gelling and Bloom. For example, applying higher
helices are re-formed and the three-chain helix forms (Djabourov, extraction time (12.05 h) has been stated to end in the lower Bloom
Lechaire, & Gaill, 1993). As a result, the solution undergoes a values for mechanically deboned chicken residue (Rafieian et al., 2013),
three-dimensional structure that guarantees the strength and elasticity demonstrating that as the extraction time for hydrolysis affects the
20
Table 7
Gel strength, melting and gelling points and viscosity of various poultry gelatins.
Gelatin type Concentration Gel strength Gelling point Melting point Viscosity Reference
(%) (g)n (◦ C) (◦ C)
Method and viscosity value (in

original unit)
CFG a 10 264.3 NR a 26.7 Brookfield at 40 ◦ C, 4.96 cP Rahman and Jamalulail (2012)

CFG 4 ~240 to 487 NR 36.38 to 38.5 HAKKE viscotester at 35 ◦ C, Choe and Kim (2018)
5.12–7.61 Pa s
CSG b 6.67 270.5 NR 39.83 NR (H.-W. Kim, Song, et al., 2012)
MDCRG c 6.67 526 NR NR Oswald at 60 ◦ C, 5.85 Pa s Rafieian et al. (2013)
MDCMG d 6.67 281 to 818 25 33.7 NR Erge and Zorba (2018)
MDTRG e 6.67 831 NR NR 1%, Oswald, 0.720 dl/g Fonkwe and Singh (1997)
CSG 6.67 355 24.88 33.57 Rheometer at 40 ◦ C, 150 ml/g Mhd Sarbon et al. (2013)
CFG 6.67 294.7 NR NR NR Almeida et al. (2013)
THG f 6.67 368.4 NR NR NR Du et al. (2013)
CHG g 6.67 247.9 NR NR NR Du et al. (2013)
CHG 6.67 113 to 355 NR 34.5 to 42.2 Oswald at 60 ◦ C, 1.41 to 9.45 mP Gál et al. (2020)
MSTM h 6.67 338.4 27.0 to 27.9 31.4 to 34.5 NR Du et al. (2014)
CDRG i 6.67 520 NR NR Oswald at 60 ◦ C, 55.5 mP Rafieian et al. (2015)
CSG 6.67 NR 23.68 32.64 NR Rasli and Sarbon (2015)
CFG 6.67 119.2 to NR NR NR Chakka et al. (2017)
204.3
CFG 6.67 79.23 and 185 NR NR NR Widyasari and Rawdkuen (2014)
CFG 6.67 294.8 NR NR NR Santana et al. (2020)
DFG j 6.67 and 10 209 to 334.3 20.5 to 26.65 27.8 to 36.4 10%, Brookfield at 40 ◦ C, 0.64 P (Abedinia et al., 2017), (Y. H. Kuan et al.,
2017)
CHG 6.67 38.6 to 355.7 25.8 to 26.0 30.8 to 32.3 NR Ee et al. (2019)
DSG k 6.67 210 to 260 NR 31.2 to 33.8 Brookfield at 35 ◦ C, 56.9–77.8 (T.-K. Kim et al., 2020)
mPa s
BCSG and 6.67 239 to 263.5 NR NR NR Saenmuang et al. (2019)
BCFG l
CLSG m 6.67 75 to 85 NR NR Brookfield at 40 C, 7 to 8.9 cP
◦
Sompie et al. (2019)
Bovine gelatin 6.67 218 to 240 24.5 28 to 29 Brookfield at 60 ◦ C, 9.8 cP (Cheow et al., 2007), (Mohtar et al., 2010)
Porcine 6.67 216 NR 29.1 Brookfield at 60 ◦ C, 5 cP (Jan Arne Arnesen & Gildberg, 2007), (
gelatin Mohtar et al., 2010)
a Chicken feet gelatin
.
b Chicken skin gelatin
.
c Mechanically deboned chicken residue gelatin
.
d Mechanically deboned chicken residue gelatin
.
e Mechanically deboned turkey residue gelatin, solution of 7.14% was used for Bloom test
.
f Turkey head gelatin
.
g Chicken head gelatin
.
h Mechanically separated turkey meat
.
i Chicken deboned residue
.
j Duck feet gelatin
.
k Duck skin gelatin
.
l Black-bone chicken feet and skin gelatins
.
m Chicken leg skin gelatin
*Not reported.
n
The difference in the values obtained from the results of Bloom strength depends on the temperature and time of extraction, the strength of the chemical treatment
used in the extraction, the texture from which the gelatin is extracted which can affect the amount of product imino acids (the most important factor influencing the
amount of Bloom), method applied for Bloom determining and gelatin concentration in test.
degree of cross-linking of collagen, it subsequently has a noticeable ef similar to those in mammalian and its viscosities are relatively higher
fect on the gel formation capacity. One of the most prominent features of (Mhd Sarbon et al., 2013; Rafieian et al., 2015). The representative
gelatin that makes it a desirable material for food and pharmaceutical values of the gelation and melting points of the poultry by-products are
use is the melting properties of gelatin in the mouth or in the range of 20–28 ◦ C and 26.7 to 34.5 ◦ C, respectively, whereas those
melt-in-the-mouth property (usually lower than human body tempera corresponding temperatures are in the range of 20–25 ◦ C and 28 to 31
ture) which is due to the prominent properties of gelatin dissolvability in ◦
C, respectively, for bovine and porcine gelatins, which demonstrates
water and capacity to make thermally reversible gels. The rheological the effect of gelatin origin (Table 7). Du et al. (2013) compared the
attributes of the thermoreversible gels are essentially a function of the rheological properties of turkey and chicken gelatin to mammalian
temperature below the melting point and the gelatin concentration gelatins. The results showed that the elastic modulus G′ (which mainly
(Zhou et al., 2006). Collagen transformation to gelatin is deciphered as describes the viscoelastic properties) in turkey gelatin was higher than
the crumbling of the helical structures into irregular coils. Upon cooling, the critical concentration of CHG but comparable to mammalian sam
simultaneously while they endeavor to change the initial structure ples. The rheological, physicochemical and structural properties of the
(Mackie, Gunning, Ridout, & Morris, 1998), the irregular coils experi gelatin extracted from chicken skin showed a significant difference (p <
ence a coil to helix move (Kuijpers et al., 1999). The strength and 0.05) in the melting temperature of the chicken gelatin (33.57 ◦ C) with
integrity of the gel is the result of the three-dimensional structure ob that of the gelatin extracted from the bovine skin (31.55 ◦ C), but the
tained from this process. gelation temperature of both gelatin was about 24 ◦ C (Mhd Sarbon et al.,
Although a wide range of melting and gelling points has been re 2013). Avoiding widespread degradation of the peptide structure at all
ported for the PG, but the gelling and melting points of PG are relatively stages of the extraction process should be considered as an important
21
principle in this process as extensive changes in this structure lead to a Rasli and Sarbon (2015) stated that the reason for the significantly
significant reduction in the resulting gel strength. M. Gómez-Guillén higher FS of gelatin from chicken skin (176%) than bovine gelatin
et al. (2002) commented that the factors affecting gelatin gel properties (61.17%) is the higher hydrophobic amino acids such as proline,
that are more important than amino acid composition for determining phenylalanine, leucine and isoleucine.
these properties are the average molecular weight and, in particular, the
distribution of α-, β-, or γ-chains that affect the physical properties of the 2.2.4. Film-forming and composites properties
resulting gelatin and, among them, any gelatin containing higher Research on the fabrication of films from PG and their specifications,
amounts of α-chains exhibits greater gel resistance (H. Liu et al., 2008). though limited, has shown that PG represents excellent film-forming
T.-K. Kim et al. (2020) proved that the heating method at duck skin properties (J.-H. Lee et al., 2015; Nazmi et al., 2017; Abedinia et al.,
gelatin (DSG) extraction stage can make a difference of about two de 2018; Said & Sarbon, 2020; Norafidah Suderman & Sarbon, 2020).
grees at the melting point (31.25–33.88). Overall, mechanical properties tensile strength (TS), elongation at
Rahman and Jamalulail (2012) explained the viscosity influenced by break (EAB), Young’s modulus (YM) and heat seal strength (HS) of PG
some factors during production. The CFG gelatin was significantly less films have been reported as similar to that of bovine bone gelatin
viscous than the CBG, which was related to the molecular weight, mo (Abedinia et al., 2018). In food packaging, one of the primary functions
lecular size distribution, and gelatin pH so that the lowest viscosity was is to barricade or reduce moisture transition between product and the
observed at pH 6 to 8 and if during production the pH was out of this surrounding atmosphere. Low water vapor permeability (WVP) widens
range, the viscosity increased. Greater amounts of crosslinking com the utilization of the composite packaging film, especially in an envi
pounds such as –β and -ϒ in gelatin make the viscosity and Bloom higher ronment with high moisture levels (Qi et al., 2015). In addition to the
(Ogawa et al., 2004). In other words, higher viscosity gelatin has a amount and ration of imino acids, the major factors that influence the
longer chain content which is resist the flow. Finally, extraction time has structural and physical properties of the resulting gelatin include mo
a negative effect on viscosity. In general, the PG viscosity is higher than lecular weight distribution and amino acid composition, which play a
mammals because their bloom content is also higher. For example, key role in determining the barrier (WVP, oxygen permeability (OP),
Rafieian et al. (2015) and Mhd Sarbon et al. (2013) compared the vis ultraviolet (UV) and transparency) and mechanical properties (M. C.
cosity of PG and BG and the results showed the CDR gelatin of 55.5 vs. Gómez-Guillén et al., 2011; Abedinia et al., 2018).
29 mP and the CS gelatin of 150 vs. 127 ml/g, respectively. The collagen and gelatin coating or film shows desirable WVP and
OP properties, making it perfect for use in food preservation, among
2.2.3. Emulsifying and foaming properties other applications. For example, it has been used to coat a variety of
meat products to reduce purge, preserve color, improve sensory prop
The remarkable active-surface properties of gelatin make it a suitable erties, slow degradation and prevent spoilage as well as act as an anti
candidate for foaming, emulsifying (emulsifier in oil-in-water emul oxidant (Antoniewski & Barringer, 2010). The chicken skin gelatin
sions) and moisturizing agent in food, pharmaceutical and medical and (CSG) film shows a low WVP value (1.36 × 10− 4 g m− 1 s− 1 Pa− 1) (Nazmi
technical applications. (Lobo, 2002; M. C.; Gómez-Guillén et al., 2011). et al., 2017). Edible DFG-based, chicken feet protein (CP) and CFG films
The emulsifying and foaming properties of gelatin are the result of the plasticized by glycerol show even a lower WVP than CSG and bovine
existence of hydrophobic segments on its peptide chains (Huang et al., films with 5 × 10− 11, 3.44 × 10− 9 and 1.27 × 10− 9 g m− 1 s− 1 Pa− 1,
2017). Since the gelatin emulsifier properties are lower than conven respectively (J.-H. Lee et al., 2015; Abedinia et al., 2018; Norafidah
tional surface-active agents such as globular proteins and gum arabic, Suderman & Sarbon, 2020). The lower WVP in poultry feet gelatin-based
they form large droplets if used alone in the homogenization process films compared to those from poultry skin or mammalian is due to the
(Huang et al., 2020). Thus, two ways to modify the gelatin emulsifier levels of proline and hydroxyproline in this type of gelatin which are
property are to either be modified by bonding non-polar sidebands explained in terms of the amino acid composition (Abedinia et al.,
hydrophobically, or used in conjunction with anionic surfactants (Surh, 2018). Poultry feet gelatins have higher hydrophobicity than mamma
Gu, Decker, & McClements, 2005). lian gelatins due to high proline and hydroxyproline contents. The re
The multifunctional properties of gelatin (emulsifier and foaming) sults show that the properties of poultry feet gelatin films are suitable for
are considered especially in cases such as emulsified powders (Chakka use as an alternative material to bovine gelatin film.
et al., 2017). In such powders, during the emulsification process, both Fabricating biodegradable edible films by blending polymers
the surface-active properties and gelatin film formation are successfully together, has been conducted by some researchers to investigate the
exploited for the purpose. Desirable properties of gelatin including properties of PG -based films. Soo and Sarbon (2018) showed that the
gelation and stabilization are used in subsequent encapsulation pro addition of rice flour to CSG increased the WVP, transparency, thermal
cesses. During marshmallows cooling, the gel-forming properties of properties (TM) and decreased the solubility, UV–visible light trans
gelatins are applied to stabilize the foam. In a gelatin-foamed food such mission of the films. The crystalline nature of the films also improved.
as ice cream, the unique behavior of the gel melts at a temperature range Mechanically, the films showed higher TS and EAB. Nazmi et al. (2017)
of 10–30 ◦ C causing the gelatin gels to melt in the mouth. The feature showed that composite films of CSG/CMC as compared to bovine gelatin
that makes gelatin a unique ingredient for most applications is not only films have similar TS and WVP properties. This study demonstrates
its active surface properties but also a combination of surface, rheo potential of films for use in packaging materials or coatings in food
logical and chemical properties (de Wolf, 2003). products. Loo and Sarbon (2020) prepared CSG/tapioca starch with
The number of studies on the gelation, emulsion and foaming different concentrations of starch (0–25%) and observed that the addi
properties of PG is limited. Dewi Yuliani, Awalsasi, and Jannah (2019) tion of tapioca starch increased the thickness, thermal stability and
studied the emulsion stability (ES) of CBG which were in range from improved the water resistance of the films. X-ray diffraction analysis
9.82 to 61.19% and concluded that higher concentration and extraction showed an increase in film crystallinity as a function of tapioca starch
times led to higher ES. Rafieian et al. (2015) investigated foam capacity content. The resulting films (especially the best formula of CSG/10%
(FC) and foam stability (FS) of CDRG. The CDRG showed the same FS as tapioca starch) showed higher tensile strength and elongation at break
analytical, food grade porcine and Shark cartilage gelatins at 290, 280, values. Using RSM, Said and Sarbon (2020) obtained optimum amounts
and 260 mL/100 mL, respectively (S. Cho et al., 2004), but was much of rice starch and curcumin to make CSG-based composite films that
higher than (P < 0.05) that obtained for BG at 93 mL/100 mL (Hafidz, exhibited good antioxidant (DPPH (2,2-diphenyl-1-picrylhydrazyl) ac
Yaakob, Amin, & Noorfaizan, 2011). The accumulation of proteins that tivity = 85.6%), WVP (1.48 × 10− 10 g/m.s.Pa) and mechanical prop
interfere with the interaction between water and foam proteins is known erties (TS = 8.47 MPa and EAB = 416.43%) for food packaging
to decrease the foaming properties (S. Cho et al., 2004). applications. Films obtained from CSG incorporated with urban extract
22
also showed high antioxidant properties, including total phenolic con especially as a stabilizer in the production of foam in cakes, pies and
tent of 10.79 mg/mg gallic acid, 68.6% of DPPH, and reducing power breads.
14.4%. The addition of herbal extracts reduced TS and WVP and
increased the EAB (N Suderman & Sarbon, 2019). Alias and Sarbon 4. Challenges associated with poultry gelatin
(2019) found that adding potato starch to CSG improves the viscose
behavior of film forming solutions and has a positive effect on me PG market share is still relatively small compared to cow, pig, and
chanical, WVP and UV inhibition properties. fish gelatin. Factors limiting the PG industry include:
2.2.5. Sensory properties • Availability of raw materials: According to reports released by

H. Y. Kim, Lee, and Kim (2012) evaluated the effect of CFG and FAOSTAT (2019), the amount of raw material available for gelatin
wheat fiber levels on the sensory properties of semi-dried chicken jerky. preparation from poultry by-products is much lower than the raw
They found that the tenderness slightly increased with increasing CFG. material from cattle and pigs. According to statistics released by the
Almeida et al. (2013) studied the acceptability of samples of gelatins FAO in 2013, the world production of poultry was 65 billion head, of
using sensory affective tests such as flavour, color and aroma, comparing which about 15% were used for gelatin production, while the figure
with the sensorial qualities of a commercial gelatin. They served gelatin for only hide cattle fresh was 314 million heads. Hence, poultry
samples solutions containing different levels of gelatin and sugar to production is still considered exceptionally low compared to mam
panelists directly to study the sensory properties. The results indicate mals, hence the restricted production of PG. Other than that, the
that if the amount of fatty acids and effective compounds in the odor is production of reliable poultry species in satisfactory amounts is
not eliminated in gelatin extraction, the resulting gel in comparison with troublesome for gelatin producers. Another problem is the need to
commercial gelatin is generally less acceptable. H.-W. Kim et al. (2014) get certification on poultry raw material. Certification is for the
added different concentrations of DFG to duck meat jelly to study its traceability, which is the fundamental necessity for nourishment
physicochemical, textural and sensory properties. Obtained data showed added substances particularly from animal source (Karim & Bhat,
that melting property in the mouth is one of the reasons for differences 2009).
between gelatins. The concentration of DFG had effect on these results as • Price: Although the price of gelatin produced from poultry, for
with increasing of DFG concentration the color score improved, but it example from chicken feet, is cheaper than mammalian extracted
was cause to decreasing the hardness and dispersibility satisfaction gelatin in the market (Almeida et al., 2013), prices for some poultry
scores. The results indicated that although overall acceptance was are particularly expensive, especially for ducks, and people are less
observed in 3% of DFG, but the increase of DFG resulted in a high likely to buy them (Mead, 2004). Therefore, gelatin production from
satisfaction score of appearance; the addition of DFG higher than 5% these poultry species is more costly due to their limited availability.
resulted in the highest appearance score (p < 0.05). On the other hand, • Variety of gelatin quality: The gelatin quality varies based not only
Nik Muhammad et al. (2018) used quantitative descriptive analysis on the methods, extraction conditions, and species used, but also on
(QDA) to measure the effect of the type of acid used for extraction of the composition of the raw materials used in production, namely
DFG on its characterization and sensory property. The results of skin, mechanically deboned residue, feet and bone.
comparing the gelatin obtained from duck feet with commercial bovine • Health risks: First health concerns due to H5N1 associated with
gelatin showed that gelatin obtained from duck feet was brighter in diseases called highly pathogenic avian influenza virus (HPAIV)
appearance than bovine gelatin, as a result of different extraction infection has been reported in Hong Kong in year of 1997 (Suarez,
methods. The strong odor of DFG gelatin was also due to the high level of 2008). Human affirmed cases have moreover been detailed by
fat in gelatin, so it is recommended to use methods that reduce fat by Joannis, Lombin, De Benedictis, Cattoli, and Capua (2006). The
about 0.1%. In general, they concluded that the type of acid used in HPAIV outbreak is recognized to have negative background on the
gelatin extraction could have a large effect on the final product. Finally, deals of poultry and financial matters of production (Fasanmi,
the use of optimum value of fat removers (like some alcohols, e.g. Odetokun, Balogun, & Fasina, 2017). So there are still public con
butanol 10%) before acidic extraction of PG is proposed to improve the cerns about the transmission of the disease from poultry products to
PG sensory properties. human food chain.
3. Application of poultry gelatin 5. Prospects, conclusions and future outlook of poultry gelatin
as an alternative to mammalian gelatin
The obtained gelatin from the poultry by-products such as skins,
mechanically deboned residue and feet showed high gel strength and Two important justifying reasons for conducting industrial studies on
relatively equal gelling and melting points to mammalian gelatins, gelatin production from poultry sources are increasing global demand
which nominates it as a replacement for mammalian consumption in the for gelatin consumption and the need to find healthy alternatives to
industry. As stated in Table 6, gelatin extracted from duck feet showed mammalian gelatin to avoid the strict food consumption limits set by
low gelling temperature, a property that offers novel possible applica religious laws. To date, studies for commercial production of PG have
tions for PG in micro-encapsulation of bioactive components. been limited to initial evaluation of the essential properties of gelatin
In the past, bioactive peptides with multiple properties have been derived from skin, feet, mechanically deboned residue, neck, and head,
attempted to be extracted from various protein sources, with a focus on and research is lacking on finding optimal extraction conditions,
the production of these active compounds from collagen and gelatin including time, temperature and pretreatment, for a mixture of poultry
hydrolysates, resulting in significant advances in modern analysis that by-products. Since the poultry’s gelatin is classified by high Bloom
have led to deeper research on novel sources of gelatin and collagen content (>200 g), it seems that it can be used in combination with fish
extraction and production. J.-H. Lee et al. (2015) produced a bioactive gelatin to modify the physical and chemical properties of this kind of
film by blending CFG and the marjoram, coriander, and clove bud oil alternative gelatin.
and measured its antimicrobial and antioxidant effects in the packaging On the other hand, gelatin extraction with active peptides with
of cheddar cheese slices during storage. They observed that this package antioxidant and antimicrobial properties has been the subject of
could delay oxidation and microbial growth. considerable research over the past decade. The findings have shown
Chakka et al. (2017) suggested that the CFG has potential for that combining the gelatin with essential oils in fruit and plants would
application in dessert/jelly-based products and due to the high value of produce films with desirable properties of DPPH, radical scavenging,
foam formation of the CFG, it can also be used in the baking industry, ferric reducing antioxidant power (FRAP) and hydrophobic and WVP
23
activities. Hence the gelatin matrix would be suitable for release of Bichukale, A., Koli, J., Sonavane, A., Vishwasrao, V., Pujari, K., & Shingare, P. (2018).
Functional properties of gelatin extracted from poultry skin and bone waste.
bioactive compound (Tongnuanchan, Benjakul, & Prodpran, 2012;
International Journal of Pure & Applied Bioscience, 6, 87–101.
J.-H.; Lee et al., 2015). Bohidar, H. B., & Jena, S. S. (1993). Kinetics of sol–gel transition in thermoreversible
S.-J. Lee, Kim, Hwang, et al. (2012) extracted an antioxidant peptide gelation of gelatin. The Journal of Chemical Physics, 98, 8970–8977.
from poultry by-product (duck skin) with molecular weight of 941.43 Cao, J., Duan, Q., Liu, X., Shen, X., & Li, C. (2019). Extraction and physicochemical
characterization of pepsin soluble collagens from golden pompano (Trachinotus
Da, the sequence of His-Thr-Val-Gln-Cys-Met-Phe-Gln, IC50 = 32.6 μg/ blochii) skin and bone. Journal of Aquatic Food Product Technology, 28, 837–847.
ml and DPPH of 22.7%. Then, they investigated its protective effect on Cao, S., Wang, Y., Xing, L., Zhang, W., & Zhou, G. (2020). Structure and physical
normal liver cells damaged by alcohol 3.5%. The results showed that this properties of gelatin from bovine bone collagen influenced by acid pretreatment and
pepsin. Food and Bioproducts Processing, 121, 213–223.
poultry-derived peptide could prevent the production of reactive oxygen Chakka, A. K., Muhammed, A., Sakhare, P., & Bhaskar, N. (2017). Poultry processing
species (ROS) and the cell death of these alcohol-damaged liver cells. waste as an alternative source for mammalian gelatin: Extraction and
Wan Omar and Sarbon (2016) extracted chicken skin gelatin hydroly characterization of gelatin from chicken feet using food grade acids. Waste and
Biomass Valorization, 8, 2583–2593.
sate (CSGH) and investigated its antioxidant and functional properties Cheng, F. Y., Liu, Y. T., Wan, T. C., Lin, L. C., & Sakata, R. (2008). The development of
with a DPPH radical scavenging activity of 47.33%. NM and WAN angiotensin I-converting enzyme inhibitor derived from chicken bone protein.
(2019) also produced CSGH enzymatically using alcalase, pronase E, Animal Science Journal, 79, 122–128.
Cheng, H., Zhu, X., Zhu, C., Qian, J., Zhu, N., Zhao, L., et al. (2008). Hydrolysis
and collagenase with angiotensin converting enzyme inhibitory (ACEI) technology of biomass waste to produce amino acids in sub-critical water.
activity of 69.64–87.69%. S.-J. Lee, Kim, Kim, et al. (2012) also inves Bioresource Technology, 99, 3337–3341.
tigated biological activity of gelatin hydrolysates from duck skin Cheow, C. S., Norizah, M. S., Kyaw, Z. Y., & Howell, N. K. (2007). Preparation and
characterisation of gelatins from the skins of sin croaker (Johnius dussumieri) and
by-products. Results indicated that the pepsin hydrolysate exhibited the
shortfin scad (Decapterus macrosoma). Food Chemistry, 101, 386–391.
highest free radical scavenging activity. According to the reports on the Choe, J., & Kim, H. (2018). Effects of chicken feet gelatin extracted at different
antioxidant properties of peptide products extracted from poultry skin, it temperatures and wheat fiber with different particle sizes on the physicochemical
can be concluded that this type of gelatin has desirable properties for properties of gels. Poultry Science, 97, 1082–1088.
Cho, S. M., Gu, Y. S., & Kim, S. B. (2005). Extracting optimization and physical properties
application in the bioactive compounds delivery. of yellowfin tuna (Thunnus albacares) skin gelatin compared to mammalian gelatins.
Food Hydrocolloids, 19, 221–229.
References Cho, S., Kwak, K., Park, D., Gu, Y., Ji, C., Jang, D., et al. (2004). Processing optimization
and functional properties of gelatin from shark (Isurus oxyrinchus) cartilage. Food
Hydrocolloids, 18, 573–579.
Abdelmalek, B. E., Gómez-Estaca, J., Sila, A., Martinez-Alvarez, O., Gómez- Cliche, S., Amiot, J., Avezard, C., & Gariepy, C. (2003). Extraction and characterization
Guillén, M. C., Chaabouni-Ellouz, S., et al. (2016). Characteristics and functional of collagen with or without telopeptides from chicken skin. Poultry Science, 82,
properties of gelatin extracted from squid (Loligo vulgaris) skin. Lebensmittel- 503–509.
Wissenschaft und -Technologie- Food Science and Technology, 65, 924–931. Damrongsakkul, S., Ratanathammapan, K., Komolpis, K., & Tanthapanichakoon, W.
Abedinia, A., Ariffin, F., Huda, N., & Mohammadi Nafchi, A. (2018). Preparation and (2008). Enzymatic hydrolysis of rawhide using papain and neutrase. Journal of
characterization of a novel biocomposite based on duck feet gelatin as alternative to Industrial and Engineering Chemistry, 14, 202–206.
bovine gelatin. International Journal of Biological Macromolecules, 109, 855–862. Djabourov, M., Lechaire, J.-P., & Gaill, F. (1993). Structure and rheology of gelatin and
Abedinia, A., Ariffin, F., Huda, N., & Nafchi, A. M. (2017). Extraction and collagen gels. Biorheology, 30, 191–205.
characterization of gelatin from the feet of Pekin duck (Anas platyrhynchos Du, L., Keplová, L., Khiari, Z., & Betti, M. (2014). Preparation and characterization of
domestica) as affected by acid, alkaline, and enzyme pretreatment. International gelatin from collagen biomass obtained through a pH-shifting process of
Journal of Biological Macromolecules, 98, 586–594. https://doi.org/10.1016/j. mechanically separated Turkey meat. Poultry Science, 93, 989–1000.
ijbiomac.2017.01.139. Du, L., Khiari, Z., Pietrasik, Z., & Betti, M. (2013). Physicochemical and functional
Ahmad, T., Ismail, A., Ahmad, S. A., Khalil, K. A., Kumar, Y., Adeyemi, K. D., et al. properties of gelatins extracted from Turkey and chicken heads. Poultry Science, 92,
(2017). Recent advances on the role of process variables affecting gelatin yield and 2463–2474.
characteristics with special reference to enzymatic extraction: A review. Food Ee, S., Saari, N., Abas, F., Ismail, A., Bakar, M., & Bakar, J. (2019). Properties of chicken
Hydrocolloids, 63, 85–96. head gelatins as affected by extraction method. International Food Research Journal,
Aksun Tümerkan, E. T., Cansu, Ü., Boran, G., Regenstein, J. M., & Özoğul, F. (2019). 26.
Physiochemical and functional properties of gelatin obtained from tuna, frog and Erge, A., & Zorba, O. (2018). Optimization of gelatin extraction from chicken
chicken skins. Food Chemistry, 287, 273–279. mechanically deboned meat residue using alkaline pre-treatment. Lebensmittel-
Alias, S. A., & Sarbon, N. M. (2019). Rheological, physical, and mechanical properties of Wissenschaft & Technologie, 97, 205–212.
chicken skin gelatin films incorporated with potato starch. Npj Science of Food, 3, Eysturskarð, J., Haug, I. J., Elharfaoui, N., Djabourov, M., & Draget, K. I. (2009).
1–9. Structural and mechanical properties of fish gelatin as a function of extraction
Alireza Seidavi, H. Z. E., & Scanes, C. G. (2019). Poultry byproducts. In Byproducts from conditions. Food Hydrocolloids, 23, 1702–1711.
agriculture and fisheries (pp. 123–146). FAOSTAT. (2019). Food and agriculture organization of the united nations. http://www.fao.
Almeida, P. F., da Silva Lannes, S. C., Calarge, F. A., de Brito Farias, T., & Santana, J. org/faostat/en/#data/QL Accessed: 3 November, 2019.
(2012). FTIR characterization of gelatin from chicken feet. Journal of Chemistry and Fasanmi, O. G., Odetokun, I. A., Balogun, F. A., & Fasina, F. O. (2017). Public health
Chemical Engineering, 6, 1029–1032. concerns of highly pathogenic avian influenza H5N1 endemicity in Africa. Veterinary
Almeida, P. F., da Silva, J. R., da Silva Lannes, S. C., de Brito Farias, T. M., & World, 10, 1194.
Santana, J. C. C. (2013). Quality assurance and economical feasibility of an Fonkwe, L. G., & Singh, R. K. (1997). Production and characterization of gelatinous
innovative product obtained from a byproduct of the meat industry in Brazil. African protein extracts from Turkey deboner residue. Process Biochemistry, 32, 309–318.
Journal of Business Management, 7, 2745–2756. Gál, R., Mokrejš, P., Mrázek, P., Pavlačková, J., Janáčová, D., & Orsavová, J. (2020).
Almeida, P. F., & Lannes, S. C.d. S. (2017). Effects of chicken by-product gelatin on the Chicken heads as a promising by-product for preparation of food gelatins. Molecules,
physicochemical properties and texture of chocolate spread. Journal of Texture 25, 494.
Studies, 48, 392–402. Giménez, B., Turnay, J., Lizarbe, M. A., Montero, P., & Gómez-Guillén, M. C. (2005). Use
Antoniewski, M., & Barringer, S. (2010). Meat shelf-life and extension using collagen/ of lactic acid for extraction of fish skin gelatin. Food Hydrocolloids, 19, 941–950.
gelatin coatings: A review. Critical Reviews in Food Science and Nutrition, 50, 644–653. GME. (2020). Gelatin manufacturers of europe. http://www.gelatine.org/en/gelatine/ove
Araghi, M., Moslehi, Z., Mohammadi Nafchi, A., Mostahsan, A., Salamat, N., & Daraei rview/127.htm Accessed: 5 February, 2020.
Garmakhany, A. (2015). Cold water fish gelatin modification by a natural phenolic Gómez-Guillén, M. C., Giménez, B., López-Caballero, M. E., & Montero, M. P. (2011).
cross-linker (ferulic acid and caffeic acid). Food Sciences and Nutrition, 3, 370–375. Functional and bioactive properties of collagen and gelatin from alternative sources:
Arnesen, J. A., & Gildberg, A. (2002). Preparation and characterisation of gelatine from A review. Food Hydrocolloids, 25, 1813–1827.
the skin of harp seal (Phoca groendlandica). Bioresource Technology, 82, 191–194. Gómez-Guillén, M., Turnay, J., Fernández-Dıaz, M., Ulmo, N., Lizarbe, M., & Montero, P.
Arnesen, J. A., & Gildberg, A. (2007). Extraction and characterisation of gelatine from (2002). Structural and physical properties of gelatin extracted from different marine
Atlantic salmon (Salmo salar) skin. Bioresource Technology, 98, 53–57. species: A comparative study. Food Hydrocolloids, 16, 25–34.
Asghar, A., & Henrickson, R. L. (1982). Chemical, biochemical, functional, and Hafidz, R., Yaakob, C., Amin, I., & Noorfaizan, A. (2011). Chemical and functional
nutritional characteristics of collagen in food systems. In C. O. Chischester, properties of bovine and porcine skin gelatin. International Food Research Journal, 18,
E. M. Mark, & G. F. Stewart (Eds.), Advances in food research (Vol. 28, pp. 232–372). 813–817.
Aykın-Dinçer, E., Koç, A., & Erbaş, M. (2017). Extraction and physicochemical Hamdan, F., & Sarbon, N. (2019). Isolation and characterisation of collagen from
characterization of broiler (Gallus gallus domesticus) skin gelatin compared to fringescale sardinella (Sardinella fimbriata) waste materials. International Food
commercial bovine gelatin. Poultry Science, 96, 4124–4131. Research Journal, 26.
Badii, F., & Howell, N. K. (2006). Fish gelatin: Structure, gelling properties and Hanani, Z. A. N. (2016). Gelatin. In Encyclopedia of food and health (pp. 191–195).
interaction with egg albumen proteins. Food Hydrocolloids, 20, 630–640. Oxford: Academic Press.
24
Haroun, A., Beherei, H., & El-Ghaffar, M. A. (2010). Preparation, characterization, and in Liu, D., Lin, Y., & Chen, M. (2001). Optimum condition of extracting collagen from
vitro application of composite films based on gelatin and collagen from natural chicken feet and its characetristics. Statistics, 2, 35.
resources. Journal of Applied Polymer Science, 116, 2083–2094. Lobo, L. (2002). Coalescence during emulsification: 3. Effect of gelatin on rupture and
Haug, I. J., Draget, K. I., & Smidsrød, O. (2004). Physical and rheological properties of coalescence. Journal of Colloid and Interface Science, 254, 165–174.
fish gelatin compared to mammalian gelatin. Food Hydrocolloids, 18, 203–213. Loo, C. P., & Sarbon, N. M. (2020). Chicken skin gelatin films with tapioca starch. Food
Hazaveh, P., Mohammadi Nafchi, A., & Abbaspour, H. (2015). The effects of sugars on Bioscience, Article 100589.
moisture sorption isotherm and functional properties of cold water fish gelatin films. Mackie, A., Gunning, A., Ridout, M., & Morris, V. (1998). Gelation of gelatin observation
International Journal of Biological Macromolecules, 79, 370–376. in the bulk and at the air-water interface. Biopolymers: Original Research on
Huang, T., Tu, Z.-c., Wang, H., Shangguan, X., Zhang, L., Zhang, N.-h., et al. (2017). Biomolecules, 46, 245–252.
Pectin and enzyme complex modified fish scales gelatin: Rheological behavior, gel Mad-Ali, S., Benjakul, S., Prodpran, T., & Maqsood, S. (2016). Characteristics and gel
properties and nanostructure. Carbohydrate Polymers, 156, 294–302. properties of gelatin from goat skin as influenced by alkaline-pretreatment
Huang, T., Tu, Z., Zou, Z., Shangguan, X., Wang, H., & Bansal, N. (2020). Glycosylated conditions. Asian-Australasian Journal of Animal Sciences, 29, 845.
fish gelatin emulsion: Rheological, tribological properties and its application as Mahmoudi Saber, M. (2019). Strategies for surface modification of gelatin-based
model coffee creamers. Food Hydrocolloids, 102, Article 105552. nanoparticles. Colloids and Surfaces B: Biointerfaces, 183, Article 110407.
Huda, N., Seow, E., Normawati, M., & Aisyah, N. N. (2013). Preliminary study on Masood, M., & Chen, T. (1995). Gelatin, calcium and phosphorus contents of chicken
physicochemical properties of duck feet collagen. International Journal of Poultry broth from broiler deboning. Journal of Food Processing and Preservation, 19,
Science, 12, 615–621. 165–173.
Jamilah, B., & Harvinder, K. (2002). Properties of gelatins from skins of fish—black Mead, G. C. (2004). 1 - meat quality and consumer requirements. In G. C. Mead (Ed.),
tilapia (Oreochromis mossambicus) and red tilapia (Oreochromis nilotica). Food Poultry meat processing and quality (pp. 1–20). Woodhead Publishing.
Chemistry, 77, 81–84. Meky, N., Fujii, M., Ibrahim, M. G., & Tawfik, A. (2019). Biological hydrogen gas
Joannis, T., Lombin, L., De Benedictis, P., Cattoli, G., & Capua, I. (2006). Confirmation of production from gelatinaceous wastewater via stand-alone circular dark/photo
H5N1 avian influenza in Africa. The Veterinary Record, 158, 309. baffled fermenter. Energy Procedia, 157, 670–675.
Jridi, M., Nasri, R., Ben Slama-Ben Salem, R., Lassoued, I., Barkia, A., Nasri, M., et al. Mhd Sarbon, N., Badii, F., & Howell, N. K. (2013). Preparation and characterisation of
(2015). Chemical and biophysical properties of gelatins extracted from the skin of chicken skin gelatin as an alternative to mammalian gelatin. Food Hydrocolloids, 30,
octopus (Octopus vulgaris). Lebensmittel-Wissenschaft und -Technologie- Food Science 143–151.
and Technology, 60, 881–889. Mohtar, N. F., Perera, C., & Quek, S.-Y. (2010). Optimisation of gelatine extraction from
Ju, H., Liu, X., Zhang, G., Liu, D., & Yang, Y. (2020). Comparison of the structural hoki (Macruronus novaezelandiae) skins and measurement of gel strength and
characteristics of native collagen fibrils derived from bovine tendons using two SDS–PAGE. Food Chemistry, 122, 307–313.
different methods: Modified acid-solubilized and pepsin-aided extraction. Materials, Montero, P., & Gómez-Guillén, M. C. (2000). Extracting conditions for megrim
13, 358. (lepidorhombus boscii) skin collagen affect functional properties of the resulting
Jun, M., Lee, J.-M., Lee, K.-S., & Kim, K.-O. (2000). The effects of preparation conditions gelatin. Journal of Food Science, 65, 434–438.
on the properties of jokpyun (traditional Korean gel type food) model system. Food Muyonga, J. H., Cole, C. G. B., & Duodu, K. G. (2004). Fourier transform infrared (FTIR)
Science and Biotechnology, 9, 27–31. spectroscopic study of acid soluble collagen and gelatin from skins and bones of
Karim, A., & Bhat, R. (2009). Fish gelatin: Properties, challenges, and prospects as an young and adult Nile perch (Lates niloticus). Food Chemistry, 86, 325–332.
alternative to mammalian gelatins. Food Hydrocolloids, 23, 563–576. Nagai, T., & Suzuki, N. (2000). Isolation of collagen from fish waste material—skin, bone
Ketnawa, S., Martínez-Alvarez, O., Benjakul, S., & Rawdkuen, S. (2016). Gelatin and fins. Food Chemistry, 68, 277–281.
hydrolysates from farmed Giant catfish skin using alkaline proteases and its Nalinanon, S., Benjakul, S., Visessanguan, W., & Kishimura, H. (2008). Improvement of
antioxidative function of simulated gastro-intestinal digestion. Food Chemistry, 192, gelatin extraction from bigeye snapper skin using pepsin-aided process in
34–42. combination with protease inhibitor. Food Hydrocolloids, 22, 615–622.
Khiari, Z., Rico, D., Martin-Diana, A. B., & Barry-Ryan, C. (2011). The extraction of Nazmi, N. N., Isa, M. I. N., & Sarbon, N. M. (2017). Preparation and characterization of
gelatine from mackerel (Scomber scombrus) heads with the use of different organic chicken skin gelatin/CMC composite film as compared to bovine gelatin film. Food
acids. Journal of FisheriesSciences. com, 5. Bioscience, 19, 149–155.
Kim, T.-K., Ham, Y.-K., Shin, D.-M., Kim, H.-W., Jang, H. W., Kim, Y.-B., et al. (2020). Nik Muhammad, N. A., Huda, N., Karim, A. A., & Mohammadi Nafchi, A. (2018). Effects
Extraction of crude gelatin from duck skin: Effects of heating methods on gelatin of acid type extraction on characterization and sensory profile of duck feet gelatin:
yield. Poultry Science, 99, 590–596. Towards finding bovine gelatin alternative. Journal of Food Measurement and
Kim, H. Y., Lee, J. W., & Kim, C. J. (2012). Effects of chicken feet gelatin and wheat fiber Characterization, 12, 480–486.
levels on quality properties of semi-dried chicken Jerky. Korean Journal for Food NM, S., & WAN, W. A. (2019). Angiotensin-I converting enzyme (ACE) inhibitory
Science of Animal Resources, 32, 732–739. peptides from chicken skin gelatin hydrolysate and its antihypertensive effect in
Kim, H.-W., Park, J.-H., Yeo, E.-J., Hwang, K.-E., Song, D.-H., Kim, Y.-J., et al. (2014). spontaneously hypertensive rats. International Food Research Journal, 26.
Effect of duck feet gelatin concentration on physicochemical, textural, and sensory Norziah, M. H., Kee, H. Y., & Norita, M. (2014). Response surface optimization of
properties of duck meat jellies. Korean Journal for Food Science of Animal Resources, bromelain-assisted gelatin extraction from surimi processing wastes. Food Bioscience,
34, 387. 5, 9–18.
Kim, H.-W., Song, D.-H., Choi, Y.-S., Kim, H.-Y., Hwang, K.-E., Park, J.-H., et al. (2012). Ogawa, M., Portier, R. J., Moody, M. W., Bell, J., Schexnayder, M. A., & Losso, J. N.
Effects of soaking pH and extracting temperature on the physicochemical properties (2004). Biochemical properties of bone and scale collagens isolated from the
of chicken skin gelatin. Korean Journal for Food Science of Animal Resources, 32, subtropical fish black drum (Pogonia cromis) and sheepshead seabream
316–322. (Archosargus probatocephalus). Food Chemistry, 88, 495–501.
Kobya, M., Senturk, E., & Bayramoglu, M. (2006). Treatment of poultry slaughterhouse Okanović, Đ., Ristić, M., Kormanjoš, Š., Filipović, S., & Živković, B. (2009). Chemical
wastewaters by electrocoagulation. Journal of Hazardous Materials, 133, 172–176. characteristics of poultry slaughterhouse byproducts. Biotechnology in Animal
Kuan, Y.-H., Nafchi, A. M., Huda, N., Ariffin, F., & Karim, A. A. (2016). Effects of sugars Husbandry, 25, 143–152.
on the gelation kinetics and texture of duck feet gelatin. Food Hydrocolloids, 58, Oladzadabbasabadi, N., Ebadi, S., Mohammadi Nafchi, A., Karim, A. A., &
267–275. Kiahosseini, S. R. (2017). Functional properties of dually modified sago starch/
Kuan, Y. H., Nafchi, A. M., Huda, N., Ariffin, F., & Karim, A. A. (2017). Comparison of κ-carrageenan films: An alternative to gelatin in pharmaceutical capsules.
physicochemical and functional properties of duck feet and bovine gelatins. Journal Carbohydrate Polymers, 160, 43–51.
of the Science of Food and Agriculture, 97, 1663–1671. Padilha, A. C. M., Silva, T. N.d., & Sampaio, A. (2006). Desafios de adequação à questão
Kuijpers, A., Engbers, G., Feijen, J., De Smedt, S., Meyvis, T., Demeester, J., et al. (1999). ambiental no abate de frangos: o caso da perdigão agroindustrial–unidade industrial
Characterization of the network structure of carbodiimide cross-linked gelatin gels. de Serafina corrêa–RS. Teoria e Evidência Econômica, 14, 109–125.
Macromolecules, 32, 3325–3333. Park, J.-H., Choe, J.-H., Kim, H.-W., Hwang, K.-E., Song, D.-H., Yeo, E.-J., et al. (2013).
Lee, S.-J., Kim, Y.-S., Hwang, J.-W., Kim, E.-K., Moon, S.-H., Jeon, B.-T., et al. (2012a). Effects of various extraction methods on quality characteristics of duck feet gelatin.
Purification and characterization of a novel antioxidative peptide from duck skin by- Korean Journal for Food Science of Animal Resources, 33, 162–169.
products that protects liver against oxidative damage. Food Research International, Pelizer, L., Pontieri, M., & Moraes, I. (2007). Use of agro-industrial waste in
49, 285–295. biotechnological processes as prospect of reducing environmental impact. JOTMI, 2,
Lee, S.-J., Kim, K. H., Kim, Y.-S., Kim, E.-K., Hwang, J.-W., Lim, B. O., et al. (2012b). 118–127.
Biological activity from the gelatin hydrolysates of duck skin by-products. Process PRC. (2019). Global religious futures. Pew Research Center. http://www.globalre
Biochemistry, 47, 1150–1154. ligiousfutures.org/.
Lee, J.-H., Lee, J., & Song, K. B. (2015). Development of a chicken feet protein film Qi, X.-M., Liu, S.-Y., Chu, F.-B., Pang, S., Liang, Y.-R., Guan, Y., et al. (2015). Preparation
containing essential oils. Food Hydrocolloids, 46, 208–215. and characterization of blended films from quaternized hemicelluloses and
Lin, L., Regenstein, J. M., Lv, S., Lu, J., & Jiang, S. (2017). An overview of gelatin derived carboxymethyl cellulose. Materials, 9, 4.
from aquatic animals: Properties and modification. Trends in Food Science & Rafieian, F., Keramat, J., & Kadivar, M. (2013). Optimization of gelatin extraction from
Technology, 68, 102–112. chicken deboner residue using RSM method. Journal of Food Science and Technology,
Liu, D.-C. (2002). Better utilization of by-products from the meat industry food and fertilizer 50, 374–380.
technology center. http://www.fftc.agnet.org/library.php?func=view&id=2011070 Rafieian, F., Keramat, J., & Shahedi, M. (2015). Physicochemical properties of gelatin
6135001 Accessed: 14 February, 2020. extracted from chicken deboner residue. Lebensmittel-Wissenschaft und -Technologie-
Liu, H., Li, D., & Guo, S. (2008). Rheological properties of channel catfish (Ictalurus Food Science and Technology, 64, 1370–1375.
punctaus) gelatine from fish skins preserved by different methods. LWT-Food Science Rahman, M. N. A., & Jamalulail, S. A. S. K. A. (2012). Extraction, physicochemical
and Technology, 41, 1425–1430. characterization and sensory quality of chicken feet gelatin. BORNEO SCIENCE, 30.
25
Rammaya, K., Ying, V. Q., & Babji, A. S. (2012). Physicochemical analysis of gelatin Surh, J., Gu, Y. S., Decker, E. A., & McClements, D. J. (2005). Influence of environmental
extracted from mechanically deboned chicken meat (MDCM) residue. Health, 5, 3. stresses on stability of O/W emulsions containing cationic droplets stabilized by
Ranganathan, S., Balagangadharan, K., & Selvamurugan, N. (2019). Chitosan and SDS− fish gelatin membranes. Journal of Agricultural and Food Chemistry, 53,
gelatin-based electrospun fibers for bone tissue engineering. International Journal of 4236–4244.
Biological Macromolecules, 133, 354–364. Tongnuanchan, P., Benjakul, S., & Prodpran, T. (2012). Properties and antioxidant
Rasli, H. I., & Sarbon, N. M. (2015). Effects of different drying methods on the activity of fish skin gelatin film incorporated with citrus essential oils. Food
rheological, functional and structural properties of chicken skin gelatin compared to Chemistry, 134, 1571–1579.
bovine gelatin. International Food Research Journal, 22, 584–592. Wan Omar, W. H., & Sarbon, N. M. J. (2016). Effect of drying method on functional
Saenmuang, S., Phothiset, S., & Chumnanka, C. (2019). Extraction and characterization properties and antioxidant activities of chicken skin gelatin hydrolysate. Journal of
of gelatin from black-bone chicken by-products. Food Science and Biotechnology, Food Science and Technology, 53, 3928–3938.
1–10. Wang, T.-Y., Hsieh, C.-H., Hung, C.-C., Jao, C.-L., Chen, M.-C., & Hsu, K.-C. (2015). Fish
Said, N. S., & Sarbon, N. M. (2020). Response surface methodology (RSM) of chicken skin skin gelatin hydrolysates as dipeptidyl peptidase IV inhibitors and glucagon-like
gelatin based composite films with rice starch and curcumin incorporation. Polymer peptide-1 stimulators improve glycaemic control in diabetic rats: A comparison
Testing, 81, Article 106161. between warm-and cold-water fish. Journal of Functional Foods, 19, 330–340.
Salminen, E., & Rintala, J. (2002). Anaerobic digestion of organic solid poultry Wangtueai, S., & Noomhorm, A. (2009). Processing optimization and characterization of
slaughterhouse waste–a review. Bioresource Technology, 83, 13–26. gelatin from lizardfish (Saurida spp.) scales. Lebensmittel-Wissenschaft und
Santana, J. C., Gardim, R. B., Almeida, P. F., Borini, G. B., Quispe, A. P., Llanos, S. A., -Technologie- Food Science and Technology, 42, 825–834.
et al. (2020). Valorization of chicken feet by-product of the poultry industry: High Weng, W., Zheng, H., & Su, W. (2014). Characterization of edible films based on tilapia
qualities of gelatin and biofilm from extraction of collagen. Polymers, 12, 529. (Tilapia zillii) scale gelatin with different extraction pH. Food Hydrocolloids, 41,
Sarabia, A. I., Gómez-Guillén, M., & Montero, P. (2000). The effect of added salts on the 19–26.
viscoelastic properties of fish skin gelatin. Food Chemistry, 70, 71–76. Widyasari, R., & Rawdkuen, S. (2014). Extraction and characterization of gelatin from
Schrieber, R., & Gareis, H. (2007). Gelatin handbook. Theory and industrial practice. John chicken feet by acid and ultrasound assisted extraction. Food and Applied Bioscience
Wiley & Sons. Journal, 2, 85–97.
Shabani, H., Mehdizadeh, M., Mousavi, S. M., Dezfouli, E. A., Solgi, T., Khodaverdi, M., de Wolf, F. A. (2003). Collagen and gelatin. In Progress in biotechnology (Vol. 23, pp.
et al. (2015). Halal authenticity of gelatin using species-specific PCR. Food Chemistry, 133–218).
184, 203–206. Yasin, H., Babji, A. S., & Norrakiah, A. S. (2017). Modification of chicken feet gelatin
Sheela, A. (2014). Gelatin Market-global industry analysis, size, share, growth, trends and with aqueous sweet basil and lemongrass extract. LWT-Food Science and Technology,
fsorecast, 2012-2018. https://doi.org/10.1016/s1364-5439(13)70125-4. URL, 77, 72–79.
Accessed: 3 October, 2013. Ye, M., Mi, S., Zhang, C., Yue, J., Jia, W., & German, S. (2020). Effect of heat treatment
Silva, R. S. G., Bandeira, S. F., & Pinto, L. A. A. (2014). Characteristics and chemical on gelatin properties of pepsin-soluble collagen from chicken bones. Current Topics in
composition of skins gelatin from cobia (Rachycentron canadum). LWT - Food Science Nutraceutical Research, 18.
and Technology. Yeo, E.-J., Song, D.-H., Ham, Y.-K., He, F.-Y., & Kim, C.-J. (2013). Effect of duck feet
Sompie, M., Siswosubroto, S., Rembet, G., & Ponto, J. (2019). Effect of different types of gelatin on quality properties of low-fat sausage.
acid solvent on functional and microbiological properties of chicken leg skin gelatin. Yilmaz, M. T., Kesmen, Z., Baykal, B., Sagdic, O., Kulen, O., Kacar, O., et al. (2013).
In IOP conference series: Earth and environmental science (Vol. 387)IOP Publishing, A novel method to differentiate bovine and porcine gelatins in food products:
Article 012128. NanoUPLC-ESI-Q-TOF-MSE based data independent acquisition technique to detect
Soo, P., & Sarbon, N. (2018). Preparation and characterization of edible chicken skin marker peptides in gelatin. Food Chemistry, 141, 2450–2458.
gelatin film incorporated with rice flour. Food Packaging and Shelf Life, 15, 1–8. Yuliani, D., Awalsasi, D. R., & Jannah, A. (2019). Characterization of gelatin profile of
Soukoulis, C., Behboudi-Jobbehdar, S., Yonekura, L., Parmenter, C., & Fisk, I. D. (2014). chicken broiler (Gallus domestica) bone using SDS-PAGE electrophoresis. ALCHEMY,
Stability of Lactobacillus rhamnosus GG in prebiotic edible films. Food Chemistry, 7, 7–12.
159, 302–308. Yuliani, D., Maunatin, A., Jannah, A., & Fauziyyah, H. (2019). Effect of phosphoric acid
Sow, L. C., & Yang, H. (2015). Effects of salt and sugar addition on the physicochemical pretreatment on characterization of gelatin from broiler chicken (Gallus gallus
properties and nanostructure of fish gelatin. Food Hydrocolloids, 45, 72–82. domesticus L.) bones. In IOP conference series: Earth and environmental science (Vol.
Suarez, D. L. (2008). Avian influenza. Wiley. 293)IOP Publishing, Article 012013.
Suderman, N., & Sarbon, N. (2019). Preparation and characterization of gelatin-based Zarai, Z., Balti, R., Mejdoub, H., Gargouri, Y., & Sayari, A. (2012). Process for extracting
films with the incorporation of Centella asiatica (L.) urban extract. Food Research, 3, gelatin from marine snail (< i> Hexaplex trunculus</i>): Chemical composition
506–514. and functional properties. Process Biochemistry, 47, 1779–1784.
Suderman, N., & Sarbon, N. M. (2020). Optimization of chicken skin gelatin film Zhou, P., Mulvaney, S. J., & Regenstein, J. M. (2006). Properties of Alaska pollock skin
production with different glycerol concentrations by response surface methodology gelatin: A comparison with tilapia and pork skin gelatins. Journal of Food Science, 71,
(RSM) approach. Journal of Food Science and Technology, 57, 463–472. C313–C321.
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Trends in Food Science & Technology 104 (2020) 14–26

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Trends in Food Science & Technology

Poultry gelatin: Characteristics, developments, challenges, and future

1. Introduction Selvamurugan, 2019), nanoparticles as drug and gene delivery systems

Table 4 Table 4 (continued )

2.2.3. Enzyme aid treatment

Method and viscosity value (in

CFG a 10 264.3 NR a 26.7 Brookfield at 40 ◦ C, 4.96 cP Rahman and Jamalulail (2012)

2.2.5. Sensory properties • Availability of raw materials: According to reports released by

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