Fish Sci (2014) 80:1083–1088
DOI 10.1007/s12562-014-0769-z
ORIGINAL ARTICLE
Changes in the pericellular connective tissue and breaking
strength of the three types of muscles of the cultured carp
Cyprinus carpio during storage in ice
Jia Liang • Riho Miyazaki • Xianxian Zhao •
Katsuya Hirasaka • Shigeto Taniyama •
Katsuyasu Tachibana
Received: 25 February 2014 / Accepted: 31 May 2014 / Published online: 24 June 2014
Ó Japanese Society of Fisheries Science 2014
Abstract To elucidate the structural changes in pink (P),
white (W), and red (R) muscles during storage in ice, we
measured the breaking strength and changes in pericellular
connective tissues of cultured carp. The breaking strength
just after killing was highest in R muscle (1.00 ± 0.20 N),
lowest in W muscle (0.37 ± 0.07 N), and intermediate
(0.84 ± 0.12 N) in P muscle. During the storage period,
the breaking strength decreased first in R muscle, then in P
muscle, followed by W muscle. The diameter of muscle
fibers was greater in W muscle (113 ± 15 lm) than in P
muscle (72 ± 3 lm) and R muscle (48 ± 2 lm).
Destruction of the honeycomb structure of the pericellular
connective tissue occurred most rapidly in W muscle and
most slowly in R muscle. These results suggest that the
interposing of P muscle fibers in the dorsal ordinary muscle
contributes to the acceleration of post-mortem tenderiza-
tion in fish.
Keywords Breaking strength
Cultured carp

Freshness
Muscle types
Pericellular connective tissue

Pink muscle
Tenderization
Introduction
Fish freshness can be assessed by visual inspection,
chemical analysis, sensory evaluation, histological obser-
vation, among other methods [1]. More recently, sensory
J. Liang
R. Miyazaki
X. Zhao
K. Hirasaka
S. Taniyama

K. Tachibana (&)
Laboratory of Fishery Nutritional Science, Graduate School of
Fisheries Sciences & Environmental Studies, Nagasaki
University, 1-14 Bunkyo-machi, Nagasaki 852-8521, Japan
e-mail: orenge@nagasaki-u.ac.jp
Food Science and Technology
evaluation has been used under research conditions to
assess seafood quality. Indeed, firmness is one of the
important characteristics considered in the sensory evalu-
ation of fish because the Japanese have the custom of
eating raw seafood, such as ‘‘sashimi’’ and ‘‘sushi’’ [2–7].
The texture of the flesh changes post-mortem, becoming
more tender during storage. These changes are due to a
number of factors, including structural changes to the
myofibril protein which is mainly composed of structural
and/or regulatory proteins. We have previously reported
that the degradation of a-actinin, which was detected on
the Z-line in muscle cells using immunoelectron micros-
copy, was observed by immunoblotting sodium dodecyl
sulfate-polyacrylamide gel electrophoresis in cultured red
sea bream during storage in ice [8]. Tsuchiya et al. [9] and
Tachibana et al. [10] also reported that the fragmentation of
myofibrils in fish muscles during storage might be caused
by the decomposition of a-connectin to b-connectin. Ku-
mano and Seki [11] additionally observed that a decrease in
the breaking strength of fish muscles during storage
occurred after the loss of a-connectin. Changes in flesh
structure post-mortem also occur due to structural changes
in the pericellular connective tissue, which is mostly
composed of type V collagen. Ando et al. [12, 13] reported
that the post-mortem tenderization of fish muscle is related
to the gradual disintegration of the pericellular structure, as
observed by light microscopy following the compression
test of the fish muscle. Similarly, scanning electron
microscopy (SEM) has revealed that deterioration of the
collagen fibril network structure corresponds to the post-
mortem tenderization that occurs in fish muscle pericellular
connective tissue [14–16]. The disintegration of collagen
fibers accompanied by a decrease in the breaking strength
has also been observed using transmission electron
microscopy [17, 18].
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Previous studies on fish muscle tenderization have
focused on the dorsal ordinary muscle. The skeletal muscle
of fish comprises two distinct layers of ordinary and dark
muscles, and ordinary muscles consist of white muscle
fibers only or white and pink muscle fibers [19].
We previously demonstrated that interposition of pink
muscle fibers promotes a decrease in the freshness of fish
[20]. However, there has been no study on tenderization in
relation to pericellular connective tissues of the three types
of muscle fibers in fish during storage. In our study, to
elucidate the decrease in firmness accompanying structural
changes in pericellular connective tissues of the pink
muscle as compared to the white and red muscles, we
evaluated the breaking strength of pericellular connective
tissues as an index of texture. We also observed morpho-
logical changes in the pericellular connective tissues using
SEM.
Materials and methods
Sample fish
Cultured carps (Cyprinus carpio) were used as sample fish.
Samples of large fish [body weigh 3.0 ± 0.5 kg; body
length 48.6 ± 3.1 cm (n = 4)] were purchased from fish
farmers in Nagasaki and Fukuoka prefectures and trans-
ported alive to the laboratory. They were held in a tank for
1 day at room temperature under conditions similar to
those of the cultivation pond. The fish were then killed by
swiftly cutting through the hindbrain and kept in polyeth-
ylene bags. The muscles were then divided into three
muscle regions: the dark and intermediate muscle region,
colored dark red or light pink, the ordinary muscle region
adjacent to intermediate muscle, and the deep ordinary
muscle region which was relatively white in color to the
naked eye. The three types of muscles were taken from
each muscle region near the lateral line and used in sub-
sequent experiments. Sampling for the experiment took
place immediately after killing and after 1, 3, 5 and 7 days
of storage in ice.
Distinguishing muscle fiber types
Muscle fiber types were distinguished according to previ-
ously published criteria [21–23]. We used dorsal muscle
blocks in our experiments and removed dark-red dark
muscle, light-pink intermediate muscle, and white ordinary
muscle from each of the respective muscle regions near the
lateral line. Each of these muscle types consists of red,
pink, and white muscle fibers, respectively [21]. Muscle
types were also confirmed by the acid and alkaline stabil-
ities of actomyosin ATPase.
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Fish Sci (2014) 80:1083–1088
Evaluation of breaking strength
To evaluate the three types of muscles, we sliced off blocks
of muscle of the three muscle types from the dorsal muscle
to the lateral line, cutting at a thickness of 10 mm vertically
to the orientation of muscle fibers. Because the pink muscle
area is very small, we used a cylindrical plunger (diameter
2 mm) to measure firmness. The plunger was inserted into
the sliced block, parallel to the orientation of each type of
muscle fiber, at a speed of 1 mm/s using a Rheoner model
RE-3305s rheometer (Yamaden Co., Tokyo, Japan). The
maximum force needed to penetrate the muscle was
regarded as the breaking strength (N). Pairwise compari-
sons between the three muscle types were conducted using
the Student’s t test.
Preparation of samples for SEM observation
The cell maceration/SEM method [24] with SEM was used
to reveal the three-dimensional structure of the collagen
fibril network of the pericellular connective tissue. The
three muscle types in the dorsal muscle were distinguished
by naked eye, and each muscle type was cut into small
2 9 2 9 8 mm cubes along the parallel orientation of the
muscle fibers. The cubes were pre-fixed in 0.1 M phos-
phate buffer containing 2.5 % glutaraldehyde and 2 %
paraformaldehyde (pH 7.2) for 4–7 days [25]. To expose
the collagen fibril network, cubes of the white, pink, and
red muscles were immersed in 2 N NaOH solution for
3–7 days at room temperature. After three rinses in dis-
tilled water for 10 min each rinse, the cubes were postfixed
with 1 % tannic acid solution and 1 % osmium tetroxide
solution for 2 h [26]. Samples were then washed thor-
oughly with distilled water and dehydrated through a series
of graded methyl alcohol, frozen in liquid nitrogen, and
fractured with a cooled sharp blade. The fractured samples
were substituted in 2-methyl-2-propanol, freeze-dried,
sputter-coated with a gold/palladium alloy (30 mA, 30 s)
using an auto fine coater (JFC-1600; JEOL, Tokyo, Japan)
and then observed by SEM (JSM6380; JEOL) using an
accelerating voltage of 15 kV.
Measurement of cell diameter in the honeycomb
Cells in the honeycombs of each muscle type were pho-
tographed at a magnification of 3009 or 4009 magnifi-
cation (SEM) and the diameter of the cells calculated from
the scanning photographs.
Statistical analysis
Individual differences between the test groups were
assessed by a Tukey’s multiple test.
Fish Sci (2014) 80:1083–1088
1.2
Breaking strength (N)
0.8
0.4 *P
*P
**R *R
*R
0 1 3 5
Storage period (day)
Fig. 1 Changes in breaking strengths of white, pink, and red muscles
in cultured carp during storage in ice. Symbols mean breaking
strength, whiskers standard deviation (SD) (n = 4). Open circles
white muscle, filled triangles pink muscle, filled circles red muscle.
*P (p \ 0.05) Significant difference in same storage periods between
white muscle and pink muscles, **R (p \ 0.01), *R (p \ 0.05)
significant difference (p \ 0.01) in same storage periods between red
muscle and white muscle. Breaking strength values are measurements
of at least four independent studies
Results
Changes in breaking strengths of white, pink, and red
muscles
Figure 1 shows the breaking strengths of white, pink, and
red muscles. The breaking strength of white muscle was
0.37 ± 0.07 N just after killing and barely changed
throughout the storage period. In comparison, the breaking
strength of red muscle was 1.00 ± 0.20 N immediately
following killing, the highest of the three muscle types at
this time, but decreased to 0.63 ± 0.11 N after 1–3 days of
storage in ice. Thereafter, it remained at almost the same
level until the end of storage period. In the pink muscle, the
breaking strength was 0.84 ± 0.12 N just after killing and
remained constant on the first day, decreasing to
0.50 ± 0.06 N after 3 days of storage in ice. Parallel to the
changes observed in red muscle, the breaking strength of
pink muscle also decreased after killing and remained the
same until the end of the storage period.
Changes in pericellular connective tissues as observed
by SEM among white, pink, and red muscles
Figure 2 shows the pericellular connective tissue changes
in white, pink, and red muscle fiber types during storage in
ice. Just after killing (0 day), sockets were clearly exposed,
with the complete removal of myomeres by the NaOH
solution using the cell-maceration method, resulting in the
1085
collagen fibers of each muscle type forming a honeycomb
structure from the collagen fibers. The paries of the peri-
cellular connective tissue structure of red and pink muscles
was relatively thicker than that of white muscles. By
contrast, the diameter of cells in the honeycomb in white
muscles was 113 ± 15 lm, which is clearly larger than
that in pink and red muscles whose cell diameters were
72 ± 3 and 48 ± 2 lm, respectively (Fig. 3).
*R
At day 1 of storage, the honeycomb structure of white
**R muscles collapsed to a certain extent compared to that just
after killing and the layer surrounding the honeycomb
structure became thinner. The honeycomb structure of the
7 white muscle collapsed almost totally after 3 days of
storage in ice and maintained that condition up to 7 days of
storage. In the pink muscle, the honeycomb structure of
pericellular connective tissues remained nearly unchanged
after 1, 3, and 5 days storage compared to that just after
killing. After 7 days storage in ice, the honeycomb struc-
ture was slightly collapsed and the collagen fibers of per-
icellular connective tissues had become somewhat looser,
but the honeycomb structure itself was in a better condition
than in white muscle stored in ice for the same period of
time.
Consistent with observations on the pink muscle, the
honeycomb structure of connective tissues of the red
muscle hardly collapsed during the 1-, 3-, or 5-day storage
period in ice. The collapse of the honeycomb structure and
the loosening of collagen fibers in pericellular connective
tissues to some degree were also observed after 5–7 days of
storage in ice.
Discussion
In this study, we found that white muscle of cultured carps
exhibited a low breaking strength just after killing and that
this low breaking strength did not significantly change
during the storage period. However, the honeycomb
structure of pericellular connective tissues in the white
muscle collapsed after day 1 in storage. In contrast to white
muscle, pink and red muscles both showed high breaking
strength just after killing, but with a subsequent marked
decrease during storage, and the honeycomb structure of
pericellular connective tissues of these latter muscles
hardly collapsed during storage.
It has been reported that a decrease in breaking strengths
is closely related to the collapse of the pericellular con-
nective tissue structure in ordinary muscle of fish [5, 12]. In
our study, the breaking strength of white muscle hardly
changed throughout the storage period. In pink muscle, the
breaking strength was 0.84 ± 0.12 N just after killing and
remained constant on the first day, subsequently decreasing
to 0.50 ± 0.06 N after 3 days of storage in ice, following
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Fig. 2 Scanning electron micrographs of the different muscle types
in cultured carp during the storage period. Scale bars: 50 lm.
Samples were pre-fixed in 2.5 % glutaraldehyde and 2 % parafor-
maldehyde (pH 7.2, 0.1 M phosphate buffer) for 4–7 days, immersed
in 2 N NaOH solution for 3–7 days, and then postfixed with 1 %
tannic acid solution and 1 % osmium tetroxide solution for 2 h.
140
Diameter of honeycomb structure (µm)
**P
120 **R
100
80
60
40
20
0 12, 31], our results show that the breaking strength of
White muscle Pink muscle
Fig. 3 Diameter of cells in the honeycomb structure of white, pink
and red muscles of cultured carp just after killing. Bar mean value,
whiskers SD (n = 4). **P (p \ 0.01) significant difference between
pink muscle and white muscles, **R (p \ 0.01) significant difference
between red muscle and white muscles. Breaking strength values are
measurements of at least four independent studies
which it remained at almost the same level until the end of
the storage period. We did not use ordinary muscle but
instead separated the white, pink and red muscles from the
dorsal muscle for our experiments in order to be able to
make a comparison with values reported previously [20,
22, 23, 27]. Just after killing, the red muscle showed a
slightly higher breaking strength than the pink muscle, and
the breaking strengths of these two muscles were signifi-
cantly higher than that of the white muscles. In addition,
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Fish Sci (2014) 80:1083–1088
Samples were then dehydrated through a series of graded methyl
alcohol, frozen in liquid nitrogen, fractured using a cooled sharp
blade, substituted with 2-methyl-2-propanol, freeze-dried, and then
sputter-coated with a gold/palladium alloy for observation by
scanning electron microscopy (15 kV)
the diameter of muscle fibers, as observed by SEM, was
largest in white muscles, followed by pink and red muscles
in order of decreasing diameter. These results suggest that
the breaking strength of each muscle type just after killing
is related to the density of pericellular connective tissues.
Hatae et al. [7] and Sato et al. [28] reported that
muscle collagen contents play an important role in
determining the firmness of meat in some fishes. It is
also known that the pericellular connective tissue is
mainly composed of type V collagen [29, 30]. Contrary
to previous studies where a decrease in breaking strength
occurred in ordinary muscles during storage in ice [4, 5,
Red muscle
white muscle actually did not change during storage in
ice. This is in contrast to red and pink muscles which
showed remarkable decrease in breaking strength during
the storage period. The honeycomb structure of pericel-
lular connective tissue in white muscle collapsed con-
spicuously after 1 day of storage in ice, while that in
pink and red muscles changed only slightly during
storage. In these experiments, we used a thinner plunger
(diameter 2 mm) to sample breaking strength than that
used in previous studies [4–7]. Therefore, our measure-
ment of breaking strength in white muscle during the
early storage period might not be completely correct. In
our study, the breaking strength of three muscle types at
1 day of storage in ice was not less than that just after
killing. In an earlier publication we also reported the
same result, as well an increase in breaking strength due
Fish Sci (2014) 80:1083–1088
to acute muscle contracture induced by caffeine [27]. To
the contrary, Ando et al. [4, 5, 12, 13, 16, 18] reported
that breaking strength of ordinary muscle at 1 day of
storage at 5 °C was lower than that just after killing.
‘Cold shortening,’ i.e., muscle contraction/shortening
before the onset of rigor mortis due to exposure to low
temperatures, occurs in many fishes during storage at
0 °C [32, 33]. Therefore, these phenomena likely indi-
cate that our results on breaking strength were strongly
affected by rigor mortis. In any case, our results indicate
the possibility that the occurrence of tenderization during
storage in ice may be independent of the destruction of
pericellular connective tissues in dorsal muscles of fish.
Numerous studies have reported that the structural
change in pericellular connective tissues, which consist of
collagen fibers, correspond to post-mortem tenderization
[5, 6, 12, 13, 16]. These studies investigated the ordinary
muscle of fish, which includes both white and pink
muscles. To the contrary, we report that the interposition
percentage of pink muscle fiber in dorsal ordinary muscle
varies from 0 to 55 % depending on the fish species and
that this percentage affects the increasing rate of the K-
value [34]. The prolongation of tenderization affects not
only the disruption of connective tissues surrounding the
muscle fibers, but also the fragmentation of the Z-disc in
the muscle fibril [31]. In chicken muscles, Takahashi
et al. [35] reported that the disintegration of the Z-disc in
the muscle fibril could be due to tenderization during
chilly storage. Likewise, using transmission electron
microscopy we previously observed the disintegration of
the Z-disc in fish muscle fibril during storage in ice [10].
Our present finding of a decrease in the breaking strength
of pink and red muscles after 3 days of storage in ice is
consistent with our previous result of Z-disc disintegration
in pink and red muscles after 3 days of storage in ice
[20]. Thus, we consider that the tenderization of ordinary
muscle during storage in ice is, at least in part, affected
by the interposition of pink muscle fiber in ordinary
muscle.
Since enzymes for proteolysis in pink and red muscles
have relatively higher activities than those in white muscle,
the integration of pink and red muscles occurs rapidly
during proteolysis [36–40]. However, it is not yet known
whether it is the pericellular connective tissue or the
intercellular muscle fibril that is mainly influenced by
enzymes in the three types of muscles; hence, further
investigation is required. Our results indicate that interpo-
sition of pink muscle fiber in the dorsal ordinary muscle
might accelerate the decrease in freshness and also suggest
that the interposing of pink muscle fiber in the dorsal
ordinary muscle may control meat tenderization to a certain
extent.
1087
Acknowledgments We thank Dr. Satuito Cyril Glenn Perez,
Nagasaki University, for reviewing this manuscript.
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