ARTICLE IN PRESS

FOOD
HYDROCOLLOIDS
Food Hydrocolloids 22 (2008) 313–322
www.elsevier.com/locate/foodhyd

Rheological properties of HPMC enhanced surimi analyzed by

small- and large-strain tests—II: Effect of water content and ingredients
Hui-Huang Chen, Yu Chuan Huang
Department of Food Science, National Ilan University, 1 Sec. 1, Shen Nung Road, Ilan city, Taiwan, ROC
Received 16 March 2006; accepted 8 December 2006

Abstract

In order to develop a hydroxylpropylmethylcellulose (HPMC) enhanced surimi product with desirable flow properties and gel-forming
ability at higher water contents, thermal scanning rheological monitor (TSRM) and rotational viscometer were used to perform small-
and large-strain tests, respectively, to investigate the rheological properties of HPMC enhanced surimi at various water contents. The
apparent viscosity, fluid consistency index and yield stress of HPMC powder enhanced surimi were higher than those of the HPMC sol
enhanced sample. The addition of HPMC improved flow properties, decreased the shear thinning properties, and increased the G0 of
surimi. Disintegration was offset by HPMC thermal gelation in these stabilized surimi gels. The critical water content (CWC) of water
holding capacity for horse mackerel surimi was around 82% and, when surimi water content exceeded CWC, we found marked decrease
in G0 and gel strength. While adding HPMC enhanced the G 0 , gel strength did not improve. Furthermore, the absorption of water in the
surimi by potato starch granules is more effective than by HPMC. The water molecules desorption of HPMC during thermal gelation
caused excess water to be exuded from the kamaboko.
r 2007 Elsevier Ltd. All rights reserved.

Keywords: HPMC; Surimi; Horse mackerel; Rheological properties; Water content; Starch

1. Introduction Horse mackerel is one of the most important fish species

Surimi is primarily a concentrate of myofibrillar proteins
(MPs). Once solubilized by salt and water and heated, these
cross-linked proteins form the continuous matrix of a
surimi hydrogel. Viscoelasticity is always an important
quality indicator for surimi. Many researchers are working
to develop higher viscoelastic surimi and surimi-based
products. Nevertheless, high viscoelastic surimi is more
difficult to work with due to undesirable flow properties
during processing, both in the factory and in the kitchen.
An increasing range of surimi-based products could
become available to consumers should desirable flow
properties be developed in commercial frozen product that
allowed surimi to be handled within its protective packa-
ging, semi-rigid collapsible tubes, or with a decorating bag.
Corresponding author. Tel.: +886 3 9357400x824;
fax: +886 3 9310722.
E-mail address: hhchen@niu.edu.tw (H.-H. Chen).
in the Far East countries. Surimi prepared from horse
mackerel has mostly been used for traditionally low-priced
products due to its relative weak gelation, relative
undesirable color and flavor (Chen, Ferng, Chen, Sun, &
Lee, 2005; Okubo, Hossain, Kuwahara, & Nozaki, 2005).
Certain characteristics (e.g., relatively high levels of fat and
protease) of horse mackerel mince can interfere with or
prevent the formation of strong protein–protein networks,
the bonds required for successful surimi gelling (Spencer &
Tung, 1994). In our previous study (Chen, 2000), hydro-
xylpropylmethyl cellulose (HPMC) had been used as a
gelation-aid material in the preparation of horse mackerel
surimi. The addition of HPMC lowered the breaking force
and increased the gel strength of heated surimi gel resulting
from the substantial rise in deformation. Most interesting
was that the surimi became progressively softer as the level
of added HPMC increased. Therefore, HPMC enhanced
surimi has the potential to realize the dual benefits of
better flow properties coupled with improved gel-forming
ability.

0268-005X/$ - see front matter r 2007 Elsevier Ltd. All rights reserved.
doi:10.1016/j.foodhyd.2006.12.006
 ARTICLE IN PRESS
314 H.-H. Chen, Y.C. Huang / Food Hydrocolloids 22 (2008) 313–322
MPs play a dominant role in surimi gelation, while
H-bonds and other polar bonds are thought to play
important roles once salt is added to chopped mince to
make ‘‘sol’’ (Niwa, Matsubara, & Hamada, 1982). In
addition to disulfide bonding, hydrophobic interaction or
covalent cross-linking reaction resulted of transglutami-
nase, may be involved in the inter- and intra-molecules of
MPs during setting phenomenon as the ‘‘sol’’ becomes a
‘‘gel’’ (Niwa, 1992; Niwa, Kohda, & Nakayama, 1986).
The degree by which MPs unfold intensifies as cooking
temperatures rise. Partly hydrophobic cysteine residues
also become more exposed, converting intramolecular
disulfide bonds to intermolecular disulfide bonds (Itoh,
Yoshinaka, & Ikeda, 1979; Kim, 1987; Niwa, 1992). These
bondings or interactions within proteins during the surimi
process determine the flow properties of surimi and
physical properties of heated surimi gel. A communicated
mixture of surimi forms a three-dimensional protein
network during thermal gelation. Both the rheological
properties and texture must be correlated with the structure
and composition of the surimi products. Therefore,
evaluating a surimi product’s rheological properties can
help manufacturers to understand its flow and operation
properties, estimate the protein network and gelation
mechanism, and predict final product texture (Park,
Yongsawatdigul, & Lin, 1994).
Thermal scanning rigidity monitor (TSRM) is commonly
used to conduct small-strain tests as it allows for
programmable thermal control. In small-strain theory,
tests on the rheological properties of surimi gel have
previously been made in the Hookian elastic strain region
with compressional study and shear modulus with
dynamic/oscillation curve analysis. Small-strain theory
related to stress relaxation and creep compliance has been
widely used to study surimi gelation properties by
analyzing the dynamic viscoelasticity variations within
surimi products (Niwa, 1992; Sue, Chen, & Kong, 1995).
Nevertheless, the modulus of rigidity obtained by a small-
strain test does not necessarily indicate the textural sense
intensity of food (Hamman, Purkayastha, & Lanier, 1990).
Therefore, in addition to the small-strain test, the
rheological properties of surimi gel must be characterized
through the use of a large-strain test (e.g., compression,
tensile or torsion tests) and be analyzed in accordance with
large-strain theory (Kong, Ogawa, & Iso, 1999a, 1999b,
1999c; Kong, Park, & Ogawa, 2005).
Ingredient composition is one of the most significant
factors influencing the rheological and gel-forming proper-
ties of surimi (Kong et al., 1999a). Starch is the most widely
used ingredient in surimi to improve the textural properties
of products (Kong et al., 1999a, 1999b). Among starches,
potato starch has the great gel-strengthening effect owing
to its ability to bind a large amount of water and swell to a
large diameter (Kim & Lee, 1987). Therefore, the potato
starch has been added in surimi to prepare high water
content surimi and to study its rheological properties
(Yoon, Gunasekaran, & Park, 2004; Yoon, Park, & Kim,
1997 ). Yoo and Lee (1993) reported that Alaska pollack
surimi sol exhibited pseudoplastic flow properties and that
the ingredient composition significantly influenced the fluid
consistency index (b). Adding carrageenan increased the
b-value, while adding egg white, starch or corn oil
decreased the b-value. The flow behavior indexes (n) were
distributed in the range of 0.118–0.226 and were dependant
upon the type and concentration of added ingredients.
These tendencies of dependent variables of the sol also
reflected on the shear force, compressive force and the
other physical properties of heated surimi gel. Further-
more, because of the large surface area and polymeric
nature, cellulose has the ability to absorb a large amount of
water (Yoon & Lee, 1990). Some modified celluloses, such
as carboxymethylcellulose (CMC) and methylcellulose
(MC) react with muscle proteins and can provide cohesion
in restructured protein gel. They could be used to similar
advantage in certain surimi-based food products (Lee, Wu,
& Okada, 1992). The HPMC owns hydroxylpropyl and
methyl groups on cellulose chains and has the unique
ability to gel when heated and melt when cooled. The
probable mechanism of thermal gelation of HPMC is the
sufficient energy results in the outer layers of water
molecules are driven from the cellulose ether chains and
the chains lock and the solution is transformed into a gel
(Dziezak, 1991; Glicksman, 1969). HPMC form (powder
and sol) and addition timing apparently affects the
structural geometry of the combination gel matrix, result-
ing in variations in rigidity, thermal stability and gel
strength (Chen et al., 2005).
However, the interaction between MPs and HPMC in
gelation as well as the rheological properties of combina-
tive gel in different protein concentration has not been
adequately assessed. To develop a HPMC added surimi
product with desirable flow properties and gel-forming
ability at higher water content levels, we used small-strain
tests to investigate flow properties and large-strain tests to
investigate gel-forming properties in this study.
2. Materials and methods
2.1. Materials
2.1.1. Horse mackerel mince
Frozen horse mackerel (Trachurus japonicus) was pur-
chased from Cheer-Foods Enterprise Co. Ltd. (Ilan, ROC)
The fish block used for this study (10 kg) had been
previously frozen for two months at 20 1C, and was
thawed at 25 1C for 12 h. The fish mince was prepared from
ordinary muscles were collected from the thawed fish and
then squeezed through a sieve with 3 mm diameter holes.
2.1.2. HPMC
The HPMC (Celacol CC-001, Courtaulds Chemicals
Celacol Co., Derby, UK) was purchased from Toong
Yeuan Enterprise Co., LTD. (Taipei, ROC).
 ARTICLE IN PRESS
H.-H. Chen, Y.C. Huang / Food Hydrocolloids 22 (2008) 313–322
2.1.3. Starch
Potato starch (Ji-Cheng Co. Ltd., Ilan, ROC) was
purchased from Ming-Shing store (Ilan, ROC) and was
added during chopping to prepare high water content
surimi.
2.2. Samples preparation
2.2.1. HPMC sol
The HPMC powder was weighed and hydrated with
distilled water (w/w ¼ 1/4 or 1/49) in a Stephan vertical
vacuum cutter (Model UM 5 Universal; Stephan Machin-
ery Co., Hameln, Germany) for 1 min at 1600 rpm.
A vacuum of around 600 mm-Hg was used during the
final 0.5 min in order to obtain final concentrations of 20%
and 2%.
2.2.2. Myofibrillar proteins (MPs)
MP was prepared according to Noguchi (1974). Ten
grams of mince obtained from ordinary muscle was
homogenized (Polytron PT3000, Kinematica AG, Switzer-
land) with 200 ml of cold de-ionized water for 2 min at
3500 rpm. The homogenate was centrifuged for 20 min at
6500  g and the sediment was mixed with 0.6 M
KCl–0.02 M cold phosphate buffer (NaH2PO4/Na2HPO4,
pH 7.2) and stirred for 30 min at 4 1C. The resultant
solution was then centrifuged for 20 min at 6500  g.
Supernatant was collected as salt-soluble proteins and then
dialyzed to obtain the MP solution. MP concentration was
determined in accordance with the method recommended
by Bradford (1976), using bovine serum albumin (BSA) as
the standard. Absorbance was measured at 595 nm. The
MP solution was filtered through a Millipore membrane
(Centricon YM-3, Millipore) to obtain a concentrated MP
solution. The concentrated MP solution was adjusted to a
concentration of 20 mg/mL with phosphate buffer (pH
7.2). The HPMC was then added into the MP solution
(w/v ¼ 4 mg/1 mL) to become the HPMC/MP mixture.
2.2.3. Surimi
Quantities of mince (around 150 g) were weighed into a
2.0 L beaker and washed with a water/mince ratio of 5:1.
The mince was washed for three cycles, 10 min per cycle,
with cold distilled water and the water was replaced after
each cycle. The washed mince was dewatered by centrifu-
ging at 1500 rpm for 2 min and adjusted to water content of
78%, 80%, 82%, 84% and 86% to obtain the protein
contents of 18.1%, 16.5%, 14.8%, 13.2% and 11.5%,
respectively. It was then chopped in a Stephan vertical
vacuum cutter (Model UM 5 Universal) with a circulating
chiller that maintained the sample temperature at less than
10 1C. The mince was first chopped for 1 min at 1600 rpm
(i.e., no-salt-chopping) and named no-salt-added surimi.
An amount of salt equivalent to 2.5% of mince weight was
added and then chopped at 1600 rpm for another 2 min
(i.e., salt-chopping) under a vacuum of approximately
600 mm-Hg in order to become salt-ground surimi. Since
315
the rheological properties of surimi were determined after
salt-chopping, surimi was called for short to represent the
salt-ground surimi in the text. HPMC powder or sol was
added: (i) before chopping (BC); (ii) during chopping
(between no-salt-chopping and salt-chopping process, DC);
and (iii) after chopping (the HPMC was added after salt-
chopping and manually blended for 0.5 min, AC) to
achieve a final concentration of 2.0%. In the ingredients
test, 0.5%, 1.0%, 2.0%, and 4.0% HPMC powder and 5%,
10%, 15%, and 20% potato starch were added during
chopping, the chopping conditions are same as simple
surimi process. The surimi was also kept at 4 1C for 30 min
before rheological properties were measured.
2.2.4. Kamaboko
The surimi paste was packed in a 3 cm dia polyvinylidene
chloride (PVDC) casing, allowed to keep at 4 1C for 30 min,
and then heated in a water bath at 85 1C for 30 min to
become heated surimi sausage (‘‘kamaboko’’). The heated
kamaboko was cooled immediately with running water and
then kept at 4 1C overnight before gel strength was
measured.
2.3. Rheological properties determination
2.3.1. Small-strain testing—TSRM
Rheological properties of HPMC were analyzed by a
small amplitude oscillatory test using a TSRM (Rheometer
AR-550, TA Instruments, New Castle, USA). The TSRM
was equipped with parallel-plate geometry (40 mm dia-
meter), with gap and strain set at 1.0 mm and 1.0%,
respectively. For temperature sweeps, oscillation tempera-
ture ramp mode (1 1C/min) was used to heat the specimen
from 10 to 80 1C. The frequency was fixed at 1 Hz. For
viscosity measurement, the shear rate was scanned from 0.1
to 100 1/s at 25 1C. Specimens were set on the peltier of the
rheometer, protected by a cover split to prevent vapor
dissipation. Three replicate scans were made and the
storage modulus (G0 ), tan d and flow property indexes
were recorded. We employed the fluid consistency (b), Flow
behavior index (n), yield stress (c) and shear sensitive factor
(log Z/log g) to estimate the flow properties of sample with a
power law model: t ¼ bgn+c. Where Z, t and g presented
apparent viscosity, shear stress and shear rate, respectively.
2.3.2. Large-strain testing—gel strength
The gel-forming ability of the heated surimi gel was
determined on 3 cm diameter, 3 cm length sections using a
Rheometer (SUN RHEOMETER CR-150) as described in
a previous paper (Chen et al., 2005). Briefly, we pressed one
end of each sample with a 5 mm diameter spherical head
plunger at a deformation rate of 60 mm/min. We recorded
the load (as breaking force) and the depth of depression (as
deformation) when the test sample lost its resistance and
ruptured. Six replicates were determined at 25 1C and the
gel strength (G) was calculated as B  D, where B
 ARTICLE IN PRESS
316 H.-H. Chen, Y.C. Huang / Food Hydrocolloids 22 (2008) 313–322

represents breaking force (N) and D represents deforma- 3.2. Small-strain tests on HPMC enhanced surimi—flow
tion (mm). properties

3. Results and discussion
3.1. Small-strain tests of HPMC and MP
The 2% HPMC sol, MP and HPMC/MP mixture
showed pseudoplastic fluid properties (Table 1). The
apparent viscosity of the 2% HPMC sol and MP were
0.2 and 0.44 Pa s, respectively. The addition of HPMC
lessened the apparent viscosity and increased the flow
behavior index (n) of the MP solution, resulting in the
improvement of protein solution flow properties. Glicks-
man (1969, 1982) reported that HPMC is soluble in cold
water, in which it becomes a slippery mucus, and, upon
heating, does decrease viscosity up to a point. Secondary
bonds, such as H-bond, are the principal contributors to
the interaction between HPMC and MP within the
combinative gel (Chen, Lin, & Chen, 2001). In addition,
rising shear stress gives a more than proportional increase
in shear rate for the pseudoplastic fluid (Bourne, 1982).
Because no strong chemical bonds were found in the
HPMC/MP mixture (Chen et al., 2001), the long cellulose
chains of HPMC may behave as a flow conditioner in
temperatures below the thermal gelation temperature.
Table 1
Flow properties of HPMC and myofibrillar protein prepared from horse
mackerel in small-strain testing at 25 1C
Sample Fluid properties Apparent
viscosity
(Pa s)
HPMC (2%) Pseudoplastic 0.20
MPa Pseudoplastic 0.44
HPMC/MP mixtureb Pseudoplastic 0.22
a
Myofibrillar protein solution (20 mg/ml).
b
Myofibrillar protein (20 mg/ml) mixed with HPMC (v/w ¼ 1 ml/4 mg).
The horse mackerel surimi with 84% water content
showed Bingham pseudoplastic flow behavior for 0ono1
and C40. The addition of HPMC lessened the apparent
viscosity, fluid consistency index (b) and yield stress (c),
while increasing the flow behavior index (n moved to 1.0)
of surimi (Table 2). These indexes are similar to the results
obtained with Alaska pollack surimi to which corn oil had
been added as reported by Yoo and Lee (1993). An n-value
close to 1 indicates that pseudoplastic properties abate and
that Newtonian flow properties increase. The lower the
b-value the lower the consistency, and the lower the c-value
the lower initial stress is required to achieve flow (Bourne,
1982). All of these indexes reflect the addition of HPMC
improved flow properties of surimi. Adding HPMC
reduced the shear sensitive factor (i.e., reduced the shear
thinning property). The strong shear thing behavior
observed of surimi is due to the entanglement of fish
muscle protein molecules, mainly composed of flexible
actomyosin (Yoon et al., 2004). As anticipated in a
previous report (Chen et al., 2005), the addition of HPMC
stabilized surimi gel structure and made deformation along
the force direction more difficult.
In our small-strain test, HPMC forms (powder and sol)
and addition timing apparently affects surimi flow proper-
ties. The apparent viscosity, the b and c values of HPMC
enhanced surimi, were higher than that of HPMC sol
enhanced surimi (Table 2). This reflects that adding HPMC
powder stabilized the surimi protein network more
effectively than did the addition of HPMC sol, and that
Flow the stabilized structure was able to better withstand surimi
behavior
deformation and flow under stress. In terms of timing, a
index (n)
lower apparent viscosity and higher n value were observed
0.91 in surimi into which HPMC powder was added before
0.82 chopping (HPBC) as well as HPMC sol after chopping
0.89 (HGAC). The former exhibited the lowest and the latter
exhibited the highest shear thinning properties, respec-
tively. We postulate that the powder form HPMC occupied

Table 2
The effect of HPMC on the flow properties of surimi with 84% water content prepared from horse mackerel in small-strain testing at 25 1C

Sample Flow behavior Apparent Flow behavior Fluid consistency Yield stress (c, Pa) Shear sensitive
viscosity (Pa s) index (n) index (b, Pa s) factor

Surimi BPPa 2778.55 0.046 1960.63 1932.63 0.929

HFBCb BPP 1617.03 0.261 1120.24 979.95 0.687
HFDCb BPP 2275.82 0.247 1430.54 947.35 0.705
HFACb BPP 2009.30 0.251 1321.06 963.19 0.700
HGBCc BPP 1435.66 0.217 951.26 878.91 0.739
HGDCc BPP 1429.81 0.219 950.42 879.47 0.738
HGACc BPP 1080.05 0.219 842.13 768.84 0.741
a
BPP: Bingham-pseudoplastic fluid.
b
HFBC, HFDC and HFAC are acronyms used to indicate whether the HPMC powder was added before, during or after chopping, respectively, to
achieve a final concentration of 2%.
c
HGBC, HGDC and HGAC are acronyms used to indicate whether the HPMC gel solution was added before, during or after chopping, respectively, to
achieve a final concentration of 2%.
 ARTICLE IN PRESS
H.-H. Chen, Y.C. Huang / Food Hydrocolloids 22 (2008) 313–322
a smaller space in the protein gel matrix than the sol form
HPMC. HPMC cellulose ether chains moved closer to one
another in the congested space, with the interaction of
threadlike polymer molecules making the chains lock
together and transform into a gel more easily (Chen
et al., 2005). Therefore, the filling effect of HPMC powder
added before chopping resulted in a stable and firm surimi
gel, and the high yield stress was caused by the high
resistance to flow upon initial stress application. As soon as
the flow resistance (yield stress) was overcome, the high
cohesiveness and lower viscous properties make it easier to
flow. On the other hand, the overall bulk of HPMC
polymer aggregate would increase due to water being
absorbed by the aggregate’s long threadlike polymer
molecules, resulting in a reduced capacity of the surimi
gel to entrap large polymers. The result would be a mixed
gel with no continuous combinative network, but rather
two independent gel systems (Chen et al., 2005). Blending
the protein gel and HPMC gel without copolymerization
resulted in an unstable mixed gel that flowed easily and
exhibited high shear thinning properties and low yield
stress.
3.3. Effect of water content on thermal gelation in HPMC
enhanced surimi
A four-staged process of change in G0 was observed in
horse mackerel surimi as its temperature was increased,
and the value of G0 decreased as water content was
increased (Fig. 1(a)). The four-stage progression in G0 was
particularly conspicuous in surimi of 78–80% water
content. The stages were classified as ‘‘softening’’, ‘‘first
heat gelation’’, ‘‘resolution’’ and ‘‘second heat gelation’’
for horse mackerel surimi paste. The first, second and third
20000 a surimi
10000
9000
8000
7000
6000
G' (Pa)
5000
4000
3000
2000
1000
20 30 40 50
Fig. 1. Storage moduli (G0 ) of horse mackerel surimi (a) and surimi with 2% HPMC addition (b) of various water contents.
317
break-points of the TSRM curves were defined as the onset
temperature of the first heat gelation (T1), gel resolution
(T2) and the second heat gelation (T3), respectively (Chen
et al., 2005).
For surimi of 78–86% water content, T1, T2 and T3 were
around 38–40, 50–54 and 64–66 1C, respectively (Fig. 1(a)).
G0 did not increase significantly during the first heat
gelation and did not decrease significantly during resolu-
tion for high water content (X82%) surimi. The G0
increased indicated the surimi formed network structure
during heat gelation. The G0 became progressively higher
according to the increase in the density of cross-link, and
accordingly increasing added water content of surimi is
supposed to be resulted in the decrease in density of cross-
link (Hamada & Inamasu, 1983). This result coincides with
the thought that the amounts of MP per unit volume
decreased according as added water content increased. In
addition, the hardness of molecular chains and strength of
the junction zone contribute to the G0 and reflect gel
elasticity (Lai, Kuo, Li, & Lii, 1996). Therefore, the
phenomenon that results in lower water content delivering
a higher G0 for surimi is attributable to higher heat gelation
efficiency. Transformation of bonding involved in the
inter- and intra-molecules of MP occurs during the thermal
process and alters the conformation of surimi protein
gel (Asghar, Samejima, & Yasui, 1984). Furthermore,
H-bonds, ionic bonds and hydrophobic interactions, which
formed during setting (the first heat gelation) and
participated in the surimi protein gel (Niwa, 1992), thus
serves to increase G0 . Surimi with lower water content has a
higher concentration of MP that contributes to the
formation of the gel matrix. Furthermore, the higher
cross-link density of the gel gives rise to a higher water
holding capacity (Hamada & Inamasu, 1983; Reppond,
b surimi with 2% HPMC addition
water content:
78%
80%
82%
84%
86%
60 70 80 20 30 40 50 60 70 80
Temperature (°°C)

318 H.-H. Chen, Y.C. Huang / Food Hydrocolloids 22 (2008) 313–322
Babbitt, Berntsen, & Tsuruta, 1995; Sylvia, Claus,
Marriott, & Eigel, 1994). Therefore, lower water content
surimi exhibits higher consistency and effectively adheres
to the TSRM adaptor, causing the higher shear stress that
needed to be overcome during oscillation.
Water content evidently influences the resolution of
surimi at around 60 1C. The lack of measurable decrease of
G0 during resolution stage in the high water content surimi
was due to G0 not increasing substantially after the first
heating stage (Fig. 1(a)). Meanwhile, the T2 shifted to a
lower temperature and T3 shifted to a higher temperature,
reflecting the resolution temperature range was spread out
in high water content surimi. The reason for surimi gel
resolution around 60 1C has been speculated as resulting
from a heat activated proteolytic degradation of MP, from
intense thermal coagulation shrinkage caused liberation of
water and heterogeneity in the dispersion of the gel
network, or from the participation of nonenzymatic
modori-inducing proteins (Makinotan, 1982; Niwa, Naka-
jima, Hagiwara, & Miyake, 1975). The broadened resolu-
tion stage of higher water content surimi might result from
a protein gel that is easily damaged due to lower cross-link
density that causes the gel to disintegrate at lower
temperatures. The abrupt rise of G0 after T3 in all the
surimi products was caused by the stable network resulting
from the formation of chemical bonds or interactions
within proteins molecules during the second heating
gelation (Niwa, 1992; Sue et al., 1995).
The addition of HPMC increased the G0 of surimi, and
the four-stage change in G0 was still conspicuous in high
water content surimi (Fig. 1(b)). The first heat gelation
returned a high G0 for HPMC enhanced surimi with water
contents above 82%. Also, T1 values were observed at
1.0
a surimi
0.8
0.6
tan δ
0.4
0.2
0.0
20 30 40 50
Fig. 2. Loss tangent (tan d) of horse mackerel surimi (a) and surimi with 2% HPMC addition (b) of various water contents.
ARTICLE IN PRESS
lower temperatures (34–38 1C), while T2 values were
observed at higher temperatures (54–60 1C), probably
because the first heat gelation occurred earlier and
resolution occurred later than those in surimi in which no
HPMC was added.
The higher tan d was observed in the higher water
content surimi and peak temperature of each tan d curve
lay around 64 1C (Fig. 2). In the small amplitude oscillatory
test, all the energy input is stored and the stress and the
strain will be in phase (tan d ¼ 0) for a perfect elastic solid.
In contrast, for a liquid with no elastic properties, the stress
and strain will be out of phase by 901. The G0 –G00 crossover
(tan d ¼ 1) time might be close to the sol/gel transition time
(Lopes da Silva & Rao, 1999). While, there was no G–G00
crossover for some high concentration gel, the maximal
gelation may occur when tan d becomes stable or declines
to a wave trough and the gel resolution may occur when
tan d rises and up to peaks in the TSRM diagram (Lai
et al., 1996). In Fig. 2, tan do1 for all of the surimi with
or without HPMC addition at various water content, and
rose between 50–64 1C. The tan d increased with decreasing
the number of cross-link per unit volume. Viscous
component of higher water content surimi appeared to
increase at lower temperature due to the collapse of the
lower cross-link density protein gel. It reveals that the
lower cross-link density protein gels are more susceptible to
temperature and caused gel resolution.
The rising of tan d was lagged for HPMC enhanced
surimi. The inhibition in gel resolution of HPMC added
surimi reveals that adding HPMC contributes to surimi
gel thermogelation and enhances its gel structure. Al-
though the level of HPMC addition was only 2%, the
limited available water in the surimi conducted the high
b surimi with 2% HPMC addition
water content:
78%
80%
82%
84%
86%
60 70 80 20 30 40 50 60 70 80
Temperature (°°C)

H.-H. Chen, Y.C. Huang / Food Hydrocolloids 22 (2008) 313–322
concentration HPMC gel property during the combinative
gelation. As the G0 of the high concentration HPMC
increased significantly from 54 1C during heating (Chen,
2006), surimi resolution may be offset by the thermal
gelation of HPMC.
The large-strain test demonstrated that adding HPMC
significantly decreases the breaking force, while increasing
deformation in kamaboko. This results in the heated gel
exhibiting a pliable texture. Furthermore, gel strength of
kamaboko decreases as water content increases and even
becomes unmeasurable when its water content is 86%,
regardless of whether HPMC was added or not (Fig. 3). In
our previous research, we found that the maximal change
rate of water induced gel strength of spotted shark surimi
came when the water content was raised from 79% to 82%
(Chen & Lee, 1997). This reflected that a water content of
around 79% is the critical boundary for the water holding
capacity of spotted shark surimi gel. The protein network
could not firmly envelope additional water molecules,
which ended up in the apertures of surimi with weak
adsorption. In this study, gel strength decreased markedly
as the water content in kamaboko increased from 82% to
84%. This indicates that 82% may be the critical water
content (CWC) of horse mackerel surimi. Yoon et al.
(2004) also reported that the marked shift of viscosity on
water content 485% indicated some possible structural
changes in the MP aggregates at high water content for
Alaska pollack surimi. It revealed that the CWC is fish
species dependence and related to its protein gel forming
ability.
Consequently, the G0 of HPMC added surimi with water
contents below and above than the critical point (i.e., 80%
and 84%, respectively) were examined. G0 increased as the
level of HPMC in surimi increased. The four-stages of
change in G0 were conspicuous for the HPMC added surimi
with 80% water content, while the G0 only increased
400–600 Pa during the diminished first gelation stage
(38–50 1C) for the 84% water content surimi with HPMC
addition level less than 1% (Fig. 4). When 2% HPMC
was added to the surimi, the increase in G0 attained
500
400
Breaking force (g)
300
200
100
0 0.0
78 80 82 84
Fig. 3. Gel strength of kamaboko prepared from horse mackerel surimi with 2% HPMC with various water contents.
ARTICLE IN PRESS
319
2400 Pa during extended heat gelation (34–56 1C). The gel
resolution stage was not observed in 4% HPMC surimi.
These results revealed that the appropriate addition of
HPMC, with its thermal gelation ability, to high water
content surimi could improve the gelation and raise the
value of G0 .
For the kamaboko prepared from surimi with 80% and
84% water content, the breaking force decreased and
deformation increased as the level of HPMC increased.
Increased gel strength with increased HPMC was observed
for kamaboko at 80% water content, but not for
kamaboko at 84% water content (Fig. 5). This revealed
that the addition of HPMC could improve the gelation and
rise the G0 of surimi but could not improve the elasticity of
kamaboko when water content was higher than its CWC.
When we prepared kamaboko from HPMC enhanced
surimi with water content higher than CWC in the lab, we
found that water exuded from cooled kamaboko and
remained in the PVDC casing. The amount of exuded
water correlated positively to the amount of HPMC added
in the kamaboko. Although a similar phenomenon could
also be observed in HPMC-free kamaboko at 84% and
86% water content, the amounts of exuded water was less
than those from HPMC enhanced surimi.
The HPMC gelation phenomenon reflects the nature of
the solution, which jackets the long threadlike polymer
molecules with layers of water molecules and thereby
increases the bulk of the polymer aggregate. As the
temperature increases, the energy of these loosely bound
water molecules increases. When enough of the attached
water molecules are driven from the cellulose ether chains,
the chains lock and the solution transforms into a gel
(Dziezak, 1991; Glicksman, 1969). It is therefore presumed
that the HPMC powder, entrapped in surimi protein gel
and swollen by water molecules adsorption, would release
water molecules from the cellulose ether chains when the
kamaboko is heated. These released water molecules could
not be bound firmly in the protein network with low cross-
link density and then exuded from kamaboko due to the
cold shortening during rapid cooling.
surimi surimi with 2% HPMC addition
400
0.8
Gel strength (gxcm)
Deformation (cm)
300
0.6
200
0.4
0.2 100
0
86 78 80 82 84 86 78 80 82 84 86
Water content (%)
 ARTICLE IN PRESS
320 H.-H. Chen, Y.C. Huang / Food Hydrocolloids 22 (2008) 313–322

30000
a 80% water content surimi b 84% water content surimi
with HPMC addition : with HPMC addition :

20000

G' (Pa)

10000
9000
8000
7000
0%
6000
0.5%
5000 1%
2%
4000 4%

3000
20 30 40 50 60 70 80 20 30 40 50 60 70 80
Temperature (°°C)

Fig. 4. Storage moduli (G0 ) of horse mackerel surimi enhanced with HPMC at: (a) 80% and (b) 84% water contents.

Water content : 80% 84%

500 400
0.8
400
Gel strength (gxcm)
Breaking force (g)

300
Deformation (cm)

0.6
300
200
0.4
200

0.2 100
100

0 0.0 0
0 1 2 3 4 0 1 2 3 4 0 1 2 3 4
HPMC addition level (%)

Fig. 5. Gel strength of kamaboko prepared from horse mackerel surimi enhanced with HPMC at: (a) 80% and (b) 84% water contents.

3.4. Comparison between HPMC and starch addition effect ment agent and are also thought to act as an water
on surimi absorbent in surimi (Kim & Lee, 1987). The reason for
the increase in G0 should be the absorption of water in
To support the above speculation, we added potato the surimi by starch granules to make the surimi more
starch to high water content (84% and 86%) surimi and rigid. For starch enhanced kamaboko with 86% water
examined the gelation properties and the amount of exuded content, even though it was higher than CWC of
water in order to compare the results with that of HPMC horse mackerel surimi, resulted in no exuded water found
enhanced kamaboko. The higher G0 was observed for the in the casing. The exuded water of HPMC-enhanced
surimi with higher addition level of starch. The G0 did not kamaboko primarily represented water released during
decrease during the gel resolution stage during thermal HPMC thermal gelation.
scanning for the starch-enhanced surimi. Thermogram
patterns were similar to that of 84% water content 4% 4. Conclusion
HPMC surimi (Fig. 6). Adding starch increased the
breaking force, deformation and gel strength of kamaboko. The addition of HPMC stabilized the surimi gel
A minimum of 10% starch was required for the gel structure and improved flow properties. For the high water
strength of 86% water content kamaboko to become content surimi, HPMC and protein combinative gel
detectable (Fig. 7). Starch granules act as a filler reinforce- enhanced the gelation ability of low cross-link density in
 ARTICLE IN PRESS
H.-H. Chen, Y.C. Huang / Food Hydrocolloids 22 (2008) 313–322 321

20000 a 84% water content surimi b 86% water content surimi

with starch addition : with starch addition :

10000
9000
8000
7000
6000
G' (Pa)

5000

4000

3000
0%
5%
2000 10%
15%
20%

1000
20 30 40 50 60 70 80 20 30 40 50 60 70 80
Temperature (°°C)

Fig. 6. Storage moduli (G0 ) of horse mackerel surimi enhanced with potato starch at: (a) 84% and (b) 86% water contents.

Water content : 84% 86%

500 400
0.8
400
Gel strength (gxcm)
Breaking force (g)

Deformation (cm)

300
0.6
300
200
0.4
200

0.2 100
100

0 0.0 0
0 5 10 15 20 0 5 10 15 20 0 5 10 15 20
Starch addition level (%)

Fig. 7. Gel strength of kamaboko prepared from horse mackerel surimi enhanced with potato starch at: (a) 84% and (b) 86% water contents.

surimi protein gel. The gel resolution stage was even no References
more observed in the 84% water content surimi with 4%
HPMC addition. The mechanism of water exudation in Asghar, A., Samejima, K., & Yasui, T. (1984). Functionality of muscle
HPMC-enhanced kamaboko with high water content need proteins in gelation mechanisms of structured meat products. CRC
Critical Review of Food Science and Nutrition, 22, 27–106.
further investigation and to solve this phenomenon. Bourne, M. C. (1982). Food texture and viscosity: Concept and measure-
Nevertheless, HPMC is the useful gelation aid material to ment. New York, NY: Academic Press, Inc. pp. 199–246.
improve the flow and handling properties of surimi and Bradford, M. M. (1976). A rapid and sensitive method for the quantitation
gives surimi product a soft gelatinous texture. of microgram quantity of protein utilizing the principle of protein-dye
binding. Analytical Biochemistry, 72, 248–254.
Chen, H. H. (2000). Effects of polysaccharides on thermo-gelation of
surimi and cooking-tolerance of kamaboko prepared from horse
Acknowledgments mackerel. Food Science and Agricultural Chemistry (Taiwan), 2(2),
75–80 (in Chinese, with English abstract).
The author wishes to thank the National Science Council Chen, H. H. (2006). Thermal gelation behaviors of surimi protein
(NSC-90-2313-B-197 -008) for financial support of this mixed with hydroxypropylmethylcellulose. Fisheries Science, 72,
679–685.
study, and also expresses appreciation for the assistance of Chen, H. H., Ferng, L. H., Chen, S. D., Sun, W. C., & Lee, Y. C. (2005).
Y.I. Cho, W.C. Sun, S.Y. Chang, C.L. Jiang, C.Y. Chen, Combination model for the spatial partition of surimi protein and
and W.S. Hsieh in the experiments. hydroxylpropylmethylcellulose. Food Hydrocolloids, 19, 761–768.
 ARTICLE IN PRESS
322 H.-H. Chen, Y.C. Huang / Food Hydrocolloids 22 (2008) 313–322
Chen, H. H., & Lee, Y. C. (1997). Effects of water content and chopping
method on the physical properties of surimi and kamaboko. Fishery
Science, 63(5), 755–761.
Chen, H. H., Lin, S. B., & Chen, L. C. (2001). Gelation modulus of horse
mackerel myofibrillar proteins with HPMC. Report of National Science
Council of R.O.C (NSC-89-2313-B-197-019).
Dziezak, J. D. (1991). A focus on gums. Food Technology, 45(3),
116–132.
Glicksman, M. (1969). Gum technology in the food industry (pp. 437–455).
San Diego, CA: Academic Press.
Glicksman, M. (1982). Food Hydrocolloids, Vol. 1. Boca Raton, FL: CRC
Press, Inc. (pp. 151–156).
Hamada, M., & Inamasu, Y. (1983). Influence of temperature and water
content on the viscoelasticity of kamaboko. Nippon Suisan Gakkaishi,
49, 1797–1902.
Hamman, D. D., Purkayastha, S., & Lanier, T. C. (1990). Applications of
thermal scanning rheology to the study of food gels. In V. R.
Harwalkar, & C. Y. Ma (Eds.), Thermal analysis of foods
(pp. 306–332). New York, NY: Elsevier Applied Science.
Itoh, Y., Yoshinaka, R., & Ikeda, S. (1979). Behavior of the sulfhydryl
groups of carp actomyosin by heating. Nippon Suisan Gakkaishi, 45,
1019.
Kim, B. Y. (1987). Rheological investigation of gel structure formation by
fish proteins during setting and heat processing. Ph.D. dissertation.
Raleigh, NC: North Carolina State University.
Kim, J. M., & Lee, C. M. (1987). Effect of starch on textural properties of
surimi gel. Journal of Food Science, 52(3), 722–725.
Kong, C. S., Ogawa, H., & Iso, N. (1999a). Compression properties of
fish-meat gel as affected by gelatinization of added starch. Journal of
Food Science, 64(2), 283–286.
Kong, C. S., Ogawa, H., & Iso, N. (1999b). Rheological analysis of fish-
meat gel added starch using the large-deformation theory. Fisheries
Science, 65(5), 754–758.
Kong, C. S., Ogawa, H., & Iso, N. (1999c). Rheological analysis in
consideration of volume change on compressional properties of fish-
meat gel. Fisheries Science, 65(5), 759–764.
Kong, C. S., Park, K. Y., & Ogawa, H. (2005). Applicability of the
modified Mooney–Rivlin equation on the rheological analysis of fish-
meal gel. Fisheries Science, 71(2), 374–379.
Lai, M. F., Kuo, M. I., Li, C. F., & Lii, C. Y. (1996). The influence of
concentration on phase transition and rheological properties of red
algal polysaccharide. Food Science (Taiwan), 23(4), 554–566 (in
Chinese, with English abstract).
Lee, C. M., Wu, M. C., & Okada, M. (1992). Ingredient and formulation
technology for surimi based products. In T. C. Lanier, & C. M. Lee
(Eds.), Surimi technology (pp. 273–302). New York, NY: Marcel
Dekker, Inc.
Lopes da Silva, J. A., & Rao, M. A. (1999). Rheological behavior of food
gel system. In M. A. Rao (Ed.), Rheology of fluid and semisolid foods
(pp. 219–318). Gaithersburg, Maryland: Aspen Publication, Inc.
Makinotan, Y. (1982). Modori (Thermo-integration of meat jelly). In Y.
Shimizu (Ed.), Science and technology of fish paste products (p. 36).
Tokyo: Koseisha Koseikaku.
Niwa, E. (1992). Chemistry of surimi gelation. In T. C. Lanier, & C. M.
Lee (Eds.), Surimi technology (pp. 389–427). New York, NY: Marcel
Dekker, Inc.
Niwa, E., Kohda, S., & Nakayama, T. (1986). Exposure of hydrophobic
amino acid residues from myosin on freezing. Nippon Suisan
Gakkaishi, 52, 2127–2130.
Niwa, E., Matsubara, Y., & Hamada, I. (1982). Hydrogen and other polar
bonding in fish flesh gel and setting gel. Nippon Suisan Gakkaishi, 48,
667–670.
Niwa, E., Nakajima, G., Hagiwara, N., & Miyake, M. (1975). On the
retardation of modori in kamaboko processing. Nippon Suisan
Gakkaishi, 41, 1293–1297.
Noguchi, S. (1974). The control of denaturation of fish muscle protein during
frozen storage. Doctoral dissertation. Tokyo, Japan: Sophia University.
Okubo, K., Hossain, M. A., Kuwahara, k., & Nozaki, Y. (2005). Effect of
trehalose on the gel-forming ability, state of water and myofibril
denaturation of horse mackerel Trachurus japonicus surimi during
frozen storage. Fisheries Science, 71(2), 367–373.
Park, J. W., Yongsawatdigul, J., & Lin, T. M. (1994). Rheological
behavior and potential cross-linking of pacific whiting (Merluccius
productus) surimi gel. Journal of Food Science, 59(4), 773–776.
Reppond, K. D., Babbitt, K., Berntsen, S., & Tsuruta, M. (1995). Gel
properties of surimi from pacific herring. Journal of Food Science,
60(4), 707–710, 714.
Spencer, K. E., & Tung, M. A. (1994). Surimi processing from fatty fish.
In F. Shahidi, & J. R. Botta (Eds.), Seafoods chemistry, processing
technology and quality (pp. 288–319). Glasgow, UK: Blackie Academic
& Professional.
Sue, C. W., Chen, T. H., & Kong, M. S. (1995). Multiplicity of protein
sol–gel transitions on heating 20 meat pastes monitored by TSRM.
Food Science (Taiwan), 22(6), 819–833 (in Chinese, with English
abstract).
Sylvia, S. F., Claus, J. R., Marriott, N. G., & Eigel, W. N. (1994). Low-fat,
high-moisture frankfurters: effects of temperature and water during
extended mixing. Journal of Food Science, 59(5), 937–940.
Yoo, B., & Lee, M. (1993). Rheological relationships between surimi sol
and gel as affected by ingredients. Journal of Food Science, 58(4),
880–883.
Yoon, K. S., & Lee, C. M. (1990). Effect of powered cellulose on the
texture and freeze-thaw stability of surimi-based shellfish analog
products. Journal of Food Science, 55(1), 87–91.
Yoon, W. B., Gunasekaran, S., & Park, J. W. (2004). Evaluating viscosity
of surimi paste at different moisture contents. Applied Rheology, 14(3),
133–139.
Yoon, W. B., Park, W. B., & Kim, B. Y. (1997). Surimi–starch interaction
based on mixture design and regression model. Journal of Food
Science, 62(3), 555–560.