R: Concise Reviews

in Food Science

Analytical Methods for Gelatin

Differentiation from Bovine and Porcine
Origins and Food Products
Raja Mohd Hafidz Raja Nhari, Amin Ismail, and Yaakob B. Che Man

Abstract: Usage of gelatin in food products has been widely debated for several years, which is about the source of gelatin
that has been used, religion, and health. As an impact, various analytical methods have been introduced and developed to
differentiate gelatin whether it is made from porcine or bovine sources. The analytical methods comprise a diverse range
of equipment and techniques including spectroscopy, chemical precipitation, chromatography, and immunochemical.
Each technique can differentiate gelatins for certain extent with advantages and limitations. This review is focused on
overview of the analytical methods available for differentiation of bovine and porcine gelatin and gelatin in food products
so that new method development can be established.
Keywords: analytical methods, food products, gelatin

Introduction
Gelatin is a heterogeneous mixture of polypeptides obtained
through partial hydrolysis of collagens from animal connective tis-
sues by acidic or alkaline treatments (Zhang and others 2009).
The transformation of collagen to gelatin is interpreted as disin-
tegration of the helical structures of collagen into random coils.
Upon cooling, the random coils undergo a coil-to-helix transi-
tion during which they attempt to reform the original structure
(Karim and Bhat 2009). When collagen is subjected to mild acid
or alkaline treatment or heating in water, the fibrous structure
of collagen is broken down irreversibly and gelatin is formed.
During the transformation, the breakdown of cross-linkages be-
tween polypeptide chains of collagen occurs (Yang and others
2007). The gelatin manufacturing processes involve general steps
including pretreatment of the raw material, extraction, purifica-
tion, and drying to produce desired gelatin. The most common
raw materials for industrial-scale gelatin are obtained from slaugh-
ter byproducts due to its availability in sufficient quantities at an
economical price. The gelatins derived from porcine skins are
treated with acidic treatments (type A) to avoid saponification due
to high fat content in this skin. Generally, the acidic treatment
is limited to the tissue of younger animals that have lesser degree
of covalent bonding in collagen that ensures a good yield and
quality of gelatin. The alkaline treatment (type B) is applied to
chopped split material and ossein prepared from bones (Schrieber
and Gareis 2007). The central layer of cattle hide contains native
collagen that is suitable as raw material in gelatin manufacturing
process. The physicochemical properties of gelatin are determined
by amino acid sequence, the resulting 3-dimensional structure,
the molecular mass distribution, pH, ionic strength, and reaction
with other components. Type A and B gelatins are different in
terms of isoelectric point (IEP) where IEP of type A is in the pH
MS 20110838 Submitted 7/12/2011, Accepted 10/20/2011. Authors are with 2003; Venien and Levieux 2005a, 2005b). The bovine and porcine
Halal Products Research Inst., Putra Infoport, Univ. Putra Malaysia, 43400 UPM gelatins also would give risks to gelatin-allergic patients (Doi and
Serdang, Selangor, Malaysia. Direct inquiries to author Nhari (E-mail: raja_hafidz@ others 2009). Thus, the gelatin authentication is very crucial so
yahoo.com).
range of 8 to 9 while for type B, its IEP is in the between pH 4.8
and 5.5. The functional properties of gelatin are associated with
gelling (bloom strength, gelling time, setting and melting temper-
ature, viscosity) and surface behavior (formation and stabilization
of foams and emulsions, adhesive properties, and dissolution be-
havior) (Schrieber and Gareis 2007).
This well-known food hydrocolloid has been applied in food
products as agents for gel formation in jellies and fruit gummies,
foam formation and stabilizer in ice creams, marshmallows, emul-
sifier and foam stabilizer in caramels, syneresis stabilizer in yo-
gurt, foam formation in foamed milk dessert, gel formation in
jellied milk dessert, emulsion stabilizer in meat and sausages, bind-
ing agent in broths and canned meats, pharmaceuticals (soft and
hard capsules, gel-forming component in dental pharmaceuticals,
thickener in liquid dosage forms, tablets, ointments for mucosal
membranes of the mouth, vitamin coating, pastilles, globules),
photography (ink jet printing), cosmetic and medical products
(blood plasma substitutes, gelatin sponges) (Hidaka and Liu 2003;
Venien and Levieux 2005a, 2005b; Schrieber and Gareis 2007).
There is high demand for gelatin especially in Europe, North
America, South America, and certain countries in Asia Pacific
due to its unique properties that suit its application in a wide
range of products (GMIA 2001; SAGMA 2004; GMAP 2005;
GME 2011).
Due to the various sources of gelatins that have been con-
sumed, the gelatin authentication has become a major concern
among communities including Muslims, Jews, Hindus, and veg-
etarians. For instance, gelatin from slaughtered cow that has not
followed Islamic law and the usage of porcine origin are forbidden
for Muslims. Hindus also prohibits the usage of cow while the
animal-based food is banned by vegetarian. In health aspects, the
outbreak of bovine spongiform encephalopathy (BSE) or com-
monly known as mad cow disease in Europe has caused restriction
on the usage of bovine gelatin in food products (Hidaka and Liu
that the gelatin is confirmed to abide with its label description

C 2011 Institute of Food Technologists

 R

R42 Journal of Food Science r Vol. 71, Nr. 1, 2012 doi: 10.1111/j.1750-3841.2011.02514.x
Further reproduction without permission is prohibited
 R: Concise Reviews
Analytical methods for gelatin differentiation . . .

whether it is made from bovine or porcine. However, the trans-
parency of food ingredients is not always readily noticeable. Im-
proper labeling of gelatin origin is the most common case occurred
in food industry. Thus, the reliable methods to detect the source of
animal utilized in food products are needed and usable to identify
the food components so that the adulteration can be identified
(Murugaiah and others 2009).
Eight studies have been published since 2003 until 2010 to dif-
ferentiate gelatins especially involving bovine and porcine gelatins.
They have claimed that differentiation of both gelatins can be
made using analytical methods including the applications of spec-
troscopic, chemical, liquid chromatography, and immunochemi-
cal techniques (Hidaka and Liu 2003; Nemati and others 2004;
in Food Science
Venien and Levieux 2005a, 2005b; Zhang and others 2008, 2009;
Doi and others 2009; Hashim and others 2010). To the best of
our knowledge, no review related to differentiation of gelatins has
been published. Thus, this paper reviews summarization of the
related studies about analytical methods including advantages and
limitations (Table 1). With this review, it can be used as a quick
reference so that new analytical methods can be tested.
Analytical Methods
Spectroscopic technique
Fourier transform infrared (FTIR) spectroscopy has been used
as a detection tool in food adulteration (Van de Voort 1992;

Table 1–Differentiation of gelatins using various analytical methods.

Method
Fourier transform infrared (FTIR)
spectroscopy
Chemical precipitation
High performance liquid
chromatography (HPLC)
ELISA
Advantages Limitations References
Rapid analysis; Require high purity of sample; Hashim and others (2010)
able to differentiate between raw unable to differentiate a mixture of
bovine and porcine gelatins based raw gelatins
on spectra’s intensity using
discriminant analysis
Differentiation can be made at Unable to differentiate the origin of Hidaka and Liu (2003)
concentrations of 0.5 mg/mL gelatin in food products
(bovine bone gelatin) and
4.0 mg/mL (porcine skin gelatin)
that stimulate HAP transformation
Utilizing PCA to differentiate both Unable to differentiate a mixture of Nemati and others (2004)
raw gelatin of bovine and porcine gelatins because their same
chemical properties; amount of
amino acids is different and
inconsistent in each analysis
HPLC coupled with mass Hydroxylation of proline and lysine Zhang and others (2008, 2009)
spectrometry (HPLC/MS): could increase the difficulties in
Differentiation of raw gelatin can differentiation of marker peptides
be based on marker peptides in for both gelatins;
collagen sequences marker peptides might be destroyed
during manufacturing
Indirect competitive ELISA: Less sensitive to species specific due Venien and Levieux (2005a)
Sensitive technique to differentiate to high homology of animal’s
the origin of gelatin; collagen sequence;
certain antibodies can detect the antibodies raised against bovine
presence of gelatin in food (not tyrosylated gelatin could not
species or process sensitive); differentiate from porcine bone
several antibodies are highly gelatin prepared from alkaline
sensitive to acid or alkaline process process.
of bovine and porcine gelatin;
antibodies raised against porcine
tyrosylated gelatin more sensitive to
porcine gelatin except for porcine
alkaline bone gelatin
Indirect competitive ELISA: Only specific to bovine gelatin Venien and Levieux (2005b)
More species-specific to bovine
gelatin;
detection of high bloom bovine
gelatin in high bloom porcine
gelatin was more sensitive;
efficient control of gelatin batches
manufactured;
can be applied for pharmaceutical
and food manufacturers to secure
supply chain
Sandwich ELISA: established ELISAs Production of false positive for Doi and others (2009)
method could be used to gelatinized heated meat
determine bovine and porcine
gelatin in commercial processed
foods ;
The goat pAb3-pAb3 ELISA has
weaker reactivity to cooked meat,
less cross-reactivity for boiled squid
and no false positives or negatives

Vol. 71, Nr. 1, 2012 r Journal of Food Science R43

R: Concise Reviews Analytical methods for gelatin differentiation . . .
in Food Science
Rodriguez-Saona and Allendorf 2011). For instance, it was used
in detection of food hydrocolloids in confectionary and food
supplements (Čopı́ková and others 2001). In infrared (IR) spec-
troscopy, IR radiation is passed through a sample with some of
the IR radiation is absorbed and transmitted. The resulting spec-
trum represents the molecular absorption and transmission, cre-
ating a molecular fingerprint of the sample. Each sample from
different sources produces different IR spectrum that represent
its unique molecular structures. This makes IR spectroscopy
suitable for gelatin analysis because it shows the information
on functional group especially chemical composition of specific
substances.
Hashim and others (2010) studied the utilization of FTIR as a
rapid method to differentiate the source of raw gelatin. A FTIR
spectroscopy in combination with attenuated total reflectance
(ATR) and discriminant analysis is useful to compare bovine and
porcine gelatin spectra. ATR is a technique whereby the sample is
placed in contact with ATR element and a spectrum is recorded
based on that contact. The spectra for both gelatins are closely sim-
ilar between wavelengths of 4000 and 650 cm−1 . The major differ-
ences among gelatins spectra can be found in 3290 to 3280 cm−1
and 1660 to 1200 cm−1 of the complete IR spectra range (4000
to 650 cm−1 ). The 3290 to 3280 cm−1 region is donated by N-
H bond-stretching mode of hydrogen bonded amide group. The
discriminant analysis for deformation of N-H bonds in the range
3290 to 3280 cm−1 and 1660 to 1200 cm−1 can determine the
unknown gelatin sources. These 2 spectra are specified through
analysis using difference of variance between spectrum of bovine
and porcine gelatin. The comparison was made based on the in-
tensity of spectra that is slightly different between both gelatins. By
using Cooman’s plot obtained from Mahalanobis distance (formu-
late a distance between clusters) to visualize discriminant analysis,
IR spectrum of bovine and porcine gelatin can be classified ac-
cording to their respective group. This technique required simple
sample preparation with rapid time analysis. However, this tech-
nique requires high purity of sample and problems may occur
when analyzing the mixture of raw gelatins from different animal
sources.
Chemical precipitation
The effects of gelatin from bovine bone and porcine skin on
calcium phosphate precipitation could be distinguished (Hidaka
and Liu 2003). The study was conducted to detect the presence of
bovine bone gelatin in food products as a concern due to the out-
break of BSE. The molecular weight of bovine bone and porcine
skin gelatins used in the study was ranged from 40000 to 50000
Da. Gelatin promotes the formation of hydroxyapatite (HAP) and
enhances amorphous calcium phosphate (ACP) formation. The
interaction of gelatin and calcium phosphate precipitation is used
to determine the source of gelatins. The concentrations of 0.5 and
4.0 mg/mL for bovine bone and porcine skin gelatins, respectively,
achieved the maximum stimulation of the HAP transformation.
The peak concentration for the stimulation of the HAP trans-
formation may be used to differentiate between them. However,
the rate of ACP formation is not affected by both gelatins. This
method is limited to analyze gelatin from bovine bone and porcine
skin. It may not be suitable to differentiate gelatins in food prod-
ucts because HAP transformation is easily interfered by variable
components such as sugars, lipids, salts, coloring agent, and other ELISA
food additives that are added in food products and subsequently, it
will give difficulty to confirm the origin of gelatin. mon technique used in determination of food authenticity because
R44 Journal of Food Science r Vol. 71, Nr. 1, 2012
High performance liquid chromatography with principal
component analysis (PCA) or mass spectrometry technique
High performance liquid chromatography coupled
with PCA. Nemati and others (2004) have differentiated bovine
and porcine gelatins using PCA based on the results of individual
amino acids. Amino acid analysis was performed using a reversed
phase-high performance liquid chromatography (RP-HPLC).
Amino acid analysis can be used to quantify the amount of protein
and peptides, to identity proteins or peptides based on their
amino acid composition, to evaluate fragmentation strategies for
peptide mapping, and to detect unusual amino acids that might be
present in a protein or peptide. The chromatograms of bovine and
porcine gelatins, which are represented by individual amino acids,
are almost the same but they had an extra amino acid for bovine
gelatin compared to porcine ones. However, it cannot be used
for differentiation of both gelatins due to their same chemical
properties. Thus, PCA was applied since it involves overall peaks
of amino acids. PCA was utilized in processing of amino acid
parameters (height, area, area percentage, and width) to obtain
the significant variables and classification of bovine and porcine
gelatin. All gelatins can be differentiated using 2-dimensional
graphs. However, this method is not suitable to analyze mixture of
gelatins because gelatins contain similar type of amino acids and the
concentration of amino acids is different and inconsistent in each
analysis.
High performance liquid chromatography coupled with
mass spectrometry. The development of high performance liq-
uid chromatography/mass spectrometry (HPLC/MS) method was
based on the theory that gelatin contains polypeptides from de-
graded collagen type I and amino acid sequence of collagens from
different animals is not identical. Thus, it leads to the identification
of marker peptides in digested gelatins using HPLC/MS (Zhang
and others 2008). Bovine and porcine gelatins were digested with
trypsin, producing peptides that have specific sequences. By com-
paring the MS/MS data with collagen database, most of peptide
sequences of bovine and porcine collagen type I were similar but
some partial sequences were specific. They indicated that more
marker peptides were found in α2 chain because the difference of
total amino acid residues was 1.1% between α1 chain of bovine
and porcine collagen type I while in α2 chain, the difference was
2.3% of total amino acid residues. The specific peptides identi-
fied in the digested bovine and porcine gelatins showed that more
markers for peptides were found in α2 chain than those found in
α1 chain. Thus, 2 peptides have been identified in α2 chain as
marker peptides including TGPPGPSGISGPPGPPGPAGK that
was found in digested bovine gelatin (α2 (I) chain of bovine col-
lagen type I) while for porcine gelatin, the specific peptide was
IGPPGPSGISGPPGPPGPAGK (α2 (I) chain of porcine colla-
gen type I). The same studies by Zhang and others (2009) in-
volved bovine gelatins with different molecular weight using high
performance liquid chromatography/tandem mass spectrometry
(HPLC-MS/MS). The more marker peptides can be detected
when higher molecular weight of gelatin is used. Both studies are
successful to differentiate the bovine and porcine gelatins but the
hydroxylation of proline and lysine that is not uniform and not
identical therefore can increase difficulty to differentiate marker
peptides for both gelatins. The marker peptides might also be
degraded during product manufacturing.
Enzyme-linked immunosorbent assay (ELISA) is the most com-

Analytical methods for gelatin differentiation . . .
of its specificity and sensitivity. It is an immunological technique
that involves an enzyme to detect the presence of an antibody or an
antigen in sample. The 2 most used ELISA for food authentication
are the indirect and the sandwich ELISA. The indirect ELISA uti-
lizes 2 antibodies, one of which is specific to the antigen and
the other of which is coupled to an enzyme. This 2nd antibody
will cause a chromogenic or fluorogenic substrate to produce a
signal. In the sandwich ELISA, the antigen is bound between 2
antibodies that consist of the capture antibody and the detection
antibody. The detection antibody can be coupled to an enzyme
or can bind the conjugate (enzyme-linked antibody) that will pro-
duce the biochemical reaction (Asensio and others 2008). Venien
and Levieux (2005a) can differentiate bovine and porcine gelatins
using polyclonal antibodies raised against tyrosylated bovine and
porcine gelatin. The tyrosylation of gelatins with tyrosine is to
increase the weak immunogenicity of its parent collagen and con-
vert gelatin into powerful antigen. By using indirect ELISA, the
developed antibodies have large differences in their sensitivity on
species and manufacturing process. Certain antibodies can detect
the presence of gelatin in food and some were highly sensitive
to acid or alkaline process of bovine and porcine gelatins. Anti-
bodies raised against porcine tyrosylated gelatin are more sensitive
to porcine gelatin except alkaline-treated porcine bone gelatin (as
a control the presence of porcine acid gelatin in bovine gelatin).
However, in ELISA technique, some antibodies have low species
specificity because of high homology of collagen sequences be-
tween different species.
In order to obtain more bovine-specific antibodies with lower
process sensitivity, Venien and Levieux (2005b) raised antibod-
ies against putative specific sequences of bovine collagen α1 (I)
chain that show amino acid changes between bovine and unre-
lated species. They have selected one recognized species-specific
sequence from the N-terminal sequence of telopeptide of bovine
α2 (I) chain as peptide 1 (Glu-Phe-Asp-Ala-Lys-Gly-Gly-Gly-
Pro-Gly) and peptide 2 (Gly-Pro-Ala-Gly-Ala-Pro-Gly-Pro-Pro-
Gly) from the central region of bovine α1 (I) chain. Antipeptide
1 antibodies have low reactivity as compared with antipeptide
2 antibodies when tested against collagen and gelatin. Antipeptide
2 antibodies are strongly reactive when react with bovine gelatins
rather than porcine gelatin. When the same mixture of gelatins
was analyzed by indirect competitive ELISA, high sensitivity is
obtained for the detection of bovine gelatins in porcine gelatins.
Detection of high bloom bovine gelatins in high bloom porcine
gelatins was more sensitive. Thus, this ELISA could be used to dif-
ferentiate bovine gelatin with porcine gelatin and could be applied
by pharmaceutical and food manufacturers. The factors affecting
the effectiveness of both ELISA are the type of gelatin process
(acid or alkaline), species origin of gelatin (bovine or porcine),
and source of gelatin (bone or skin/hide).
A sandwich ELISA method was developed to detect gelatins of
bovine and porcine in processing food for the patients with risk
of gelatin allergy (Doi and others 2009). They have established
2 sandwich ELISAs by producing polyclonal antibodies from im-
munization of gelatin in rabbit recognized as rabbit pAb2-pAb1
ELISA (pAb2 are used for the coating and pAb1 are used for
capture reactions) and in goat as pAb3-pAb3 ELISA (pAb3 was
used for both coating and capture reactions). From the reactivity
tested with various gelatins, both ELISA methods are strongly re-
acted for bovine and porcine gelatin but gave low reaction with
fish gelatin. The rabbit pAb2-pAb1 ELISA method was reacted
mostly to porcine gelatin (alkaline process) while the goat pAb3-
pAb3 ELISA was reacted more strongly to bovine and porcine
R: Concise Reviews
in Food Science
gelatin (alkaline process). Both ELISAs were successful to detect
the existence of gelatin in all commercial foods that have been de-
clared to contain gelatin. The established sandwich ELISA meth-
ods produced no false positives, except for heated meat products
or false negatives when various commercial foods were analyzed
for their gelatin content. However, the rabbit pAb2-pAb1 ELISA
cross-reacted with boiled squid, while the goat pAb3-pAb3 ELISA
did not. Thus, the proposed goat pAb3-pAb3 ELISA method is a
reliable tool for the detection of gelatin contaminants present in
processed foods because it has weaker reactivity to cooked meat,
less cross-reactivity with boiled squid, and produced no false pos-
itives or negatives. However, the limitation of ELISA method is
the resulting of false positive for gelatinized heated meat. The
factors affecting the effectiveness of ELISA method are the pro-
cess involved in gelatin production where the alkaline process
of gelatin was sensitive than acidic process ones. This method is
also slightly affected by cross-reactivity with meat (pork, beef,
chicken), seafood (fish, squid, octopus, prawn, crab, shellfish,
and roe), and various commercial foods. However, this method
was quite difficult to distinguish between gelatin and cooked
meat.
Conclusion
Gelatin from bovine and porcine origins could be differen-
tiated using various analytical methods with certain limitations.
Most of the previous studies were focused on distinguishing of
raw gelatins and detection of gelatins in food products. The most
reliable method to differentiate gelatins could be ELISA methods
due to its ability to differentiate gelatins in raw form and incorpo-
rated in processed foods. For future research, fundamental studies
involving the extraction and purification of gelatin from gelatin-
based products are needed to assure the gelatin authenticity in
gelatin-based products and give satisfaction to consumers about
the sources of gelatin that are used in the commercial products.
Acknowledgments
The research (Project Nr: 05–02-10–0935RU) funded by Univ.
Putra Malaysia through Research Univ. Grant Scheme is gratefully
acknowledged.
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