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The mixtures of fish gelatin and κ-carrageenan had the gels
with varying degree of turbidity, depending on the concentration
of polymers, pH, ionic strength, and the nature of the added salt
(Haug et al. 2004). The highest gel strength was found when
20 mM KCl and 20 mM NaCl were added into the mixtures
of 1% (w/v) κ-carrageenan with 2% and 5% (w/v) fish gelatin,
respectively. However, these mixtures exhibited more turbid gel
than κ-carrageenan or fish gelatin alone since the system undergoes associative phase separation promoted by the release of
counterions (Piculell et al. 1995). Complexes of fish gelatin and
κ-carrageenan at 60◦ C were probably stabilized by electrostatic
interactions and the solutions were highly turbid, and at 4◦ C the
strongest gel was obtained (Haug et al. 2004).
Liu et al. (2007a) determined the hardness of gelatin/pectin
mixed gels with different ratios. The addition of pectin resulted
in the increased gel hardness. The strong interactions between

two polymers in the mixed solution resulted in a synergistic
effect. At the same gelatin content, the lower pectin content
added to the system resulted in a harder gel. The excess pectin
content formed the repulsive forces in the junction zones, which
might reduce the formation of linkages between the aggregated
helices, leading to weakened gel structures (Liu et al. 2007a).

Oxidation process
Free radical-mediated protein modification affects protein functionalities. Protein oxidation can lead to the formation of several
different kinds of protein cross-links (Stadtman 1998). For example, abstraction of H atoms from protein by radical could
result in the reaction with one another to form –C–C– protein cross-linked products. The oxidation of protein sulfhydryl
groups can lead to disulfide –S–S– cross-linked proteins. Additionally, the carbonyl groups obtained by the direct oxidation
of amino acid side chains of one protein may react with the
lysine amino groups of another protein to form Schiff-based
cross-linked products.
Fenton reaction, involving a mixture of ferrous ion (Fe2+ ) and
H2 O2 , generates hydroxyl radicals (HO• ) at room temperature
(Walling 1975, Fenton 1984) as shown in equation below:
Fe2+ + H2 O2 → Fe3+ + HO• + OH−
H2 O2 is largely used in oxidation process. Its oxidizing properties are not only due to the presence of an active oxygen atom
in the molecule, but also to its ability to participate in radical reactions, with the homolysis of the O–O bond, leading to
the formation of the HO• radical (Chedeville et al. 2005). HO•
radical can oxidize organic compounds in solution (Namkung
et al. 2008).
Aewsiri et al. (2009a) reported that uses of H2 O2 for bleaching of cuttlefish skin prior to gelatin extraction could improve
the bloom strength of gelatin gel. H2 O2 might induce the oxidation of protein with the concomitant formation of carbonyl
groups. Those carbonyl groups might undergo Schiff base formation with the amino groups, in which the protein cross-links
were most likely formed (Stadtman 1997). Moreover, OH• can
abstract H atoms from amino acid residues to form carboncentered radical derivatives, which can react with one another


401

to form C–C protein cross-linked products (Stadtman 1997).
The larger protein aggregates were mostly associated with the
improved bloom strength.
Additionally, free radical in protein could be generated by
irradiation, such as UV-irradiation and gamma-irradiation. Irradiation makes protein oxidized, followed by the generation of
free radical, resulting in either cross-linking (protein aggregation) or degradation of protein. Bhat and Karim (2009) reported
that gelatin treated with UV-irradiation for 60 minutes prior
to preparing the gel showed higher gel strength than the gelatin
treated with UV-irradiation for 30 minutes as well as that without
any UV-irradiation, respectively. Bessho et al. (2007) reported
that insolubility due to cross-linking of the gelatin hydrogels
was induced at doses above 8 kGy gamma-irradiation. Hydrocarbon groups (alkyl or a phenyl group of the side chains) are
the cross-linking sites of gelatin hydrogels.

APPLICATIONS OF GELATIN
Gelatin has been used widely in many sections of the food industry. The major uses cover jellies, confectionery, meat products,
and chilled dairy products. It can be used in the pharmaceutical
industry, especially for hard and soft capsule manufacture and in
the photographic industry, which uses the unique combination
of gelling agent and surface activity to suspend particles of silver chloride or light-sensitive dyes (Kragh 1977, Fiszman et al.
1999, Soper 1999, Choi and Regenstein 2000, Park et al. 2007,
Zhou and Regenstein 2007, Cheng et al. 2008, Binsi et al. 2009).
Due to the drawbacks of fish gelatin—that it does not gel
at room temperature and requires temperature below 8–10◦ C
for setting, it can also be used in other applications that do not
require a high bloom value such as for prevention of syneresis
and modification of food texture. Fiszman et al. (1999) studied
the effect of the addition of gelatin on the microstructure of acid

milk gels and yogurt and on their rheological properties. The
addition of 1.5% gelatin developed fairly firm and deformable
gels with almost total absence of syneresis. Dynamic rheology
showed that the yogurts with added gelatin exhibited more solidlike behavior than the ones prepared without it.
Gelatins from tuna or tilapia skin (warm-water fish) have
a melting point of 25–27◦ C (Choi and Regenstein 2000) and
have a bloom value of 200–250 g. These gelatins more closely
resemble bovine or pig gelatin, which melts at 32–35◦ C. Fish
gelatin with lower gel melting temperatures had a better release
of aroma and offered a stronger flavor (Choi and Regenstein
2000). By increasing the concentration of gelatin or by using
gelatin mixtures, desserts made from fish gelatins would be
more similar to desserts made from high bloom pork skin gelatin
(Zhou and Regenstein 2007).
Cheng et al. (2008) observed that combinations of fish gelatin
with pectin have been used to make a low-fat spread. A decrease in the fish gelatin to pectin ratio (3:0, 2:1, 1:1, and 1:2)
resulted in an increase in bulk density, firmness, compressibility,
adhesiveness, elasticity, and meltability. On the other hand, use
of gelatin/sodium alginate blends to form casings could lower
water losses and lipid oxidation during chilled storage as compared to pectin casing (Liu et al. 2007b). Recently, Binsi et al.


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(2009) used gelatin from the skin of bigeye snapper (Priacanthus hamrur) to modify the texture of threadfin bream mince
gel. The addition of fish gelatin (0.1–1%) to fish mince resulted
in higher storage modulus (G ) values from the beginning of
heating regime. A maximum G value of 443.7 kPa at 68.3◦ C
was obtained in the presence of 0.5% gelatin, which was 42%
higher than that of fish mince without the added gelatin.
Fish gelatins with low melting points could also be used in
dry products. One of the major applications of fish gelatin is
in the microencapsulation of vitamins and other pharmaceutical additives. Soper (1999) described a method for microencapsulation of food flavors such as vegetable oil, lemon oil,
garlic flavor, apple flavor, or black pepper with warm-water fish
gelatin (150–300 bloom). Park et al. (2007) patented a process
describing the preparation of a film-forming composition for
hard capsules composed of fish gelatin. Using transglutaminase
for cross-linking circumvented the problems caused by the low
gelling temperature property of fish gelatin.

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