Food Hydrocolloids 16 (2002) 441±447

www.elsevier.com/locate/foodhyd

Effect of pectins on the gelling properties of surimi from silver carp

A.M. Barrera a, J.A. RamõÂrez a, J.J. GonzaÂlez-Cabriales a, M. VaÂzquez b,*
a
Unidad AcadeÂmica Multidisciplinaria Reynosa AztlaÂn, Universidad AutoÂnoma de Tamaulipas. Apdo, Postal 1015 Reynosa, Tamaulipas, 88700, MeÂxico
bÂ
Area de TecnologõÂa de los Alimentos, Escuela PoliteÂcnica Superior, Departamento Quimica Analitica, Universidad de Santiago de Compostela,
Campus de Lugo, 27002 Lugo, Spain
Received 3 August 2001; revised 12 October 2001; accepted 16 November 2001

Abstract
Protein±carbohydrate interactions affect the functional properties in foods where proteins are the major ingredients, such as meat and ®sh
processed products. The objective of this work was to evaluate the effect of pectin gum with different degree of methoxylation and calcium
chloride on the mechanical properties of surimi gels. Surimi from silver carp was supplemented with pectin gum at 1% (w/w). Four high
methoxyl pectins and two low methoxyl pectins were evaluated. Calcium chloride was added at 0.2%. Changes on shear stress, shear strain at
failure, texture pro®le analysis and water holding capacity were evaluated. LM35, an amidated low methoxyl pectin, improved shear stress,
hardness, and water holding capacity, while the four high methoxyl pectin and the no amidated low methoxyl pectin did not improved the
mechanical properties of surimi gels as compared with the control. q 2002 Elsevier Science Ltd. All rights reserved.
Keywords: Pectin; Surimi; Calcium; Silver carp; Gel

1. Introduction India, it is widely used in the composite ®sh culture, due

Polysaccharides and proteins are food hydrocolloids with
an important role in the structure, stability and functional
properties of many processed foods. Protein±carbohydrate
interactions affects the functional properties in foods where
proteins are the major ingredients, such as meat and ®sh
processed products. Surimi is a high quality myo®brillar
protein concentrate, obtained from ®sh muscle. It is techni-
cally feasible to obtain surimi from any ®sh species.
However, the functional properties of surimi are highly
dependent on ®sh species. Several hydrocolloids such as
starch, carrageenan and konjac are typically used in the
production of surimi gel products to improve mechanical
properties of surimi gels (Park, 2000). On the other hand,
alginates weaken the surimi gels when incorporated (Lee,
Wu, & Okada, 1992). Recently, the use of xanthan and locust
bean at a ratio of 0.25/0.75 has been proposed to improve
mechanical properties of surimi gels obtained from silver
carp (RamõÂrez, Barrera, Morales, & VaÂzquez, 2001).
Silver carp (Hypophthalmichthys molitrix) is an abundant
warm water ®sh, which is more appreciated in some coun-
tries for cleaning reservoirs and other waters than for its
food value (Frimodt, 1995). However, in many countries
this species is well accepted for human consumption. In
* Corresponding author. Tel.: 134-982-252231; fax: 134-982-223996.
E-mail address: vazquezm@lugo.usc.es (M. VaÂzquez).
0268-005X/02/$ - see front matter q 2002 Elsevier Science Ltd. All rights reserved.
PII: S 0268-005 X(01)00 121-7
to its quick growth and resistance to stress, disease and rough
handling (Siddaiah, Saggar Reddy, Raju, & Chandrasekhar,
2001). In some regions of Mexico, the human consumption
of silver carp has been increased for the last 5 years because
its ®llets present an attractive white colour. However, ®llet
production implies a waste of 10±20% of meat because the
edible portion has a high amount of ®sh-bone (RamõÂrez,
Santos, Morales, Morrissey, & VaÂzquez, 2000a). Despite
its very good acceptation as food, this species has a low
frozen stability (Siddaiah et al., 2001) and does not present
good gel forming ability (Luo, Kuwahara, Kaneniwa,
Murata, &Yokoyama, 2001; RamõÂrez et al., 2000a). Gel
forming ability is important to obtain ®sh products like
restructured products (from whole minced pastes) or surimi
based products (water washed pastes). Surimi solubilized by
salt and water forms a continuous matrix. Some additives
can be entrapped within this matrix and therefore ®ll the gel.
Those additives can exert their functional effects in the
surimi by: (a) in¯uencing the formation of the continuous
surimi gel matrix during heat-inducing gelation; (b) modi-
fying the viscosity, mobility and other properties of the
aqueous phase; (c) in¯uencing texture and appearance of
the ®lled hydrogel for their particle size, distribution, rheo-
logical (textural) properties, and relative volume fraction of
the gel (Lee et al., 1992).
Microbial transglutaminase (MTGase) and hydrocolloids
have been used to improve the mechanical properties of
442 A.M. Barrera et al. / Food Hydrocolloids 16 (2002) 441±447
surimi gels. The optimal conditions for using MTGase to
improve gels obtained from silver carp and stripped mullet
have been reported previously (Ramirez et al., 2000a;
RamõÂrez, RodrõÂguez-Sosa, Morales, & VaÂzquez, 2000c).
The starch is the ingredient most commonly used as ®ller
in the production of surimi or ®sh based products. It
increases ®rmness and gel strength (Lee, 1984; Lee et al.,
1992; Susuki, 1981; Wu, Hamman, & Lanier, 1985a; Wu,
Lanier, & Hamann, 1985b). Other hydrocolloids like carra-
geenans, (Gomez-GuilleÂn, Borderias, & Montero, 1997)
locust bean and xanthan gum (RamõÂrez et al., 2001) were
used in ®sh products to improve mechanical properties.
However, more studies are needed to optimise functional
properties of silver carp and other ®sh species with low
gelling capacity properties.
Pectin polysaccharides are a complex family of polysac-
charides, which are characterized by their degree of ester-
i®cation (DE). The DE varies with the age and the location
within the plant tissue, with the method of extraction, and
the neutral sugar content. Pectins are classi®ed as high
methoxyl (HM) or low methoxyl (LM) pectins. A commer-
cial HM pectin has a typical DE of 55±80%; HM pectins are
generally gelled in the presence of sugar at low pH (Morris,
1998). These gels are formed by the associations of the
chains by stacking the esteri®ed homogalacturonic acid
zones. The result is a three-fold helical con®guration
which is governed by both hydrogen bonding and hydro-
phobic interactions. In contrast, LM pectins may form gels
in the presence of calcium over a wide range of pH with or
without sugar (Fu & Rao, 2001). Gels are normally formed
at concentrations .1%. Two types of LM pectins are
produced commercially: (a) ordinary LM pectin are
prepared by acid treatment in ethanol or isopropanol and
(b) amidated pectins are prepared by the acting of ammonia
in alcoholic suspensions of pectin (Morris, 1998). The
formation of protein±polysaccharide complexes can be
employed to improve functional properties of proteins.
Protein±pectin interactions improved the solubility, emulsi-
®cation, gelation and foaming behaviour of whey protein
concentrates (Mishra, Mann, & Joshi, 2001). Pectins were
also used as a cryoprotectant in surimi (Sych, Lacroix,
Adambounou, & Castaigne, 1990; Ueng & Chu, 1996).
However, to our knowledge there are no reports about the
use of pectins to improve the mechanical properties of
surimi. The objective of this work is to determine the effect
of the presence of pectin gum with different degree of meth-
oxylation and calcium chloride on mechanical properties of
surimi gels.
2. Materials and methods
2.1. Frozen surimi
Silver carp (H. molitrix) was obtained from a ®sh market
in Tampico, Tamaulipas, Mexico. Whole fresh ®sh weigh-
ing 40 kg (ca. 50 ®shes) were washed and kept in ice until
processing. Fish was processed into surimi about 6 h after
being caught. Silver carp was headed, gutted and washed.
Skin and bones were removed with a Bibun deboning
machine (Model NF2DX, Fujiyama, Japan) with a drum
having 5 mm diameter perforations. The washing of the
mince was performed in wash tanks below 10 8C water
using a meat/water ratio of 1:3 (w/v). Washings were
followed by manually dewatering employing cheesecloth
as ®ltering material. Surimi was mixed with the cryoprotec-
tant sucrose (8%), using a Hobart mixer (model VCM. Troy,
Ohio) and then packed into polyethylene bags (2 kg), frozen
within 5 h at 230 8C in a Crepaco plate freezer (Model B-
5854-AM12, Crepaco, Chicago, IL) and stored at 220 8C
until needed. Only one batch of surimi containing 78 (^2%)
of water was used.
2.2. Surimi gel preparation
Surimi samples weighing 250 g were selected from a 2 kg
bag, partially thawed at room temperature, cut into small
pieces and chopped in a 5 qt capacity Hobart cutter (Model
84145, Troy, Ohio) for 3 min with 2.5% salt to solubilize the
myo®brillar proteins. Pectins were added as described in
Section 2.3. Final chopping temperature was maintained
below 15 8C. The paste was stuffed into stainless tubes
…diameter ˆ 1:87 cm; length ˆ 17:75 cm† and sprayed
with commercial vegetable oil to prevent sticking. Tubes
were capped before thermal treatments: 40 8C for 30 min,
followed by 90 8C for 15 min. After cooking, tubes were
immediately removed, placed in a cold water bath and
cooled at 4±5 8C for 30 min. All gels were removed from
the tubes and stored overnight at 4 8C in polystyrene bags,
prior to testing.
2.3. Pectin addition
Pectins with different DE were assayed. Four HM
pectins, RS400 (72% DE, Grindsted Pectin; Lot 804J229),
MRS351 (69±72% DE, Grindsted Pectin; Lot 717J217),
SS200 (65% DE, Grindsted Pectin; Lot 805J218), and
XSS100 (60% DE, Grindsted Pectin; Lot 804J196) were
kindly obtained from Danisco Ingredients USA (New
Century, Kansas). Two LM pectins, LM32 Powder (27±
35% DE, Tic Pretested Pectin; Lot 0004894) and amidated
LM35 Powder (27±33% DE, Tic Pretested Pectin; Lot
0003655), were provided by Tic Gums (Belcamp, MD).
Pectins and calcium chloride were added into surimi
directly. Direct addition was performed adding the mixture
of pectins and calcium chloride into the surimi in a dry form
after myo®brillar proteins were solubilized. Pectin had a
®nal concentration in the surimi of 1% (w/w) and calcium
chloride of 0.2% (w/w).
2.4. Torsion test
Gels were kept at room temperature prior to the torsion
 A.M. Barrera et al. / Food Hydrocolloids 16 (2002) 441±447 443

Table 1
Analysis of variance for the effect of pectin type and calcium level on the shear stress of surimi gels. (DF ˆ degrees of freedom)

Source of variation Sum of squares DF Mean square F-ratio P-value

Main effects
A: Pectin type 3.11 £ 10 9 6 5.19 £ 10 8 9.98 0.0001
B: Calcium level 6.56 £ 10 8 1 6.57 £ 10 8 12.63 0.0006
Interactions
AB 1.15 £ 10 9 6 1.92 £ 10 8 3.70 0.0027
Residual 4.16 £ 10 9 80 5.20 £ 10 7
Total (corrected) 8.98586 £ 10 9 93

test. Gels were cut into 3.0 cm length and milled into an 2.6. Expressible water
hourglass shape with a minimum diameter of 1 cm in the
centre. Each gel was placed in a modi®ed torsion apparatus The amount of expressible water (EW) for each treatment
composed of a Brook®eld digital viscometer (Model was measured. Three grams (^0.2 g) of surimi gels were
5XHBTD, Brook®eld Engineering Laboratories, Stoughton, weighted and put into two layers of ®lter paper. Samples
MA). The texture of each gel was measured by twisting the were placed at the bottom of 50 mL centrifuge tubes and
sample at 2.5 rpm until structural failure occurred. Shear centrifuged at 10000 g £ 15 min at 15 8C. Immediately after
stress and true shear strain at failure were calculated as centrifugation, the surimi samples were weighted and the
described by Hamman, Amato, Wu and Foegeding (1990). EW was calculated as follows:
Six gel samples of each treatment were twisted. Each treat-
ment was obtained with two replicates. Wi 2 Wf
EW ˆ 100
Wi

2.5. Texture pro®le analysis where Wi is the initial weight of surimi, Wf the ®nal weight
of surimi. Three samples were analysed for each treatment
Samples of surimi gels with 3 cm length were equili- and averages are reported. Each treatment was obtained
brated to room temperature for 30 min into a plastic bag with two replicates.
to avoid dehydration before textural analysis. Textural
analysis was determined using a TA-XT2i Stable Micro
Systems Texturometer (Viena Court, England). Textural 2.7. Statistical analysis
pro®le analysis (TPA) was performed using a cylinder
Statistical analysis was performed using a Statgraphics
probe (P50) with 50 mm of diameter. Samples were
5.0 (Software Publishing Corporation, Bitstream). The
compressed at 50% of initial height using a compression
multiple comparison procedure (LSD)'s multiple range
speed of 2 mm/s. Only hardness, springiness and cohesive-
tests were used to determine signi®cantly difference …P ,
ness were reported. Six samples were analysed for each
0:05† among treatments.
treatment. Each treatment was obtained with two replicates.

3. Results
Table 2
Effect of pectin type and calcium chloride level on shear stress of surimi.
(mean values of six replicates; DE ˆ degree of esteri®cation; a, b, c, d letter The in¯uence of pectins with different degree of meth-
distinct mean statistic difference (P , 0.05) between samples for each oxylation and calcium chloride level on mechanical proper-
calcium level (columns)) ties of silver carp surimi gels was assessed using the analysis
Pectin type (%DE) Shear stress Shear stress
of variance methodology. Pectins and calcium chloride were
(kPa) (samples (kPa) (samples added during the chopping step after the surimi paste was
without calcium) with 0.2% solubilized with salt. Pectin was added at 1% (w/w) of the
calcium) ®nal product. Surimi gels without pectin were obtained as
control. The effect of calcium chloride was assessed obtain-
Control 62.8 b 70.2 a
LM32 (27±35%) 55.6 bc 63.7 b ing gels without calcium (control) and adding 0.2% calcium
LM35 (27±33%) 75.3 a 68.6 a chloride (w/w) of the ®nal product. A complete dispersion
XSS100 (60%) 57.3 bc 68.3 a of both pectin and calcium into surimi paste was considered
SS200 (65%) 56.6 bc 52.5 c to be obtained during the chopping step, because there were
MRS351 (69±72%) 49.2 d 62.5 b
no detected visual nor lumps either into surimi paste nor
RS400 (72%) 53.6 cd 61.6 b
surimi gels.
444 A.M. Barrera et al. / Food Hydrocolloids 16 (2002) 441±447

Table 3
Analysis of variance for the effect of pectin type and calcium level on the shear strain of surimi gels

Source of variation Sum of squares DF Mean square F-ratio P-value

Main effects
A: Pectin type 2.11 6 0.3513 61.34 0.0001
B: Calcium level 0.00011 1 0.00011 0.02 0.8894
Interactions
AB 0.411 6 0.0684 11.95 0.0001
Residual 0.475 83 0.0057
Total (corrected) 2.979 96

3.1. Effect of pectin and level of calcium on shear stress of 3.2. Effect of pectin and level of calcium on shear stress of
surimi gels surimi gels

Table 1 shows the results of analysis of variance for
changes in shear stress of the surimi gels. The analysis of
variance indicated that shear stress was affected signi®-
cantly by both parameters hydrocolloid and level of calcium
chloride. A signi®cant interaction effect between pectin and
calcium was detected by the statistical analysis. Table 2
shows the changes on shear stress as affected by both para-
meters pectin and calcium chloride level. LSD determined
signi®cant differences. Shear stress values varied from 49.2
to 75.3 kPa. In gels without calcium added, the control
sample had 62.8 kPa of shear stress. This property was
improved by the amidated LM pectin LM35 (P , 0.05).
All other pectins had a negative effect on the shears stress.
The control gel containing 0.2% calcium had a higher shear
stress value than control (without calcium). This effect has
been reported in several ®sh species and have been asso-
ciated with the presence and activity of an endogenous
calcium dependent transglutaminase (TGase) which cata-
lyses covalent dependent bonding of proteins (Lee &
Park, 1998; Morales, RamõÂrez, Vivanco, & VaÂzquez,
2001; Seki et al., 1990). Only amidated LM35 and the
HM pectin XSS100 did not affected negatively the shears
stress of surimi gels containing calcium chloride.
Table 4
Effect of pectin type and calcium level on shear strain (dimensionless) of
surimi (mean values of six replicates; DE ˆ degree of esteri®cation; a, b, c,
d letter distinct mean statistic difference (P , 0.05) between samples for
each calcium level (columns))
Table 3 shows the results of analysis of variance for
changes in shear strain of the surimi gels. The analysis of
variance indicated that shear strain was affected signi®-
cantly only by the kind of hydrocolloid added. The level
of calcium chloride did not show a signi®cant effect.
However, a signi®cant interaction effect between pectin
and calcium was detected by the statistical analysis. Table
4 shows the changes on shear strain as affected by both
parameters pectin and calcium chloride level. The LSD
determined signi®cant differences. Shear strain values
varied from 0.789 to 1.337. In gels without calcium
added, the control samples showed the highest value of
shear strain. All the pectin studied decreased signi®cantly
the shear strain values (P , 0.05). In gels containing
calcium chloride, the control sample showed a lower shear
strain value than the samples without calcium added.
Several studies have reported that calcium chloride does
not improve the shear strain of surimi gels (Lee & Park,
1998; Morales et al., 2001). All pectins decreased the shears
strain values of the gels containing calcium added. The
amidated LM35 pectin showed again the lowest negative
effect on this property. The calcium chloride had a different
effect on shear strain of surimi gels as a function of the
percent of methoxylation on pectin added. Gels containing
pectin with low percent of methoxylation (LM32 and
amidated LM35) and calcium chloride, showed lower
values than the same samples without calcium. On the

Pectin type (% DE) Shear Shear Table 5

strain strain Effect of LM pectin on the mechanical properties and expressible water of
(samples (sample surimi gels (mean values of six replicates; a, b, c letter distinct mean
without with statistic difference (P , 0.05) between samples)
calcium) 0.2%
calcium) Parameter Control LM32 LM35

Control 1.337 a 1.162 a Shear stress (kPa) 58.7 b 61.4 b 67.3 a

LM32 (27±35%) 0.933 c 0.914 c Shear strain d 1.087 a 0.911 c 0.996 b
LM35 (27±33%) 1.229 b 1.032 b Hardness (g) 5029.9 c 5345.8 b 6149.4 a
XSS100 (60%) 0.907 c 0.988 bc Springiness d 0.884 a 0.873 a 0.878 a
SS200 (65%) 0.789 d 0.832 d Cohesiveness d 0.520 a 0.457 b 0.516 a
MRS351 (69±72%) 0.796 d 0.959 bc EW (%) 26.9 a 25.7 a 19.0 b
RS400 (72%) 0.806 d 0.927 c d
Dimensionless.
 A.M. Barrera et al. / Food Hydrocolloids 16 (2002) 441±447
other hand, addition of calcium improved the shear strain of
gels containing HM pectins.
3.3. Effect of low methoxyl pectins on mechanical and
functional properties
Results obtained in previously reported studies showed
that LM pectins, specially the LM35 pectin showed a higher
compatibility with surimi gels. To con®rm this results
another study was conducted. Surimi gels containing LM
pectins LM32 or amidated LM35 were obtained and
changes on the shear stress, shear strain, textural pro®le
analysis and water holding capacity were measured and
compared with a control without pectin. Table 5 shows
the results of the LSD. Signi®cantly, differences were
found between treatment as affected by the pectin added.
The amidated LM35 pectin increased signi®cantly
(P , 0.05) the shears stress, hardness and water holding
capacity of the surimi gels as compared with control. The
water holding capacity is directly associated with the
percent of water extracted by centrifugation (the lowest %
of water extracted means the highest WHC). The percent of
water extracted varied in the range 19.0±26.9. The lowest
percentage of water extracted corresponded to LM35 surimi
gels and the highest value of water extracted was obtained
by the control, while the LM32 surimi gels have a similar
value than the control. This pectin has no effect on the
springiness and cohesiveness properties. However, it had a
small but signi®cantly negative effect on shear strain
(P , 0.05). The LM32 improved only the hardness of the
surimi gels. This pectin had not a signi®cant effect on the
shear stress, springiness and water holding capacity, but
decreased the shear strain and cohesiveness (P , 0.05).
These results con®rm that amidated LM35 pectin is appro-
priated to be employed in surimi gel production to improve
mechanical and functional properties.
4. Discussion
Surimi is a wet concentrate of myo®brillar proteins.
Myosin, actin and actomyosin complex are the more abun-
dant proteins. Myosin has been recognized as the protein
responsible for functional properties (RamõÂrez, MartõÂn-Polo,
& Bandman, 2000b). However, gelling and other functional
properties of surimi are in¯uenced by the overall effect of all
proteins present in the food system. The gelling of surimi
proteins is usually obtained with 2±3% NaCl at pH close to
7 (pH of muscle in post-rigor) and ®nal heating of 90 8C for
at least 15 min. These conditions let to obtain an irrevers-
ible, opaque gel, with different level of rigidity and deform-
ability, depending on the thermal treatment, ®sh species and
other parameters. Because myo®brillar proteins are above
the isoelectric point (IP), these proteins are charged as
anions. Thus, the use of calcium has been considered to
improve protein±calcium±protein bonds during the produc-
tion of thermal induced gels, with consequently increasing
445
mechanical properties of surimi gels. On the other hand, the
presence of protein±calcium±protein interactions have been
reported as detrimental for protein stability during the
frozen storage of surimi. Recently, it has been established
that calcium improves the mechanical properties because
calcium is a cofactor of the endogenous transglutaminase
enzyme, which catalyse the covalent bond of proteins (Lee
& Park, 1998; Morales et al., 2001).
Silver carp surimi gels showed high shear stress and low
shears strain values. These kinds of gels are perceived as
`mushy' (low stiffness and low cohesiveness). This beha-
viour has been previously reported for this ®sh species
(RamõÂrez et al., 2000a, 2001). This carp species produces
surimi gels with lower mechanical properties than other carp
(Luo et al., 2001). In this work, the use of calcium improved
the shear stress of surimi control gels, but had no effect on
the shear strain. This behaviour has been reported in several
®sh species and has been associated with the presence and
activity of the endogenous transglutaminase as it was
commented previously (Lee & Park, 1998). The bene®cial
effect of calcium is highly dependent on the presence of
residual TGase after the washing±dewatering cycles needed
to obtain surimi (Morales et al., 2001).
Protein±polysaccharide interactions have been proposed
as a way to improve functional properties of surimi gels.
Pectin is an anionic hydrocolloid with different degree of
methoxylation. Therefore, pectins have different level of
ionic charges. HM pectins interact with proteins above the
IP. For example, with lysozyme (Yang, Chen, & Chang,
2001) and bovine serum albumin (Ledward, 1994). HM
pectins also improve the gelling capacity and thermal stabil-
ity of whey protein concentrate in the range pH of 4.6±8.5
when the protein concentrate was above 8% (Mishra et al.,
2001). However, information about myo®brillar proteins
interactions with pectins is scarce. Information for
protein±calcium±pectin interactions with pectin containing
different degree of methoxylation was not found. In this
work, the use of HM pectins decreased the shear stress
(Table 2) and shear strain (Table 4) of surimi gels when
added without calcium. This behaviour could be associated
with the anionic property of both kind of hydrocolloids and
consequently the repulsive driving force conducts a less
structured system. In the system containing HM pectins,
addition of calcium chloride improved the shears stress of
all gels (except for SS200 pectin) reaching equal or higher
values than control gel obtained without calcium chloride
addition. Shear strain was improved in all gels containing
HM pectins and calcium as compared with gels containing
only HM pectins. However, neither gel showed a shear
strain value equal nor higher than control gels. These results
could indicate that transglutaminase induced the formation
of stronger gels by covalent bonds. These gels were not
affected by the presence of HM pectin. Another possibility
could be that these behaviour is indicative of a protein±
calcium±pectin interactions, because as previously
discussed, TGase does not improve the shear strain of surimi
446 A.M. Barrera et al. / Food Hydrocolloids 16 (2002) 441±447
gels. Despite this kind of interactions, surimi gels containing
HM pectins showed less mechanical properties than surimi
control gels. More studies are needed to determine the effect
of different concentration of HM pectin and calcium on
mechanical properties of surimi gels. The differences
observed between the type of pectin used, could be in¯u-
enced with a different level of hydrocolloid, because
commercial samples are standardized with sugars. Other
factor which should be considered is the feasibility that b-
elimination and de-esteri®cation reactions could be present
during the cooking of surimi gels, because such reactions
can be present above pH 6 and surimi gels had pH near to 7.
Such reactions affect the structure of pectin, in¯uencing
negatively their expected functionality.
LM pectins showed a different behaviour, while amidated
LM35 increased the gel strength of surimi gels without
calcium (P , 0.05), LM32 has not effect (Tables 4 and 5).
LM pectins did not improve the shear strain. The mechan-
ical properties of surimi gels containing calcium were not
affected by adding LM pectins. This could be because
covalent bonded surimi gels masked or inhibited the
protein±calcium±pectin interactions, or because this kind
of interactions has not a bene®cial effect on the mechanical
properties of surimi gels. The bene®cial effect of amidated
LM35 was con®rmed with further studies (Table 5). The
different results obtained for both LM pectins (as with all
others pectins) must be associated with a different structure
for amidated pectins. The amidation of the LM pectin
confers to this pectin distinct physicochemical and func-
tional properties. According to the supplier (Tic Gums),
LM amidated pectins requires less calcium (10±30 mg/g
of pectin) than LM no-amidated pectin (30±50 mg/g pectin)
to form a gel. Amidated pectin are reported to work better
under acidic conditions (3.2±3.6), while no-amidated pectin
works from pH 2.8±6.5. Amidated pectin is widely used in
the pharmaceutical industry as a carrier of different active
ingredients. In food, it is a recommended gelling agent,
thicker and stabilizer agent for fruits gels, and yoghurt.
However, there are scarce scienti®c reports about the use
of this hydrocolloid in foods and to our knowledge there are
no reports about the use of LM amidated pectin to improve
mechanical and functional properties of gels obtained from
red meat, poultry or ®sh. Results obtained from this study
suggest the feasibility to employ amidated pectin in restruc-
tured meat, poultry and ®sh products, to improve both
mechanical and functional properties.
5. Conclusions
Silver carp surimi gels showed low mechanical proper-
ties. These properties can be enhanced by using calcium
chloride alone. HM pectin showed to be compatible with
surimi gels when used together 0.2% calcium chloride. The
amidated LM35 pectin was the only pectin studied which
increased the mechanical properties of surimi gels (except
shear strain). According with these studies, LM35 pectin
could be more interesting for surimi industry for its effect
on decreasing expressible water (27%), than for its effect on
increasing level of shears stress (15%), and hardness (22%).
More studies are needed to determine the effect of level of
pectin and calcium chloride addition on the functional and
mechanical properties of surimi gels.
Acknowledgements
The authors are grateful to CONACYT-SIREYES
(Mexico) for the ®nancial support of this work (Proj.
9704001017).
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