J Food Sci Technol

DOI 10.1007/s13197-012-0681-4

ORIGINAL ARTICLE

A comparative study on the physical, chemical and functional

properties of carp skin and mammalian gelatins
George Ninan & Jose Joseph &
Zynudheen Abubacker Aliyamveettil

Revised: 7 February 2012 / Accepted: 14 March 2012

# Association of Food Scientists & Technologists (India) 2012

Abstract Carp species forms the bulk of the aquaculture gelling agents to replace mammalian gelatin led to patents
production in India and studies have shown that the filleting for fish gelatin production (Grossman and Bergman 1992;
waste of these species, particularly skin can be a good Holzer 1996) as well as several published methods for fish
source of gelatin. This study is a comparison of the gelatins gelatin production (Gomez-Guillen and Montero 2001;
from these unexploited sources with that of mammalian Gudmundsson and Hafsteinsson 1997; Nagai and Suzuki
gelatins to get a better understanding of their physicochem- 2000; Arnesen and Gildberg 2002). The commercial interest
ical and functional properties with respect to mammalian in fish gelatin has this far, however, been relatively low. This is
gelatins. The study showed that mammalian gelatins had due to sub-optimal physical properties compared to mammalian
significantly superior physical properties viz., higher viscos- gelatin. Common problems connected with fish gelatin from cold
ity, melting & setting temperature and faster setting time. water species, representing the majority of the industrial fisheries,
The odour scores were significantly higher (P<0.05) for are low gelling and melting temperature and low gel modulus
bovine and porcine skin gelatins (3.1–3.12), indicating that (Leuenberger 1991). Fish collagens are of interest to the food
they had a distinguishable odour and hence can be consid- processing industry as they are used to produce gelatin which is
ered as inferior to fish skin gelatins in organoleptic qualities. extracted from the collagen (Jayathilakan et al. 2011) The trash
The gel strengths of rohu and common carp skin gelatins fish, leather jacket is a good source of Type I collagen which has
were significantly lower than mammalian gelatins. Among got good thermal properties (Muralidharan et al. 2011).
the carp skin gelatins, grass carp skin gelatin was found to Warm water fish gelatins however, have properties quite
have better compatibility with gelatin from bovine and similar to mammalian samples. Gelatin from the skin of
porcine skins. yellow fin tuna (T.albacares) had a high gel strength (426
Bloom) in comparison with bovine and porcine gelatins
Keywords Carp skin gelatin . Mammalian gelatin . Physical while gelling and melting points were lower (Cho et al.
properties . Functional properties . Organoleptic quality 2005). Jamilah and Harvinder (2002) reported bloom
strength of 180.8 Bloom for gelatin extracted from black
tilapia skin. The gelatin from channel catfish skin showed
Introduction high gel strength of 276 Bloom (Liu et al. 2008). Similarly
gelatin from the skin of grass carp showed high contents of
Gelatin from marine sources (fish skin, bone and fins) has imino acids (proline and hydroxyproline of around 19.47 %)
been looked upon as a possible alternative to bovine and and medium gel strength 267 Bloom (Kasankala et al.
porcine gelatin, especially since the outbreak of the Bovine 2007). Type A gelatins extracted from skins and bones of
Spongiform Encephalopathy in the 80’s. Search for new young and adult Nile perch had Bloom values of 81–229
and 134–179 g, respectively (Muyonga et al. 2004). George
G. Ninan (*) : J. Joseph : Z. A. Aliyamveettil et al. (2010a) has reported that the gelatin extracted from the
Fish Processing Division,
skin of Rohu and Common carp had Bloom values of
Central Institute of Fisheries Technology (ICAR),
Cochin 682 029, Kerala, India 188.6 g and 181.3 g respectively. Carp skin gelatin based
e-mail: [email protected] films had significantly lower water vapour permeability and
 J Food Sci Technol

oxygen permeability than mammalian gelatin films which who were able to detect off odour in gelatin samples having
indicated the superior barrier properties of the latter (George a slight putrid odour were selected. Samples for sensory
et al. 2010b). These reports indicate that gelatin from fish evaluation were prepared by dissolving 0.5 g of gelatin in
resources of tropical waters have comparable properties 7 ml of distilled water, to obtain a solution containing
with that of gelatin from mammalian origin. Production approximately 6.67 % gelatin. The samples were prepared
and utilization of fish gelatin not only satisfies the needs in test tubes with screw caps and dissolved as described for the
of consumers, but also serves as a means to utilize some of Bloom samples. The samples were held in a water bath at
the byproducts of the fishing industry (Karim and Bhat 50 °C, with the screw caps lightly closed. Panelists were
2009). The fishery waste generated from the processing of instructed to remove the screw caps, sniff the contents and
cultured Indian Major Carps can be a potential source for the identify the odour they perceived as well as indicate the odour
production of gelatin. Hence the objective of this study is to intensity, using a six point scale (0 0 no odour, 1 0 very mild
compare carp skin gelatin with mammalian gelatin with and only perceivable on careful assessment, 2 0 mild but
respect to the physical, chemical and functional properties. easily perceivable, 3 0 strong but not offensive, 4 0 strong
and offensive, 5 0 very strong and very offensive).

Materials and methods Foam formation ability, foam stability, water-holding and
fat-binding capacities Form formation ability (FA), foam
Materials and methods stability (FS), Water-holding capacity (WHC) and fat-
binding capacity (FBC) of the gelatins were determined
The fish gelatin samples used for the study were Rohu skin based on the methods described by Cho et al. (2004). One
gelatin (RG), Common carp skin gelatin (CG) and grass gram of gelatin was placed in 50 ml distilled water and
carp skin gelatin (GG). The mammalian gelatins used were swollen. The sample solution was dissolved at 60 °C and
Type A Porcine Skin Gelatin of 300B (G2500) and Type B the foam was prepared by homogenizing at 10,000 rpm for
Bovine Skin Gelatin of 225B (G9382). Fish skin for the 5 min in a homogenizer (Euro Turrax, T20 B IKA Labor-
extraction of gelatin was collected in fresh condition from technik, Staufen, Germany). The homogenized solution was
the filleting waste of cultured Carps viz., Rohu (Labeo poured into a 250 ml measuring flask. The foam formation
rohita), Common carp (Cyprinus carpio) and Grass carp ability was calculated as the volume ratio of foam liquid.
(Ctenopharyngodon idella). Fish skin gelatins were The foam stability was calculated as the ratio of the initial
extracted using the procedure as essentially described by volume of foam to the volume of foam after 30 min.
Gudmundsson and Hafsteinsson (1997) with slight modifi- One gram of gelatin was placed in a centrifuge tube and
cations as outlined by George et al.(2010a) and freeze dried weighed (tube with gelatin). For measuring water-holding
using a Freeze Drier (Martin Christ, Gamma 1-16 LSC, capacity and fat-binding capacity, 50 ml distilled water or
Germany). The mammalian gelatins were supplied by M/s 10 ml sunflower oil added, respectively, and held at room
Sigma Aldrich Inc., St. Louis, USA. temperature for 1 h. The gelatin solutions were mixed with
vortex mixer for 5 s every 15 min. The gelatin solutions were
Proximate composition and pH The moisture, protein, fat then centrifuged at 450 g for 20 min in a REMI Cooling
and ash contents of the gelatin samples were determined by centrifuge (Model CPR 24, REMI Instruments, Maharashtra,
the AOAC (1995) methods. For protein determination, a India). The supernatant was filtered with Whatman No. 1 filter
Nitrogen conversion factor of 5.4 was used as per Eastoe paper and the volume recovered was measured. The difference
and Eastoe (1952). The pH of gelatin solution was deter- between the initial volume of distilled water/sunflower oil
mined using the British Standard Institution method, BSI added to the gelatin sample and the volume of the supernatant
757(1975). was determined, and the results were reported as ml of water/
oil absorbed per gram of gelatin sample.
Viscosity Viscosity was measured as per the method de-
scribed by Cho et al. (2006). The viscosity (cP) of 10 ml Melting point, setting point and setting time Determination
of the Gelatin solution of 6.67 % (w/v) was determined of melting point was based on the method by Wainewright
using Brookfield digital viscometer (Model DVE Brook- (1977). Gelatin solutions 6.67 % (w/w) were prepared and a
field Engineering Laboratories Inc., Middleboro, MA) 5-mL aliquot of each sample was transferred to a small
equipped with a No.1 spindle at 33±0.2 C. culture test tube of 12×75 mm. the samples were degassed
in vacuum chamber (Heraeus vacutherm—Germany). The
Sensory evaluation Determination of odour by sensory tubes were then covered with parafilm and heated in a water
evaluation was conducted as per the method of Muyonga bath (Julabo TW 20, Germany) at 60 °C for 15 min. It was
et al. (2004) using a ten member panel. Only individuals then cooled immediately in ice chilled water and matured at
J Food Sci Technol

10 °C for 16–18 h. Five drops of a mixture of 75 % chloroform Muyonga et al. 2004) . Moisture content in all the samples
and 25 % red dye were placed on the surface of the gel. The were below 10 % which is less than the limit prescribed for
gels were then put in a water bath (circulating bath—Haake edible gelatin i.e. 15 % (GME 2008). The ash content in all
D3) at 10 °C and the water heated at the rate of 0.2 °C per the samples were in the range of 0.97–1.18 %, much less
minute. The temperature at which the drops began to move than the recommended maximum limit of 2. % set for edible
freely down the gel was taken as the melting point. gelatin (GME 2008). The pH varies between 4.05 and 4.42
The method used for the determination of setting point in fish skin gelatins. Grass carp gelatin shows significantly
and setting time of gelatin was that described by Muyonga higher values for pH (P<0.05) than the other two gelatins.
et al. (2004). Gelatin solutions of 10 % (w/w) were prepared The values of pH for gelatin samples are outside the range
in thin wall (12 mm×75 mm) test tubes in the same way as prescribed for Type A Gelatin and Type B Gelatin. This is
described for the Bloom samples. The dissolved samples because the pretreatment method employed during the ex-
from the warm water bath were transferred to another water traction process involves both alkali and acid treatments. In
bath held at 40 °C (circulating bath—Haake D3). The bath mammalian gelatins, porcine skin gelatin has a pH of 7.5
was then cooled slowly at the rate of 0.2 °C per minute. A since it is a Type A gelatin and bovine skin gelatin has a pH
thermometer was inserted into the sample and lifted out at of 5.02 since it is a Type B gelatin.
30 s intervals. The temperature of the mixture at which the The main difference in the amino acid profile of carp skin
gelatin solution no longer dripped from the tip of the ther- gelatins and mammalian skin gelatins is the lower imino
mometer was recorded as the setting temperature. Setting time acid content in the latter. The imino acid content in carp skin
was determined on samples prepared in the same way as those gelatin ranges from 19.16 % to 20.86 % whereas for bovine
for the determination of the setting temperature. Samples were and porcine skin gelatin it is 22.91 and 23.7 % respectively
transferred to a water bath maintained at 10 °C (circulating (George et al. 2010a). Overall, fish gelatins have lower
bath—Haake D3). A rod was inserted in the gelatin solution concentrations of imino acids (proline and hydroxyproline)
and raised at intervals of 15 s. The time at which the rod could compared to mammalian gelatins, and warm-water fish
not detach from the gelatin sample was recorded as the setting gelatins (big eye-tuna and tilapia) have a higher imino acid
time. content than cold-water fish (cod, whiting and halibut)
gelatins (Eastoe and Leach 1977). Four amino acids viz.,
glycine, proline, hydroxyproline and alanine account for
Statistical analysis two out of every three amino acid residues in mammalian
gelatins (Balian and Bowes 1977). These four amino acids
All data were analysed using the analysis of variance accounted for 63.51 % and 62.59 % of the total amino acid
(ANOVA) and Duncan’s multiple test were carried out to residues in bovine and porcine skin gelatins respectively
determine the significance difference between the means. whereas for carp skin gelatins the corresponding values
Statistical package used in the study was SAS, Version 6 were less than 50 %, except in the case of grass carp skin
(1989). All the data represented are the means of triplicates. gelatin which had 52.46 % of the above mentioned amino
acids (George et al. 2010b). The stability of the collagens
and gelatins is also proportional to the glycine content, apart
Results and discussion from total imino acid content (Lehninger et al. 1993).
Studies by George et al. (2010b) has shown grass carp
Proximate composition and pH The proximate composi- gelatin had gel strength of 230.2 Bloom which is compara-
tions and pH of gelatins are given in Table 1. Crude Protein ble to the reported value for bovine skin gelatin (227.2 B). It
content was significantly higher (P<0.05) for grass carp was also reported that the bloom values of rohu and com-
skin gelatin and mammalian gelatins The crude protein mon carp skin gelatins were 188.6 and 181.3 Bloom respec-
content reported for fish skin gelatin from different sources tively which was significantly lower than mammalian
is in the range of 87–89 % (Jongjareonrak et al. 2006; gelatins.

Table 1 Proximate composition

and pH of carp skin and Rohu Common carp Grass carp Porcine Bovine
mammalian gelatins
Moisture (%) 8.1±0.12a 8.5±0.11b 7.2±0.20c 8.4±0.20bd 8.5±0.20bd
Protein (%) 90.4±0.70a 89.8±0.59a 91.2±0.20ab 91.3±0.14b 91.2±0.15b
Results are presented as mean±
standard deviation of n03. Lipid (% dwb) 0.57±0.071a 0.62±0.063b 0.41±0.031c 0.78±0.050d 0.41±0.032c
Values within a row with Ash (%) 1.2±0.04a 1.1±0.02b 1.1±0.07c 1.02±0.04d 0.97±0.072d
different superscripts are pH 4.1±0.04a 4.1±0.06a 4.4±0.04b 7.5±0.03c 5.0±0.03d
significantly different (P<0.05)
 J Food Sci Technol

Viscosity Among the gelatin samples, maximum viscosity skin has the highest melting point (29.1 °C) followed by
was noted for porcine skin gelatin (7.89 cP) followed by Rohu (28.1 °C) and Common carp (28.2 °C). The melting
grass carp gelatin (7.07 cP). Bovine skin gelatin and points of carp skin gelatins were found to be higher than
grass carp skin gelatin had similar values for viscosity. those reported for many other fish species viz., 8–10 °C for
Rohu skin gelatin and common carp skin gelatin had cod skin gelatin (Gudmundsson and Hafsteinsson 1997);
significantly lower values of viscosity (P <0.05) com- 24.3 °C for yellow fin tuna gelatin (Cho et al. 2005);
pared to the other three samples (Fig. 1a). Viscosity is 21.4–26.5 °C for Nile perch gelatin (Muyonga et al.
partially controlled by molecular weight and molecular size 2004); 22.5–28.9 °C for tilapia skin gelatin (Jamilah and
distribution (Sperling 2006). The viscosities of most of the Harvinder 2002). The melting temperature of gelatin has
commercial gelatins have been reported to be in the range of been found to correlate with the proportion of the imino
2.0 to 7.0 cP for most gelatins and up to 13.0 cP for specialized acids proline and hydroxyproline (both with a 5-membered
ones (Johnston-Banks 1990). pyrrolidine ring) in the original collagen (Ledward 1986;
Piez and Gross 1960; Veis 1964). The imino acid content of
Melting point The melting point of the gel samples are grass carp gelatin was maximum (20.80 %) followed by
illustrated in Fig. 1(b). Mammalian gelatins showed signif- common carp (19.50 %) and rohu (19.49 %) gelatins where-
icantly higher (P<0.05) melting points (32.2–32.6 °C) than as the imino acid content of bovine and porcine skin gelatin
carp skin gelatins. Among the carp skin gelatins, Grass carp is 22.9 and 23.7 % respectively (George et al. 2010b). The

a b c
9 35 c c
c
8 b 34 30
b c
7 33 c

Seting point (0C)

a a
Melting point ( 0C)
Viscosity (cP)

32 25
6 b
31 20 a a
5
4 30 b
29 a 15
a
3
28 10
2 27
1 5
26
0 25 0
Rohu Common Grass Bovine Porcine Rohu Common Grass Bovine Porcine Rohu Common Grass Bovine Porcine
carp carp carp carp carp carp

d e 2.5
f
120 c c 3.5 d
c c c 2 c c
Setting time(Seconds)

100 3 b
Foam stability

a b
Foaming ability

80 2.5 1.5 a
b
a a
2
60
1
1.5
40
1
0.5
20 0.5
0 0 0
Rohu Common Grass Bovine Porcine Rohu Common Grass Bovine Porcine Rohu Common Grass Bovine Porcine
carp carp n carp carp carp carp

g h i
5
Water holding capacity (ml / g of gelatin)

Fat binding capacity ( ml /g of gelatin )

3 c
4.5
2.5 c c c
4 b b b
3.5 a
2 b a
3 3.5 b b
2.5 3 a
1.5 a
2.5 a
Odour score

2
1 2
1.5
1.5
1 1
0.5
0.5 0.5
0 0 0
Rohu Common Grass Bovine Porcine Rohu Common Grass Bovine Porcine Rohu Common Grass Bovine Porcine
carp carp carp carp carp carp

Fig. 1 Physico-chemical quality characteristics of gelatins from different mammalian and carp skins (n03). Results are presented as mean±
standard deviation of n03. Bars super scribed with different letters are significantly different (P<0.05)
J Food Sci Technol

melting point values correspond to the imino acid content in gelatin had the maximum fat binding capacity (4.57 ml/g)
the samples. Gomez-Guillen et al. (2002) correlated the and common carp skin gelatin had the minimum water-
thermal stability of gelatin to the number and stability of holding capacity (1.76 ml/g). No significant differences
Proline rich region in collagen or gelatin molecules, which were observed in the water holding and fat binding capac-
are high in fresh warm water fish and mammalian species. ities of Grass carp and mammalian skin gelatins. Water-
holding and fat-binding capacities are functional properties
Setting point and setting time Setting point and setting time that are closely related to texture by the interaction between
of the gels are given in Fig. 1 (c) & 1 (d) respectively. components such as water, oil and other components. Fat
Mammalian gels have significantly higher setting temper- binding capacity depends on the degree of exposure of the
atures (31.6–31.8 °C) than carp skin gelatins. Common carp hydrophobic residues inside gelatin . Rohu skin gelatin had
had the lowest setting temperature (17.9 °C) and the highest the highest percentage of hydrophobic residue tyrosine
was for Grass carp (20.5 °C). Also the Grass carp gel (George et al. 2010b) among the five gelatins which could
showed a significantly faster setting time (p < 0.05) of explain its higher capacity for fat binding. Water-holding
68.6 s when compared to the other two gels. Muyonga et capacity is affected by the amount of hydrophilic amino
al. (2004) reported a setting temperature of 19.5 °C and a acids like hydroxyproline. In this study highest water hold-
setting time of 60 s for the gelatin from the skin of adult Nile ing capacity (2.27–2.30 ml/g) was observed for Grass carp
perch extracted at 50 °C which is similar to the values skin and mammalian gelatins since these had significantly
observed for Grass carp skin gelatin. Gudmundsson (2002) higher percentage of hydroxyproline (George et al. 2010b).
compared the rheological properties of fish gelatins (tuna,
tilapia, cod and megrim) with conventional bovine and Sensory evaluation Odour score of the gels is given in
porcine gelatins. The gelling (setting) and melting points Fig. 1 (i). The odour scores were significantly higher
of tilapia gelatin (18.2 °C and 25.8 °C respectively) were the (P<0.05) for bovine and porcine skin gelatins (3.1–3.12)
highest among the fish gelatins and was comparable to low than carp skin gelatins, indicating that they had a distin-
molecular weight porcine and bovine gelatins. The gel set- guishable odour and hence can be considered as inferior to
ting time was significantly faster for mammalian gels. Grass fish skin gelatins in organoleptic qualities. Choi and Regenstein
carp skin gel had a setting time of 68.6 s which is comparable (2000) observed that fish gelatins had less off odour and better
to mammalian gels. Bovine and porcine gelatins have consid- aroma than pork gelatins on sensory evaluation. They noted
erably higher gelling and melting points than most fish gelat- that flavored fish gelatin dessert gel product had less undesir-
ins, and the high gelling and melting points expand the range able off-flavors and off-odors, with more desirable release of
of gelatin application. Setting temperature of gelatin has also flavor and aroma than the same product produced with pork
been found to correlate with the imino acid content which is gelatin possessing equal Bloom values, but a higher melting
typically ∼24 % for mammals and 16–18 % for most fish point. Muyonga et al. (2004) has reported that the gelatins
species (Choi and Regenstein 2000; Gilsenan and Ross- prepared from the skin and bone of Nile Perch were found to
Murphy 2000; Gudmundsson 2002; Leuenberger 1991). be free of fishy odour and to have a mild putrid odour with a
mean hedonic score of 2–2.5 with activated carbon treatment.
Foaming ability and foam stability The foaming ability and Strong fishy odour was reported for freeze dried gelatin pre-
foam stability of carp skin and mammalian gelatins are pared from the skin of black tilapia (Jamilah and Harvinder
given in Fig. 1 (e) & 1 (f) respectively. Grass carp skin 2002). Gudmundsson and Hafsteinsson (1997) reported that for
and mammalian gelatins exhibited better foam formation gelatin extraction from cod skin, the odor was absent or barely
abilities (2.9) than Rohu and Common carp skin gelatin. detectable if sulphuric acid and sodium hydroxide were used in
The hydrophobic areas on the peptide chain are responsible low concentrations. Grossman and Bergman (1992) have
for giving gelatin its emulsifying and foaming properties developed a method that can make the gelatin odorless.
(Cole 2000; Galazka, et al. 1999). Foam stability was sig-
nificantly higher for mammalian gelatins (1.4–1.6) than for
carp skin gelatins (1.8–1.9). The reduced foam formation Conclusion
and stability may be due to aggregation of proteins which
interfere with interactions between the protein and water A comparative study of mammalian skin gelatins and carp
needed for foam formation (Kinsella 1977). skin gelatins showed that mammalian skin gelatins had
significantly higher viscosity, melting & setting temperature
Water holding and fat binding capacities Water holding and and faster setting time than carp skin gelatins. The odour
fat binding capacities of carp skin and mammalian gelatins scores were higher for mammalian gelatins, indicating that
are given in Fig. 1 (g) & 1 (h) respectively. Rohu skin they had a distinguishable odour and hence can be considered
 J Food Sci Technol

as inferior to carp skin gelatins in organoleptic qualities. Foam George N, Joseph J, Zynudheen A (2010b) Physical, mechanical, and
barrier properties of carp and mammalian skin gelatin films. J
formation ability was similar for mammalian and Grass carp Food Sci 75(9):E620–E626
skin gelatins and mammalian skin gelatins exhibited signifi- Gilsenan PM, Ross-Murphy SB (2000) Rheological characterisation of
cantly better foam stability than carp skin gelatins. No signif- gelatins from mammalian and marine sources. Food Hydrocoll
icant differences were observed in the water holding and fat 14:191–195
GME (2008) Gelatin manufacturers of Europe. http://www.gelatine.org/
binding capacities of Grass carp and mammalian skin gelatins. en/gelatine/overview/127.htm (accessed July 22, 2008)
Among the carp skin gelatins, grass carp skin gelatin was Gomez-Guillen MC, Montero P (2001) Extraction of gelatin from
found to have better compatibility with gelatin from bovine megrim (Lepidorhombus boscii) skins with several organic acids.
and porcine skins. J Food Sci 66(2):213–216
Gomez-Guillen MC, Turnay J, Fernandez-Diaz MD, Ulmo N, Lizarbe
MA, Montero P (2002) Structural and physical properties of
gelatin extracted from different marine species: a comparative
Acknowledgments The authors are thankful to the Director, Central study. Food Hydrocoll 16:25–34
Institute of Fisheries Technology for according permission to publish Grossman S, Bergman M (1992) Process for the production of gelatin
the paper. The assistance rendered by the technical staff of the Fish from fish skins. US patent 5,093,474
Processing Division of the Institute is gratefully acknowledged. Gudmundsson M (2002) Rheological properties of fish gelatin. J Food
Sci 67:2172–2176
Gudmundsson M, Hafsteinsson H (1997) Gelatin from cod skins as
affected by chemical treatments. J Food Sci 62:37–47
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