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Process Biochemistry 47 (2012) 17791784

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Process Biochemistry
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Process for extracting gelatin from marine snail (Hexaplex trunculus): Chemical
composition and functional properties
Zied Zarai
a
, Rak Balti
b,
, Hafedh Mejdoub
a
, Youssef Gargouri
a
, Adel Sayari
a
a
Laboratoire de Biochimie et de Gnie Enzymatique des Lipases, Ecole Nationale dIngnieurs de Sfax, B.P. 1173, 3038 Sfax, Tunisia
b
Laboratoire de Gnie Enzymatique et de Microbiologie, Ecole Nationale dIngnieurs de Sfax, B.P. 1173, 3038 Sfax, Tunisia
a r t i c l e i n f o
Article history:
Received 9 March 2012
Received in revised form2 June 2012
Accepted 4 June 2012
Available online 18 June 2012
Keywords:
Gelatin
Marine snail
Hexaplex trunculus
Functional properties
Gel strength
a b s t r a c t
Gelatin was extracted, for the rst time, from the meat of Tunisian marine snail by the acid extraction
process with a yield of 3g/100 g. Snail meat gelatin (SMG) had high protein (88.62%) but low fat (0.77%)
content and contained a high number of imino acids. SMG showed high band intensity for - and -
components and some degradation peptides. The absorption bands of SMG in Fourier transform infrared
spectra were mainly situated in the amide band region (amide I and amide II). The gel strength of the SMG
(103g) was lower than those from other marine species reported in the literature. SMG exhibited a low
foamcapacity (75.44%) but a high emulsifying stability (38.12 min) and WHC (120%). It can be concluded
from the present study that snail meat is a prospective source to produce gelatin in good quality with
desirable functional properties.
Crown Copyright 2012 Published by Elsevier Ltd. All rights reserved.
1. Introduction
Gelatinis anirreversiblythermallydenaturedandpartlyhydrol-
ysed form of collagen [1]. In the food industry, gelatin has been
widely applied as an ingredient to improve the elasticity, consis-
tency and stability of foods. Depending on the method in which
collagens are pre-treated, two different types of gelatin with dif-
ferent characteristics including type-A, acid-treated collagen, and
type-B, an alkaline treated counterpart, can be produced [2]. Acid
treatment is the most suitable treatment for less fully cross-linked
collagens commonly found in pig or sh skins, whereas alkaline
treatment is appropriate for the more complex collagens found in
bovine hides [1,3].
Bovine and porcine skin and bone have usually been utilized
commercially for gelatin production. However, in some countries,
the use of gelatin fromwarm-blooded animals is restricted owing
to the transmission of bovine spongiform encephalopathy and
religious reasons [4]. To date, however, few alternatives are avail-
able, and as a result it has not been possible to eliminate gelatin.
Researchers fromacademia and industry are continually searching
for an alternative to gelatin, and to nd newsources of gelatin that
might be more favourably viewed. Therefore, gelatin frommarine
resources is a possible alternative for mammalian gelatins [5].

Corresponding author. Tel.: +216 74 274 088; fax: +216 74 275 595.
E-mail address: rakbalti1981@gmail.com(R. Balti).
Gelatin is a product of rapidly growing market. In 2003,
the world market for gelatin reached 278,300tonnes; consist-
ing of 42.4% from pig-skin origin, 29.3% bovine hides, 27.6%
bones and 0.7% from other sources [6]. In previous years, Karim
and Bhat [7] reported that the annual world output of gelatin
increased to 326,000tonnes with the highest source being pig-
skin (46%), followed by bovine hides (29.4%), bones (23.1%) and
other sources (1.5%). At present, the sh gelatin production is very
low, yielding about 1% of the annual world gelatin production of
270,000metric tonnes [8].
Recently, most of the published data is about gelatins from
various sh species such as brownbanded bamboo shark (Chiloscyl-
lium punctatum) and blacktip shark (Carcharhinus limbatus) skins
[9], grey triggersh skin [10], tuna heads [11] and cuttlesh skin
[12] have been extracted and characterized. However, few studies
have focused and little information regarding the characteristics of
gelatins frommarine invertebrate species, suchas marine snail, has
been reported.
Tunisias marine sheries produce several thousand metric
tonnes of shandshellshannually, mainlyfor exportation. Marine
snail (Hexaplex trunculus) is Tunisias new leading economically
important shellshspecies. H. trunculus (also knownas Murex trun-
culus or the banded dye-murex) is a medium-sized species of sea
snails, a marine gastropod mollusc in the family Muricidae, the
murex shells or rock snails.
Therefore, the aims of this investigation were to extract gelatin
fromthe meat of marine snail (H. trunculus) and to study its physic-
ochemical characteristics as well as its functional properties.
1359-5113/$ see front matter. Crown Copyright 2012 Published by Elsevier Ltd. All rights reserved.
http://dx.doi.org/10.1016/j.procbio.2012.06.007
1780 Z. Zarai et al. / Process Biochemistry 47 (2012) 17791784
2. Materials and methods
2.1. Materials
Marine snails (H. trunculus) were collected from the sh market of Sfax city
(Tunisia). The samples were placed on ice and transported, immediately, to the lab-
oratory. The outside of H. trunculus was thoroughly cleaned with fresh cold running
water. The shell was opened manually. Neither heat nor anaesthetics were used
before opening the shells, and it was ensured that no cuts were made or the soft
tissues damaged at this stage. The inside was rinsed with fresh cold running water
to remove sand or other foreign material. The meat was removed fromshell by sep-
arating adductor muscles and tissue connecting at hinge and carefully removing the
visceral mass. In each case, meat of snails was blended then stored at 20

C until
use.
2.2. Gelatin extraction
Snail (H. trunculus) meat was rstlysoakedin0.02MNaOHwithatissue/solution
ratio of 1:6 (w/v) for 60min at roomtemperature to remove non-collagenous pro-
teins and pigments. The mixture was stirred continuously and the alkaline solution
was changed every 30min. The pretreatment sturry was centrifuged at 6000g for
5 min using a Hermele Z36HK refrigerated centrifuge (Hermle Labortechnik GmbH,
Wehingen, Germany). The pelleted tissue was washed by resuspension in deionized
water with stirring at room temperature for 10min, followed by centrifugation at
6000g for 5min. The gelatin was extracted fromthe washed pelleted tissue with
3% acetic acid at pH 4.0 with a tissue/solution ratio of 1:6 (w/v) for 9h at 60

C with
gentle stirring. The mixture was then centrifuged at 6000g for 10min to remove
insoluble material and the gelatin supernatant was dialysed against 5 volumes of
deionized water. Finally, the supernatant was collected and freeze-dried (Bioblock
Scientic Christ ALPHA 1-2, IllKrich-Cedex, France). The powder obtained referred
to as snail meat gelatin (SMG) was stored at 4

C until used.
2.3. Proximate analysis
The moisture, ash and fat contents of the gelatin powder were determined
according to the AOAC methods number 927.05, 942.05 and 920.39 B, respectively
[13]. The protein content was determined by estimating its total nitrogen content
by Kjeldahl method according to the AOAC method number 984.13 [13]. A factor
of 5.4 was used to convert the nitrogen value to protein. All measurements were
performed in triplicate.
The yield of gelatin was calculated based on wet weight of fresh tissue.
Yield (%) =
Weight of freeze dried gelatin (g)
Wet weight of fresh tissue (g)
100
2.4. Determination of gel strength
Gel strength of gelatin was determined according to the method of Gmez-
Guilln et al. [3]. Gelatin sample was dissolved in distilled water at 60

C to obtain
the nal concentration of 6.67% (w/v). The solution was stirred for 30min until the
gel was solubilizedcompletelyandcooledina refrigerator at 7

Cfor 1618h. Thegel


strengthof gelatingel was determinedusinga Model TA-TX2texture analyzer witha
5 kNloadcell equippedwitha 1.27cmdiameter at-facedcylindrical Teonplunger.
The dimensions of the sample were 3.8cm in diameter and 2.7cm in height. Gel
strength was expressed as maximumforce (in g), required for the plunger to press
the gel by 4mmdepression at a rate of 0.5mm/s. The measurement was performed
in triplicate.
2.5. Determination of gelatin colour and gel clarity
The colour of dry gelatin sample was determined using a ColorFlex spectro-
colorimeter (Hunter Associates Laboratory Inc., Reston, VA, USA) based on three
colour co-ordinates, namely L (lightness), a (redness/greenness) and b (yellow-
ness/blueness). The sample was lled in a 64mm glass sample cup with three
readings in the same place and triplicate determinations were taken per sample.
The white tile and black glass were used to standardize the equipment. Clarity
was determined by measuring transmittance (%T) at 620nmin spectrophotometer
(Thermo spectronic, Cambridge, UK) through 6.67% (w/v) gelatin solution, prepared
as described previously.
2.6. Determination of amino acid composition
Gelatin samples were oxidized for 17h with a performic acid/phenol mixture,
hydrolysed in 6M HCl for 24h at 110

C (boiled under reux), pH-adjusted to 2.2,


diluted with 0.2mol/l sodiumcitrate loading buffer, pH2.2, and micro-ltered with
0.45mmSpartan membrane lter prior to analysis on a Beckman 6300 amino acid
analyzer (Beckman Instruments Inc., Fullerton, CA, USA).
2.7. Electrophoretic analysis
SDS-polyacrylamide gel electrophoresis (SDS-PAGE) was performed as
described by Laemmli [14] using 70g/l resolving gel and 40g/l stacking gel. After
electrophoresis, the gel was stained with 1g/l Coomassie brilliant blue R-250, dis-
solved in water, methanol and trichloroacetic acid (5:4:1), and de-stained using a
solutioncontaining methanol, distilledwater, andacetic acidat a ratio of 5:4:1. After
electrophoresis, the gel was stained with Coomassie Brilliant blue R-250.
2.8. Fourier transforminfrared spectroscopy
FT-IR spectra were obtained by a Nicolet Nexus FT-IR spectrometer (Thermo
Electron Corporation). The snail gelatin was tested by infrared analysis with the KBr
method.
2.9. Determination of emulsifying properties
Theemulsionactivityindex(EAI) andtheemulsionstabilityindex(ESI) of gelatin
were determined according to the method of Pearce and Kinsella [15] with slight
modications. The gelatin solutions were prepared by dissolving dry gelatin in dis-
tilled water at 60

C for 30min. Thirty millilitres of gelatin solutions 1% (w/v) were


homogenized with 10ml of soybean oil for 1min at room temperature (221

C)
using Moulinex

R62 homogenizer. Aliquots of the emulsion (50l) were taken


fromthe bottomof the container at 0and10minafter homogeneization, anddiluted
100-fold with 0.1% SDS solution. The mixtures were mixed thoroughly for 10s using
a vortex mixer. The absorbance of the diluted solutions was measured at 500nm
using a spectrophotometer (T70, UV/VIS Spectrometer, PG Instruments Ltd., China).
The absorbances measured immediately (A
0
) and 10min (A
10
) after emulsion for-
mation were used to calculate the emulsifying activity index (EAI) and the emulsion
stabilityindex(ESI) inaccordancewithas follows PearceandKinsella[15] as follows:
EAI (m
2
/g) =
2 2.303 A
0
N
c 10, 000
where N refers to dilution factor, c to the weight of protein per unit volume (g/ml),
and to the oil volumetric fraction (0.25). All determinations are means of at least
three measurements.
ESI (min) =
A
0
10
A
0
A
10
2.10. Determination of foaming properties
Foam expansion (FE) and foam stability (FS) of gelatin solutions were tested
according to the method of Shahidi et al. [16], with a slight modication. Twenty
millilitres of gelatin solutions (1%, w/v) were homogenized using a Moulinex

R62
homogenizer to incorporate the air for 1min at room temperature (251

C). The
whipped sample was then immediately transferred into a 50ml graduated cylinder,
and the total volume was measured at 0, 30 and 60min after whipping. Foamcapac-
ity was expressed as foam expansion at 0min, which was calculated according to
the following equation:
FE (%) =
VT V
0
V
0
100
Foamstability was calculated as the volume of foamremaining after 30 and 60min.
FS (%) =
Vt V
0
V
0
100
where VT is the total volume after whipping (ml); V
0
is the volume before whipping;
Vt is the total volume after leaving at roomtemperature for different times (30 and
60 min). All determinations are means of at least three measurements.
2.11. Determination of water holding capacity
Water holding capacity (WHC) of gelatin sample was measured by a partially
modied method of Lin et al. [17]. Dry gelatin (0.5g) was placed in a centrifuge
tube and weighed. Distilled water (50ml) was added and held at roomtemperature
for 1h. The gelatin solution was mixed with vortex mixer for 5s every 15min. The
mixture was then centrifuged at 450g for 20min. The upper phase was removed
and the centrifuge tube was drained for 30min on a lter paper after tilting to a 45

angle. The water holding capacity was calculated as the weight of the contents of
the tube after draining divided by the weight of the dried gelatin, and expressed as
the weight% of dried gelatin.
2.12. Statistical analysis
All data were subjected to Analysis of Variance (ANOVA) and differences
between means were evaluated by Duncans Multiple Range Test. The SPSS statistic
program(Version 10.0) (SPSS, 1.2, 1998) was used for data analysis.
Z. Zarai et al. / Process Biochemistry 47 (2012) 17791784 1781
Table 1
Proximate composition of marine snail meat and the extracted gelatin. Values are
given as meanSD fromtriplicate determination.
Composition (%) Snail meat Marine snail gelatin
Moisture
a
69.92 1.59a 6.83 0.71b
Protein
a
15.74 0.40a 88.62 0.45b
Fat
a
8.99 0.28a 0.77 0.21b
Ash
a
4.98 0.25a 0.82 0.05b
Values in the same rowwith different letters (a,b) differed signicantly (p<0.05).
a
Values are given as meanSD fromtriplicate determinations.
3. Results and discussion
3.1. Composition of snail gelatin
The proximate composition of snail meat and SMG is shown in
Table 1. Fresh snail meat contained moisture as the major compo-
nent (69.92%), followed by protein (15.74%) and fat (8.99%). SMG
had high protein (88.62%) and lowash (0.82%) and fat (0.77%) con-
tents, suggesting the efcient removal of fat and minerals fromthe
meat material. Muyonga et al. [18] reported that protein contents
of gelatins derived fromskins and bones of young Nile perch were
88.8%and83.3%, respectively. Gelatins fromskins of bigeyesnapper
and cuttlesh had protein contents of 87.9% and 91.35%, respec-
tively [12,19]. Gelatin as such is a pure protein and nothing else.
So, the presence of ash, lipid and other impurity at very low con-
tents are important for the quality of gelatins. SMG had lower ash
content than the recommended maximumvalue of 2.5%.
Gelatin was extracted fromsnail meat with a yield of 3% on the
basis of wet weight. This result was similar to those obtained from
squid (2.6%) [3], channel catsh (3.9%) [20] and mackerel (3.5%)
[21], but lower than other marine species, such as grey triggersh
(5.6%) [10], cuttlesh (7.8%) [12] and tuna (18.1%) [11]. The differ-
ence in gelatin recovery fromdifferent species could be attributed
to the intrinsic characteristics of the matrix used for extraction
and collagen molecules, the collagen content, the amount of sol-
uble components in the matrix, the loss of extracted collagen
through leaching during the series of washing steps or to an incom-
plete collagen hydrolysis [22], since these properties vary with the
species and the age of the marine species. Moreover, the degree
of conversion of collagen into gelatin depends on the processing
parameters (temperature, extraction time and pH); the pretreat-
ment conditions, and the properties and the preservation method
of the starting rawmaterial [2].
3.2. Amino acid composition of gelatin
The amino acid composition of marine snail gelatin expressed
as residues/1000 total amino acid residues is shown in Table 2. The
amino acid prole obtained for SMG is comparable to those from
gelatins extracted from other marine species and mammals [3,5],
being glycine the most predominant residue (321 residues/1000
residues). Other important residues found in SMG were alanine
(73), arginine (51), Serine (61), aspartic acid (67), glutamic acid
(99) and the imino acids proline (105) and hydroxyproline (98).
The content of the acid residues was higher in comparison to those
reported previously, and these differences may be due to the acid
pretreatment, since during this step in the gelatin extraction, some
of the glutamine and asparagine residues might have converted or
oxidized into their acidic forms.
The high content of proline (Pro) and hydroxyproline (Hyp)
in the samples were indicative of collagen and/or its derivatives
[23]. The imino acids (Pro+Hyp) content (20%) was higher to
those previously reported for cuttlesh (Sepia ofcinalis) and
other marine gelatins [3,5,12]. Both residues are known to impart
considerable rigidity to the collagen structure [2]. The stability
Table 2
Amino acid composition of marine snail (H. trunculus) gelatin.
Amino acids
a
Marine snail gelatin
Hydroxyproline (Hyp) 98
Aspartic acid (Asx) 67
Threonine (Thr) 28
Serine (Ser) 61
Glutamic acid (Glx) 99
Proline (Pro) 105
Glycine (Gly) 321
Alanine (Ala) 73
Cysteine (Cys) 0
Valine (Val) 22
Methionine (Met) 2
Isoleucine (Ile) 12
Leucine (Leu) 23
Tyrosine (Tyr) 9
Phenylalanine (Phe) 10
Hydroxylysine (Hyl) 8
Histidine (His) 3
Arginine (Arg) 51
Lysine (Lys) 8
Total 1000
Imino acids (Pro+Hyp) 203
Asx=Asp+Asn; Glx=Glu+Gln.
a
Determinations were performed in triplicate and data correspond to mean
values. Standard deviations were in all cases lower than 2%. Proline and lysine
hydroxylation are also shown (meanSD).
of the triple helical structure in gelatin has been associated
with the total content of pyrrolidone amino acids, proline and
hydroxyproline [24]. Hydroxyproline plays an important role in
the stabilization of the triple helical strands of collagen via its
hydrogen bonding ability through its OH group [24]. In addition,
the amounts of these imino acids especially that of Hyp depend on
the environmental temperature in which the sh lives, this in turn
affects the thermal stability of collagens and their derivatives.
3.3. Molecular weight distribution
Functional properties of gelatins are inuenced by the amino
acid composition, the distribution of the molecular weights, struc-
tures, and composition of their subunits. Protein patterns of gelatin
fromsnail meat under reducing condition are shown in Fig. 1.
1
-
and
2
-chains were found as the major components and similar to
that of standard collagen type I. -Component was also observed in
the gelatin fromsnail meat. Gelatin with high proportion of and
chains has also been extracted from cuttlesh [15], and Alaska
pollock [28]. In addition, proteins with molecular weights lower
than -chains (100kDa) were also observed in the snail meat
gelatinsample. This might be due to the degradationof , - and/or
-components duringgelatinextractionor preparation. Theextrac-
tion at higher temperature led to lower molecular weight peptides.
Heat-induce breakage of protein components in gelatin occurred
during the extraction process of Nile perch skin gelatin and was
enhancedwithhigher temperature of extraction[18]. Furthermore,
the degradationof gelatinfrombigeye snapper skincausedbysome
proteinases during extraction process had been reported [19]. The
formation of degradation peptides is associated with the low vis-
cosity, low melting point, low setting point, high setting time, as
well as decreased bloomstrength of gelatin [18,24].
3.4. Fourier transformed-infrared spectroscopy
The frequencies at which major peaks occurred in the SMG
FT-IR spectrum are shown in Fig. 2. Four main regions were iden-
tied: 36002300cm
1
(amide A), 16561644cm
1
(amide I),
15601335cm
1
(amide II) and 1240670cm
1
(amide III). These
peaks were similar to those reported by Muyonga et al. [26]. The
1782 Z. Zarai et al. / Process Biochemistry 47 (2012) 17791784
Fig. 1. SDS-PAGE patterns of marine snail (H. trunculus) gelatin. 1: 30g; M: molec-
ular weight markers; : -chain; 1:
1
-chain; 2:
2
-chain.
amide A peak absorption is due to N H stretching, amide I peak to
C O stretching, amide II peak to N H bending and C N stretching
vibrations, while the amide III peak is a complex system mainly
associated with CH
2
residual groups fromglycine and proline [27].
The absorption in the amide I region is probably the most useful
for infrared spectroscopic analysis of the secondary structure of
proteins. Its exact location depends on the hydrogen bonding and
conformation of the protein structure. In our study, the amide I
peak was observed at 1656cm
1
, which is in agreement with data
reported by Liu et al. [28], who stated that the absorption peak at
1650cm
1
was characteristic pattern reecting the amide I of head
bone gelatin of channel catsh.
Since most proteins have mixedsecondarystructures, the amide
I band often shows several components or shoulders, consequently
deconvolution studies can be applied to further investigate con-
formation changes. In comparison to the FT-IR spectra for other
marine gelatins [29,30], SMG showed lower intensity in the amide
I, II and III bands. These spectral changes are indicative of greater
Fig. 2. Fourier transform infrared (FTIR) spectra of marine snail (H. trunculus)
gelatin.
disorder in gelatin, and are associated with the loss of triple helix
state, as well as a decrease in molecular order. Thus, the differences
detected in the present work might be due to denaturation of col-
lagen into gelatin, which in turn provoke a change in the collagen
secondary structure. The extent of these changes seems to be inu-
enced by the gelatin extraction conditions, the number of native
crosslinks in the collagen structure, and the amount of collagenous
tissues fromwhich gelatin is extracted [26,29].
3.5. Gel strength
Gelatin is highly capable of forming hydrogen bonds with water
molecules to form a stable three-dimensional gel. Gel strength is
one of the most important functional properties of gelatin, and sh
gelatin typically has lower gel strength than mammalian gelatin
[4]. Gel strength of gelatin from marine snail (H. trunculus) meat
was shown in Table 3.
Thegel strengthobtainedinthis study(103g) was similar tothat
of salmon (108g) [31] and bigeye snapper (105g) [19] and lower
than that of cuttlesh (181g) [12], grey triggersh (168g) [10], and
Nile perch (229g) [18].
Generally, the gel strength of sh gelatin has been reported
in a wide range 124426g, compared to 200300g for bovine or
porcine gelatin. The difference in gel strength may possibly be
due to the lower content of imino acids, proline and hydroxypro-
line found in sh gelatine (1618%) compared to the mammalian
gelatines (24%). Other than the origin of the rawmaterials, the dif-
ferences in extraction process used and the intrinsic properties of
collagen which varies among sh species could be explain the dif-
ferences in gel strength. This is supported by an example on gelatin
extraction with different concentrations of sodiumhydroxide and
acetic acid [25].
3.6. Gelatin colour and gel clarity
The colour of gelatin extracted fro marine snail (H. trunculus)
was expressed in terms of L, a, and b and there were presented in
Table 3. In general, satisfactory gelatin should have little colour.
Marine snail gelatin showed a high lightness value (L). Gelatin
manufacture generally has a good process to clarify the impuri-
ties from the gelatin solution, such as chemical clarication and
ltration processes. Lower a and b values were also founded in
SMG, when compared with other gelatins from marine resources
[12]. Both colour and clarity of a gelatin gel are important aesthetic
properties, depending on the application for which the gelatin is
intended. While marine snail gelatin solution showed the high-
est transmittance (%T) (Table 3). The turbidity and dark colour
of gelatin is commonly caused by inorganic, protein and muco-
substance contaminants, introduced or not removed during its
extraction. However, the colour did not affect functional properties
of gelatin.
Table 3
Colour, gel strength and gel clarity of marine snail (H. trunculus) gelatin.
Properties Marine snail gelatin
Gel strength (g)
a
103 1.7
Colour
L
a
28.62 0.64
a
a
1.12 0.05
b
a
2.85 0.32
Transmittance (%)
a
48.77 0.48
a
Values are given as meanSD fromtriplicate determination.
Z. Zarai et al. / Process Biochemistry 47 (2012) 17791784 1783
Table 4
Functional properties of marine snail (H. trunculus). Values are given as meanSD
fromtriplicate determination.
Properties Marine snail gelatin
EAI (m
2
/g)
a
32.77 1.84
ESI (min)
a
38.12 1.05
FE (%)
a
75.44 2.66
FS (%)
a
30min 70.30 0.51
60min 61.86 2.20
WHC (%)
a
120.00 1.65
a
Values are given as meanSD fromtriplicate determination.
3.7. Emulsifying properties of gelatin
Gelatin, and to some extent collagen, are used as a foaming,
emulsifying, and wetting agent in food, pharmaceutical, medical,
and technical applications due to their surface-active properties.
Emulsion activity index (EAI) and emulsion stability index
(ESI) of marine snail gelatin was presented in Table 4. At a con-
centration of 1g/100ml, EAI of SMG was 32.771.84m
2
/g. This
value was higher than those reported for gelatins from cuttlesh
(23.670.36m
2
/g.) andgrey tiggersh(21.440.09m
2
/g) [10,12].
The amphoteric nature with the hydrophobic zones on the peptide
chain make gelatin to behave as an emulsier and it is being used
in the manufacture of toffees and water-in-oil emulsions such as
low fat margarine, salad dressings, and whipped cream. In addi-
tion, high solubility of the protein in the dispersing phase increases
the emulsifying efciency, because the protein molecules should
be able to migrate to the surface of the fat droplets rapidly.
Emulsions containing gelatin from marine snail was very sta-
ble and ESI at a concentration of 1g/100ml was 38.121.05min
(Table 4). Generally, larger and longer peptides could stabilize the
protein lmat the interface more effectively.
3.8. Foamcapacity and foamstability
Foamformation ability is another important property of gelatin
for commonly used foods such as marshmallows. Foam expan-
sion (FE) and Foamstability (FS) of marine snail gelatin are shown
in Table 4. The foam capacity of marine snail gelatin (75%), at
1g/100ml was much lower than that of bovine gelatin (119%) [12].
Foam formation is generally controlled by transportation, pene-
tration and reorganization of protein molecules at the airwater
interface. A protein must be capable of migrating rapidly to the
airwater interface, unfolding and rearranging at the interface to
express good foaming properties [12]. The positive correlation
between hydrophobicity of unfolded proteins and foaming char-
acteristics has been reported [32].
At the same concentration, and at 30 and 60min, FS of marine
snail gelatin were 70.30% and 61.86%, respectively. This result
indicates that MSG might form a lm with stronger and greater
elasticity, leading to stable foam. Foam stability of protein solu-
tions is generally positively correlated with molecular weight of
peptides. In addition, foam stability depends on the nature of the
lmand indicates the extent of proteinprotein interaction within
the matrix.
3.9. Water-holding of gelatin
The functional properties of proteins in a food systemdepend in
part onthe water holdingcapacity(WHC) whichrefers tothe ability
of protein to imbibe water and retain it against a gravitational force
within protein matrix.
The dried MSG showed a high value of WHC (120%) (Table 4),
which means that it was capable to retain 1.2g of water per
gram of gelatin. Since the primary function of hydrocolloids
is to retain water, the high value of WHC obtained for MSG
suggests the existence of a great number of pores and voids
within the gelatin structure. WHC of MSG may be attributed
to its microstructure, specically to its primary chemical struc-
ture, hydrophobic/hydrophilic balance and particle size. As shown
in Table 2, the amount of hydroxyproline in MSG was 98
residues/1000 residues. The water binding capacity of solubilized
gelatinmakes it suitable material for reducing drip loss and impair-
ing juiciness in frozen sh or meat products when thawed or
cooked, and where denatured protein has suffered a partial loss
of its water-holding capacity.
4. Conclusion
This work reported the rst process for extracting gelatin from
the meat of marine snail (H. trunculus). Electrophoretic prole of
SMG showed that is contained protein,
1
and
2
-chains as the
major component. Furthermore, the gel strength of SMG was lower
than that of mammalian gelatin, but was superior to some gelatins
from other marine species previously reported and was less yel-
lowish and reddish in colour. Results fromthe present study clearly
demonstrate that gelatincanbe successfully extractedfrommarine
snail withanacceptable quality andhaving better chemical compo-
sition and functional properties. So we can assume that the marine
snail is a prospective source to produce gelatin with the desirable
characteristics.
Acknowledgement
This work was funded by the Ministry of Higher Education and
Scientic Research, Tunisia.
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