Original Article

http://e-fas.org
Fish Aquat Sci 17(3), 299-304, 2014

Physicochemical Properties of Gelatin from Jellyfish Rhopilema

hispidum
Suengmok Cho1, Ju-Ryun Ahn2 Ja-Sung Koo2 and Seon-Bong Kim2*
Korea Food Research Institute, Seongnam, 463-746, Korea
1

Department of Food Science and Technology/Institute of Food Science, Pukyong National University, Busan 608-737, Korea
2

Abstract
The objective of this study was to elucidate the physicochemical characteristics of gelatin extracted from jellyfish Rhopilema
hispidum. We investigated the proximate composition, amino acids, gel strength, gelling/melting points, dynamic viscoelastic
properties, and viscosity of jellyfish gelatin. Jellyfish gelatin contained 12.2% moisture, 1.5% lipid, 2.1% ash, and 84.8% protein.
Glycine, hydroxyproline, proline, and alanine were the predominant amino acids. The gelatin showed a gel strength of 31.2 kPa, a
gelling point of 18.0°C, and melting point of 22.3°C. The gelatin was composed of α1-chain, α2-chain, β-chain, and γ-chain. During
cooling and heating process, jellyfish gelatin showed lower elastic modulus (G') and loss modulus (G'') values than mammalian
gelatin. Jellyfish gelatin did not show superior rheological properties to mammalian gelatin, like other fish gelatin; however, it can
be used in various food and cosmetic products not requiring high gel strength.

Key words: Gelatin, Jellyfish, Rhopilema hispidum, Physicochemical property, Gel strength

Introduction

Gelatin, a denatured protein derived from collagen by ther- physicochemical properties of gelatin from various fish sourc-
mal hydrolysis, has a rheological property of thermo-revers- es, such as harp seals (Phoca groenlandica; Arnesen et al.,
ible transformation between sol and gel (Stainsby, 1987; Cho 2002), yellowfin tuna (Thunnus albacares; Cho et al., 2005),
et al., 2004). As an important gelling agent, gelatin has widely shark cartilage (Cho et al., 2004), baltic cod (Gadus morhua;
been applied in the food, pharmaceutical, cosmetic, and pho- Kołodziejska et al., 2004), and black tilapia (Oreochromis
tographic industries (Cho et al., 2004, 2005). mossambicus; Jamilah and Harvinder, 2002).
Most commercial gelatin is produced from the by-products Although the physicochemical properties of gelatin from
of mammals such as pigs and cattle. However, bovine spon- various fish sources are known, information on jellyfish (Rho-
giform encephalopathy (BSE) and foot/mouth diseases have pilema hispidum) as a source of gelatin production is limited.
caused human health problems, and thus, mammal gelatin In Korea, jellyfish have increased substantially, causing vari-
sources have been limited (Cho et al., 2005). As a replace- ous problems. Therefore, utilization of jellyfish as alternative
ment, fish gelatin has been widely investigated. In addition, gelatin sources would be practical. Here, we investigated the
religious constraints (Kosher and Halal foods) and increasing physicochemical properties of gelatin from jellyfish through
health consciousness on the part of consumers have also re- analyses of proximate composition, amino acids, gel strength,
sulted in a high demand for fish gelatin (Kittiphattanabawon gelling point, melting point, dynamic viscoelastic properties,
et al., 2005). Numerous studies have reported production and and viscosity.

Received 23 April 2014; Revised 17 July 2014

© 2014 The Korean Society of Fisheries and Aquatic Science
This is an Open Access article distributed under the terms of the Creative
Accepted 18 July 2014
Commons Attribution Non-Commercial Licens (http://creativecommons.
org/licenses/by-nc/3.0/) which permits unrestricted non-commercial use, *Corresponding Author
distribution, and reproduction in any medium, provided the original work
is properly cited. E-mail: [email protected]

pISSN: 2234-1749 eISSN: 2234-1757 299 http://dx.doi.org/10.5657/FAS.2014.0299

Fish Aquat Sci 17(3), 299-304, 2014

Materials and Methods blue were heated at 100°C for 5 min. After heating, the so-
lution was injected on the gel, and electrophoresis was per-
Preparation of gelatin formed at 15 mA/gel with Mini-Protean 3 (Bio-Rad Labora-
tories, Hercules, CA, USA). The gel was separated, dyed in
Salted jellyfish were provided by Korea Jellyfish Inc. 0.25% (w/v) Comassie Brilliant Blue R250, and decolorized.
(Busan, Korea) and washed three times for salt removal. Sam- Calf skin collagen (Sigma-Aldrich, St. Louis, CA, USA) was
ples were kept at –20°C until gelatin extraction. The extrac- used as the marker protein.
tion of gelatin was performed according to Cho et al. (2005).
The jellyfish were washed with tap water for 12 h to remove Measurement of gel strength
foreign matter and then chopped. Samples were treated with
5 volumes (v/w) of 2% NaOH in a shaking incubator (200 Gel strength was measured according to Cho et al. (2005)
rpm) at 10°C for 8 h to remove non-collagen protein and to using rheometry (Compac-100; Sun Scientific Co., Tokyo, Ja-
swell the tissues. Following pretreatment, samples were neu- pan). Gelatin was dissolved with DW (6.67%, w/v) at 60°C for
tralized with 6 N HCl and washed with distilled water (DW). 30 min until completely dispersed and then kept at 7°C for 17
Gelatin extraction was performed in 6 volumes (v/w) of DW h. After cool maturation, gel strength was measured with the
at 60°C for 5 h while agitated. The extracted solutions were following conditions: plunger, 12.7 mm diameter; penetration
filtered using filter paper (No. 5A; Advantec, Tokyo, Japan), depth, 4 mm; penetration speed, 2 cm/min.
concentrated at 60°C, and dried at 50°C for 24 h in a hot-air
dryer (WFO-601SD; EYELA, Tokyo, Japan). Gelatin yields Measurement of gelling and melting points
were 38.5%:
Gelling and melting points were measured as described by
Gelatin weight (g)
Yield (%) = × 100 Gudmundsson (2002) and Cho et al. (2005). The gelling point
Jellyfish weight (g) was evaluated from the intersection point of the elastic modu-
lus (G', Pa) and the loss modulus (G'', Pa) during the cooling
Measurement of proximate components and pH process. The melting point was determined during the heating
process in the same manner.
Moisture content (oven-drying procedure), crude protein
(Kjeldahl), lipid (ether extraction), and ash content were esti- Measurement of dynamic viscoelastic properties
mated by the Association of Analytical Communites (AOAC,
2006). A factor of 5.55 was used to convert nitrogen values Dynamic viscoelastic properties were measured with a rhe-
to gelatin protein (Sarbon et al., 2013). pH was measured by ometer (Rheostress 1 RS30; HAAKE GmbH, Vreden, Ger-
melting 0.1 mg gelatin in 10 mL distilled water at 60°C with many). The concentration of gelatin was converted to 6.67%
a pH meter (Accumet model 15; Fisher Scientific, Waltham, with a water bath at 60°C. The measurement was performed at
MA, USA). All analyses were replicated three times. a frequency of 1 Hz and a temperature of 0.5°C/min; oscillat-
ing applied stress was at 3 Pa and the gap was at 4.2 mm. The
Analysis of amino acids temperature ranges were divided into two for measurement of
the elastic modulus (G', Pa) and loss modulus (G'', Pa): a cool-
Extracted gelatin (30 mg) was dissolved in 10 mL of 6 down from 40°C to 5°C and a heating from 5°C to 40°C.
N HCl containing 0.1% phenol and hydrolyzed in vacuum-
sealed glass tubes at 110°C for 24 h using norleucine as the Measurement of viscosity
internal standard. The hydrolysates were filtered with a glass
filter and vacuum-concentrated at 60°C. The concentrates Viscosity was measured according to Kittiphattanabawon et
were made up with 10 mL with citrate phosphate (pH 2.2) al. (2005) with a slight modification. Gelatin (0.04%, 100 mL)
and then analyzed with an automatic amino acid analyzer (S- was added to 0.1 M acetic acid at 60°C. Spindle No. 40 of a
433H; Sycam GmbH, Eresing, Germany). Brookfield Synchorolectic Viscometer (model DV II+; Brook-
field Engineering Lab, Mt. Prospect, IL, USA) was used to
Sodium dodecyl sulfate–polyacrylamide gel elec- measure viscosity at 60 rpm. Temperatures ranged from 15°C
trophoresis (SDS-PAGE) to 50°C, at 15°C/min. The experiment was carried out after
the solution was maintained at each temperature for 10 min.
SDS-PAGE was performed according to Laemmli (1970).
For polyacrylamide gels, 5% stacking gel and 6% separat- Measurement of denaturation temperature
ing gel were used. Gelatin solution (10 mg/mL) and tracking
dye mixtures containing 0.5 M Tris–HCl buffer (pH 6.8), 5% The denaturation temperature was measured according to
2-mercaptoethanol, 20% glycerol, and 0.1% bromophenol Kimura et al. (1988) with a slight modification. The denatur-

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 Cho et al. (2014) Characteristics of Jellyfish Gelatin

ation temperature was expressed by measuring the viscosity of A B

gelatin (0.03%, 5 mL) at intervals of 5°C between 20°C and
γ→
50°C with an Ostwald–Fenske viscometer (Cannon Instru-
ment Co., State College, PA, USA). During the measurement,
the temperature of the gelatin was maintained for 10 min at β→
the temperature ranges before the experiment was conducted.
The denaturation temperature (Td) was evaluated at the half
position of the measured value.

α2→
Statistical analysis
α1→
All experiments were analyzed with three repetitions per
sample using one-way analysis of variance (ANOVA; α =
0.05). Means were separated using Duncan’s multiple range
test (α = 0.05). Regression analysis for gel strength as a func- Fig. 1. SDS-PAGE patterns of gelatin from jellyfish Rhopilema hispidum.
Calf skin collagen was used as a maker protein. A, calf skin collagen; B,
tion of gelatin concentration and maturation time was per- jellyfish gelatin.
formed using the REG procedure in SAS (version 8.01; SAS
Institute, Cary, NC, USA).
of hydrogen bonds (Ledward, 1986). Generally, mammalian
gelatin contains more imino acids (Pro and Hyp) than fish
Results and Discussion gelatin (Gilsenan and Ross-Murphy, 2000; Haug et al., 2004).
In the present study, jellyfish gelatin showed lower imino acid
Proximate composition content than mammalian gelatin, as reported in previous stud-
ies. The contents of alanine and lysine in jellyfish gelatin were
The proximate composition and pH value of jellyfish gela- 6.88% and 2.49%, respectively. Gómez-Guillén et al. (2002)
tin are shown in Table 1. Jellyfish gelatin contained 12.2% reported that the low content of alanine causes poor gelation,
moisture, 75.3% crude protein, 1.5% crude lipid, and 2.1% and lysine stabilizes the gelatin structure by forming cross-
crude ash. The ash content of gelatin plays an important role linking structures between chains.
in the quality of gelatin. According to the US standards of food
(Gelatin, FCC, 1994), the maximum ash content of gelatin is Electrophoretic profiles
3%. Thus, jellyfish gelatin contains less ash than the regula-
tion level. The pH value of jellyfish gelatin was 7.32. Fig. 1. shows electrophoretic patterns of jellyfish gelatin
and calf skin collagen (a marker protein) by SDS-PAGE. The
Amino acid composition

Jellyfish gelatin contained high levels of glycine (Gly,

Table 2. Amino acid composition of gelatin extracted from jellyfish
18.90%), proline (Pro, 8.15%), and hydroxyproline (Hyp, Rhopilema hispidum
13.93%; Table 2). This originates from a repeated structure
Amino acids residues/1,000 residues
(Gly–Pro–Hyp) of collagen, the precursor of gelatin. Led-
Hydroxyproline 139.3
ward (1986) reported that gelatin has a repeated structure of Aspartic acid 54.6
Gly–X–Y. With Pro and Hyp in the X and Y positions, the Threonine 19.9
gelatin structure is stable. The total content of Gly–Pro–Hyp Serine 25.3
is an important factor that expresses thermal stability in gela- Glutamic acid 60.9
Proline 81.5
tin (Burjandze, 2000). Imino acids are involved in formation
Glycine 189.0
Alanine 68.8
Valine 19.4
Table 1. Proximate composition and pH value of gelatin extracted from Isoleucine 10.7
jellyfish Rhopilema hispidum Leucine 22.2
Tyrosine 4.5
Items Content or value
Phenyalanine 19.3
Moisture 12.2 ± 0.3% Lysine 24.9
Crude protein 75.3 ± 0.2% Histidine 6.2
Crude lipid 1.5 ± 0.3% Arginine 56.2
Crude ash 2.1 ± 0.3% Imino acids1 220.8
pH 7.32 1
Imino acids mean proline and hydroxyproline.

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Fish Aquat Sci 17(3), 299-304, 2014

50 100
A Cooling

40 a 80
a
Gel strength (kPa)

60
30

G' (Pa)
40
20

20
10

b b b b b b 0
0
0.5 1.0 1.5 2.0 3.0 4.0 5.0 6.7 40 30 20 10
Concentration of gelatins (%) Temperature (°C)

Fig. 2. Changes in the gel strength of gelatin from jellyfish Rhopilema 100
hispidum as affected by the concentration. Different letters (A, B) indicate B Heating
significant differences at level of probability of 5%. 80

60

G' (Pa)
calf skin collagen was composed of α-chains (α1:α2 = 1:2, <95
kDa), the β-component (cross-linked dimer of α-chains, <200 40
kDa), and the γ-component (cross-linked trimer of α-chains;
Gómez-Guillén et al., 2002). Jellyfish gelatin was found to be 20
composed of the α1-chain, the α2-chain, the β-chain, and the
γ-chain; the α1-chain was less clear than that in calf skin col- 0

lagen. In bone gelatin, the lower content of high-molecular-

weight fractions (β- and γ-chains) was associated with lower 10 20 30 40
viscosity, melting- and setting points, and a longer setting time Temperature (°C)
(Muyonga et al., 2004). Fig. 3. Changes in elastic modulus (G', kPa) during cooling (40-5°C) and
heating (5-40°C) process of gelatin solutions from jellyfish Rhopilema
Gel strength, and gelling and melting points hispidum. A cooling and heating rate was 0.5°C/min, and a 6.67% (w/v)
gelatin solution was used.

In the assessment of gelatin quality, physical properties such

as gel strength, and gelling and melting points are important.
The gelation of gelatin occurs by physical cross-linking, lead- concentration. Jellyfish gelatin formed a gel at higher concen-
ing to the formation of junction zones and ultimately a three- trations than porcine and bovine gelatin (5% vs. 1.5%; data
dimensional branched network (Gilsenan and Ross-Murphy, not shown). Gel strength is a function of complex interactions
2000). Generally, fish gelatin shows lower gel strength than determined by the amino acid composition, and the ratio of
mammalian gelatin (Norland, 1987; Choi and Regenstein, α-chains, and the amount of β-components (Cho et al., 2004).
2000). Among fish, tropical fish such as tilapia and tuna pos- Gómez-Guillén et al. (2002) reported that the gel structure of
sesses a superior gel strength to cold-water fish such as cod gelatin is more stable when the imino acid (Hyp and Pro) con-
(Gudmundsson and Hafsteinsson, 1997; Gómez-Guillén et tent is higher, and when the amount of aggregates of higher
al., 2002; Cho et al., 2005). The gel strength (31.2 kPa) of molecular weight is lower. The lower gel strength in jellyfish
jellyfish gelatin was lower than that of porcine (147.4 kPa) gelatin is likely due to a lower amount of total Gly+Hyp+Pro,
and bovine (107.9 kPa) gelatin (data not shown). Fig. 2 shows which stabilizes gelatin structures.
the changes in gel strength of jellyfish gelatin as affected by Gelling and melting points are also important indicators
of gelatin quality. Generally, mammalian gelatin possesses
higher gelling and melting points than fish gelatin (Choi and
Table 3. Gel strength, gelling point and melting points of gelatin ex- Regenstein, 2000; Gilsenan and Ross-Murphy, 2000; Gud-
tracted from jellyfish Rhopilema hispidum mundsson, 2002). The gelling and melting points of jellyfish
Items Values gelatin were 18.0°C and 22.3°C, respectively (Table 3). Mam-
malian gelatin has a much higher gel set temperature than
Gel strength (kPa) 31.2 ± 1.2
both warm- and cold-water fish gelatin (Avena-Bustillos et al.,
Gelling point (°C) 18.0
2006). Cho et al. (2005) reported that the respective gelling
Melting point (°C) 22.3 and melting points of mammalian gelatin were 23.8°C and

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 Cho et al. (2014) Characteristics of Jellyfish Gelatin

8 110
A Cooling
7 100

Relative viscosity (%)

90
5
G" (Pa)

80
4
70
3
60
2

1 50

0 40
40 30 20 10 10 15 20 25 30 35 40 45 50 55
Temperature (°C) Temperature (°C)
8 Fig. 5. Changes in relative viscosity of gelatin solution (0.04%, w/v) from
B Heating jellyfish Rhopilema hispidum at different temperatures.

6
G" (Pa)

The intersection point of G' and G" shows the gelling point
4 (Winter and Chambon, 1986). The G' values of jellyfish gela-
tin sharply increased when the temperature decreased during
cooling (<18°C), whereas G" values gradually increased. G'
2 and G" values of gelatin at 5°C were higher during the heat-
ing process than they were at 5°C during the cooling process
because the gelatin gel continued to stabilize for a few minutes
0
10 20 30 40 until measurement began. Gelatin with larger elastic modu-
Temperature (°C) lus values, also indicated by higher gelation temperatures,
contained higher concentrations of helical structures (Joly-
Fig. 4. Changes in loss modulus (G'', kPa) during cooling (40-5°C) and
heating (5-40°C) process of gelatin solutions from jellyfish Rhopilema Duhamel et al., 2002), indicating that mammalian gelatin pos-
hispidum. A cooling and heating rate was 0.5°C/min, and a 6.67% (w/v) sesses a higher melting point and is more thermostable than
gelatin solution was used. jellyfish gelatin.

Viscosity
33.8°C for bovine gelatin, and 25.6°C and 36.5°C for porcine
gelatin. The gelling and melting points of jellyfish gelatin Fig. 5. shows changes in the relative viscosity of jellyfish
were lower than those of mammalian gelatin. This tendency gelatin solution (0.04%, w/v) at different temperatures. At
has been reported in previous studies on fish gelatin, such as lower temperatures, the gelatin molecules begin to form triple
that from tuna (Cho et al., 2005) and tilapia (Gilsenan and helical junction zones to develop more cross-linking and to
Ross-Murphy, 2000; Gudmundsson, 2002). These results sug- eventually develop some network structure; the viscosity also
gest that jellyfish gelatin has useful physical properties differ- rapidly increases (Avena-Bustillos et al., 2006). At higher
ent from mammalian gelatin. temperatures, the gelatin molecules behaved as random coils
in solution, and all gelatins had low viscosity. When a gela-
Dynamic viscoelastic properties tin solution undergoes heat treatment, the hydrogen bonds are
broken and viscosity decreases (Nagai et al., 1999; Nagai and
Dynamic viscoelastic profiles were measured during the Suzuki, 2000, 2002). The viscosity of jellyfish gelatin solution
cooling (40°C–5°C) and heating (5°C–40°C) processes at a tended to decrease rapidly until the temperature reached 32°C
rate of 0.5°C/min. Figs. 3 and 4 show changes in the elastic and decreased gradually between 33°C and 50°C. According
modulus (G', Pa) and the loss modulus (G", Pa), respectively. to Kittiphattanabawon et al. (2005), when gelatin was extract-
The elastic modulus (G') and the loss modulus (G") are im- ed from the bones and skin of bigeye snapper, the viscosity of
portant indicators for the gelling ability of gelatin. In general, the gelatin decreased gradually between 35°C and 50°C. The
when the value of G" is higher than the value of G', a state of change in the viscosity of jellyfish gelatin showed a similar
sol occurs, whereas the opposite trend results in a state of gel. tendency.

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Fish Aquat Sci 17(3), 299-304, 2014

Acknowledgments Hydrocoll 18, 203-213.

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Joly-Duhamel C, Hellio D, Ajdari A and Djabourov M. 2002. All gelatin
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