Journal of Food Engineering 247 (2019) 30–37

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Journal of Food Engineering

journal homepage: www.elsevier.com/locate/jfoodeng

Effects of pre-emulsification by three food-grade emulsifiers on the T

properties of emulsified surimi sausage
Xiangyu Liua, Lei Jib, Tao Zhanga,b, Yong Xuea,*, Changhu Xuea
a
Department of Food Science and Engineering, Ocean University of China, Qingdao, 266003, PR China
b
Physical Chemistry and Soft Matter, Wageningen University & Research, Stippeneng 4, Wageningen, 6708 WE, the Netherlands

A R T I C LE I N FO A B S T R A C T

Keywords: In this study, we investigated the effects of peanut oil pre-emulsification by three food-grade emulsifiers (soy
Emulsified surimi sausage protein isolate (SPI), konjac glucomannan (KGM), and acetylated distarch phosphate (ADSP)) on the properties
Textural properties of emulsified surimi sausage. TPA tests showed that KGM comprehensively improved sausage texture. SPI re-
Peanut oil duced the emulsified sausage hardness from 131.37 ± 3.12 N to 111.13 ± 1.23 N and ADSP reduced the
Emulsification process
adhesiveness of the product from −0.57 ± 0.05 to −0.37 ± 0.04. The water holding capacity, emulsification
stability, and whiteness properties improved significantly after adding the pre-emulsified peanut oil (p < 0.05).
Rheology experiments and particle size measurements revealed competitive emulsification between myosin and
each emulsifier. Finally, more uniform distributions of oil droplets in the SPI, KGM, and ADSP groups were
observed by optical microscopy. Overall, KGM is suggested as the ideal candidate for the pre-emulsification of
peanut oil for emulsified surimi sausage products.

1. Introduction wider application prospects in the production of emulsified surimi

Emulsified surimi sausages are surimi products that are processed
after adding oil into the just-chopped surimi sol. During the emulsifi-
cation process, proteins are moderately denatured, and the whiteness
and water-holding capacity (WHC) of the emulsion system increase
significantly, reducing the cooking loss and making products juicier
(Pietrasik, 2000; Yoo et al., 2007). The surimi gel becomes elastic,
chewy, tender, and crisp, and the original nutrients and inherent flavor
are maximally maintained. As a result, emulsified surimi sausages have
become increasingly popular in the Chinese market. The formation of
emulsified surimi sausages depends on the dissolution of salt-soluble
proteins during the chopping process. Through hydrophobic interac-
tions, fat globules are surrounded by salt-soluble proteins (primarily
myosin) and form an emulsified film (Zahedi et al., 2010). When he-
ated, the myosin that is not involved in the emulsification process ex-
pands, aggregates, and crosslinks to form a network structure. The
emulsified oil droplets are embedded in the voids of the network
structure to act as fillers or copolymers, thereby reducing the porosity
of the gel network (Ziegler and Foegeding, 1990).
Peanut oil has a higher proportion of unsaturated fatty acids than
animal-based oils and does not contain cholesterol. Therefore, it has
sausage (Liu et al., 2010). Vegetable oils are often used as texture
modifiers, color enhancers, and processing aids to improve surimi
products (Park, 2005). Vegetable oil can be added using two methods.
One is to add the oil directly into the surimi sol after chopping. Gao
et al. (2018) found that the physical properties of surimi gel could be
improved by adding oil and strongly agitating the mixture. Benjakul
et al. (2010) found that the addition of vegetable oil to surimi effec-
tively increased its whiteness, but reduced its gel-forming ability and
lowered protein concentrations, decreasing the matrix density and in-
creasing the amount of water released during cooking. When oil is di-
rectly added to the surimi sol, myosin stabilizes the oil droplets by
forming a viscoelastic adsorption layer. The degree of protein absorp-
tion is related to the surface hydrophobicity and carried charge. Once
absorbed, proteins expand, and their secondary and tertiary structures
are rearranged. This exposes hydrophobic residues to the hydrophobic
phase. High protein concentrations are aggregated and interact to form
a coalescing physical barrier on the surface of the oil droplet (Wilde
et al., 2004).
In the second method, oil is pre-emulsified before it is added to the
just-chopped surimi sol. Noffs et al. (2009) found that pre-emulsified
vegetable oil significantly improved the rheological properties of a

Abbreviations: TPA, texture profile analysis; ADSP, acetylated distarch phosphate; KGM, konjac glucomannan; SPI, soy protein isolate; TPA, texture profile analysis;
WHC, water holding capacity
*
Corresponding author.
E-mail address: xueyong@ouc.edu.cn (Y. Xue).

https://doi.org/10.1016/j.jfoodeng.2018.11.018
Received 8 September 2018; Received in revised form 13 November 2018; Accepted 25 November 2018
Available online 26 November 2018
0260-8774/ © 2018 Elsevier Ltd. All rights reserved.
X. Liu et al.
myofibrillar gel network. The emulsified composite gel had sufficient
bonding strength and exhibited excellent rheological behavior under
shear stress. Commonly used emulsifiers are non-food-grade oil-soluble
or water-soluble substances that form flowing, densely packed mole-
cular layers on the surfaces of oil droplets, effectively reducing surface
tension. Generally, emulsifiers do not form viscoelastic surfaces. They
are more active than proteins and form a compact absorbent layer that
relies on charge repulsion or Gibbs-Marangoni mechanisms to stabilize
the oil droplets. Rapid emulsifier diffusion and migration could reduce
surface concentration gradients, which would be lifted. Fast-moving
emulsifier molecules drag the associated continuous phase and prevent
oil droplets from aggregating with one another (Wilde et al., 2004). In
actual surimi emulsion systems, there is usually an interface competi-
tion region between the proteins and the emulsifier, which helps pro-
duce a more sophisticated system.
Few studies have investigated the potential improvements in flavor
in low-fat surimi gels with emulsification. However, several commonly
used food additives have been added to surimi gels to improve their
textural properties, including soy protein isolate (SPI), konjac gluco-
mannan (KGM), and acetylated distarch phosphate (ADSP). There are
no reports on improving the textural characteristics of surimi products
by exploiting the emulsifying properties of these additives. To reduce
the negative effects of adding peanut oil directly into surimi gel, in this
paper, the three additives were used to pre-emulsify the oil prior to its
addition. We examined the effects of using emulsifiers with different
polysaccharide molecular weights (KGM and ADSP) and proteins (SPI).
Texture profile analyses (TPA), whiteness tests, water-holding capa-
cities (WHCs), and emulsion stability experiments were used to eval-
uate the textural changes in the emulsified surimi sausages. Cooking
liquid particle size, and temperature- and frequency-sweep rheology
studies were used to investigate the mechanisms behind the pre-emul-
sification effects. Additionally, the distributions of oil droplets in the
different systems were observed by optical microscopy. This study will
provide technical support for the development of new types of emul-
sified surimi sausage products, and gives a deeper understanding of the
mechanism of the formation of emulsified sausage.
2. Materials and methods
2.1. Materials
Frozen Alaska Pollock surimi (grade AAA) was purchased from
JINCAN Foods Co., Ltd. (Qingdao, Shandong, China). The surimi was
kept at −20 °C prior to use. All the chemicals used were of analytical
grade and were purchased from Sinopharm Chemical Reagent Co., Ltd.
(Shanghai, China). SPI, KGM, and ADSP were purchased from
Zhengzhou Bo Yan Biological Technology Co., Ltd. (Zhengzhou, China).
2.2. Preparation of emulsified surimi sausage
To prepare the emulsified surimi sausage, 250 g of frozen surimi
was partially thawed at 4 °C for 4 h, and then cut into small pieces
(cubes of approximately 3 cm). These cubes were chopped at a speed of
1800 rpm for 5 min in a Stephan vertical vacuum cutter (Model UM 5,
Stephan Machinery Co., Hameln, Germany). A cooling medium (etha-
nol:water, 95:5) was continuously circulated in the double-walled
chopping bowl to maintain the sample temperature below 4 °C during
chopping. Sodium chloride (2.5 wt%) was added and mixed with the
surimi at a speed of 2100 rpm for 3 min under 0.5 bar pressure, to
remove the air pockets that developed during chopping. To the re-
sulting surimi sol, peanut oil was added by different methods to prepare
the emulsified surimi sausage. For the control group, peanut oil (15 wt
%) was added directly into the surimi sol and then mixed at a speed of
2100 rpm for 5 min under 0.5 bar pressure. For the SPI, KGM, and ADSP
groups, peanut oil (15 wt%) and water (12.5 wt%) were pre-emulsified
with SPI (1 g), KGM (0.6 g), or ADSP (1 g), respectively, added into the
31
Journal of Food Engineering 247 (2019) 30–37
surimi sol, and mixed at a speed of 2100 rpm for 5 min under 0.5 bar
pressure. All samples were stuffed into plastic casings (3 cm i.d.), and
the ends sealed tightly. The emulsified surimi sausages were
7 ± 0.5 cm in length, and weighed 50 ± 5 g. All samples were heated
in a water bath at 90 °C for 30 min, then stored at 4 °C prior to mea-
surements.
2.3. TPA tests
TPA tests can provide meaningful information regarding a number
of textural features obtained from a double compression test (Chen,
2015). By compressing the sample twice and simulating the two
chewing actions of the human oral cavity, a result similar to a sensory
evaluation is obtained, and can effectively reflect the textural char-
acteristics of the emulsified surimi sausage. TPA tests of the emulsified
surimi sausage were carried out according to Kaewudom and
Kijroongrojana (2013), with a slight modification. Cylindrical samples
(1 cm in height, 2.5 cm in diameter) were cut with a cork borer for use.
TPA tests were carried out using a TMS-PRO texture analyzer (Food
Technology Co., USA). The TPA mode was used to compress the control,
SPI, KGM, and ADSP emulsified surimi sausages twice with a Ø 25 mm
compression plate and a heavy-duty platform at a deformation of 70%
of the original sample height. The cross-head speed was set at 2.4 mm/s
(16). Three replicate measurements were carried out at 25 °C. From the
resulting force-time curves, the hardness, springiness, cohesiveness,
chewiness, and adhesiveness were determined.
2.4. Determination of WHC and emulsification stability
We measured the WHC and emulsification stability of the emulsified
surimi sausages according to Gao et al. (2018), with a slight mod-
ification. The emulsified surimi sausages (water content: 80%) were cut
into several pieces, and each piece was weighed (X1). The sample was
sandwiched between five pieces of Whatman filter paper (two layers
above, and three below). After the samples were subjected to a pressure
of 5 kg for 3 min, they were removed from the papers and weighed
again (X2). The pressed sausage was dried at 105 °C for 24 h and
weighed again (X3). Three replicate measurements were carried out at
25 °C. The emulsification stability properties (total expressible fluid
(TEF, Eq. (1)), WHC (Eq. (2)), and fat content (Eq. (3)) were calculated
using the following equations:
X1 − X2
TEF% = × 100%
X1 (1)
X1 − X2
WHC = [1 − ] × 100%
X1 (2)
X1 − 2X2 + X3
Fat% = × 100%
X1 − X2 (3)
2.5. Determination of whiteness
The color of the surimi emulsified sausage was determined as de-
scribed by Buamard (2015) using a colorimeter (JP7100F, Juki Cor-
poration, Tokyo, Japan). Three replicate measurements of L* (light-
ness), a* (red hue to green hue), and b* (yellow hue to blue hue) were
made at 25 °C. The whiteness was calculated using the following
equation (Park, 1994):
2 2
[
Whiteness = 100 − (100 − L*)2 + a * + b* ]1/2 (4)
2.6. Particle size analysis of cooking liquor
We analyzed the particle sizes in the cooking liquor of the emulsi-
fied surimi sausage according to Zhang et al., 2017, with some
X. Liu et al.
modifications. The particle sizes of the cooking liquor were investigated
using a Zetasizer NanoZS80 (Malvern Instruments, Worcestershire, UK).
The emulsified surimi sausage was placed in a centrifuge tube and
heated in a water bath at 90 °C for 20 min. Then, the cooking liquor was
collected and added to the sample cell. Three replicate measurements
were carried out at 25 °C.
2.7. Rheological measurements of emulsified surimi sausage
Following the method of Singh (2017), rheological measurements of
the surimi emulsified sausage were carried out using an MCR101 rhe-
ometer (MCR101, Anton Paar, Austria) with a parallel plate (Ø50 mm)
and 1.0-mm gap. The temperature was controlled by a water bath
connected to a Peltier system in the bottom plate. Before the other
rheological measurements, strain sweep tests were performed from
0.01% to 100% at 1 Hz and 25 °C. Curves of the storage modulus (G′)
and loss modulus (G″) versus strain were recorded and analyzed to
determine the linear viscoelasticity (LVE) region of the samples. The
samples were cut into 1 mm slices (about 0.8 g) and placed in the plate
center, respectively; then, the test was started before the samples
equilibrated for 15 min. The rim of each sample was sealed with sili-
cone oil to prevent water loss during the test.
Temperature sweeps of the cold semi-gels and heat-induced gels
were performed from 10 to 100 °C at a rate of 5 °C/min, after which the
gels were maintained at 100 °C for 5 min. The dependence of the G′, G″,
and loss factor on temperature was monitored constantly throughout
the thermal treatment at a frequency of 1 Hz and strain of 2%.
Frequency sweeps were run from 0.1 to 100 rad/s with a 2% strain
(within the LVE) and at 25 °C, to determine the G′ and G″ values as
functions of frequency. The degree of dependence of G′ on the fre-
quency sweep, as well as the strength of the sample (G0′ and G0″) were
obtained by fitting the frequency sweep data into the following power
law models (Eq. (5) and (6)) (Herranz et al., 2012):
'
G' = G0'⋅ωn (5)
''
G'' = G''0⋅ωn (6)
2.8. Light microscopic images and fractal analysis
We used an optical microscope to evaluate the distributions of oil
droplets in the emulsified surimi sausage. Samples were stained with
bromophenol blue and Sudan IV. The samples were treated according to
Zhuang et al., 2016, with some modifications. First, we placed a small
amount of sample on the end of a clean, dry slide, topped with a cover
slide, and gently pressed to produce a thin, uniform sample. Then, we
placed the slide in a refrigerator at 4 °C for 24 h. These prepared
samples were first dyed with 1% bromophenol blue solution (protein
dye) for 3 min. Excess dye solution was rinsed off with distilled water.
Then, the sample was placed in 0.1% Sudan IV dye solution (fat dye) for
3 min, and the excess dye was again rinsed with distilled water. An
Olympus BX-41 optical biomicroscope was used to observe the dis-
tributions of oil droplets in the emulsified surimi sausage. Images were
taken with a high-definition digital camera (DP12) with an eyepiece of
10× and an objective lens of 10×.
The fractal dimension (Df) (Campo-Deaño et al., 2009) is based on
the calculation of the scaling rule, given as follows:
D = −log Nε /log ϵ (7)
Df = D + 1 (8)
2.9. Statistical analysis
All experimental data were calculated as the means ± standard
deviations. Differences between the means of the data were compared
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Journal of Food Engineering 247 (2019) 30–37
Fig. 1. Morphology of surimi emulsified sausage after secondary compression.
by the least significant difference (LSD) test (p < 0.05), which was
calculated using the Statistical Analysis System (SAS Institute, Inc.,
Cary, NC, USA).
3. Results and discussion
3.1. TPA
The morphology of a sample after the secondary compression pro-
cess can be seen in Fig. 1. The samples in the control group were dis-
sipated, while the samples in the SPI, KGM, and ADSP groups remained
intact. The characteristic indexes obtained from the test are shown in
Table 1. The peak obtained by the probe during the first compression
represents the hardness. The results reflect the fact that the addition of
SPI will reduce sample hardness, and the addition of KGM and ADSP
will increase sample hardness. Compared to the control group, the pre-
emulsified SPI, KGM, and ADSP groups exhibited a significant increase
in the cohesiveness, springiness, and chewiness of the emulsified surimi
sausage (p < 0.05). At the same time, the addition of SPI and KGM to
the sausages results in a significant increase in sample adhesiveness
(p < 0.05), whereas the addition of ADSP reduces the sample adhe-
siveness.
From the TPA test results, we can see that the order of structural
improvement of the emulsified surimi sausages after pre-emulsification
using the three food-grade emulsifiers is as follows:
KGM > ADSP > SPI. That is, the use of KGM comprehensively im-
proves the texture of the emulsified surimi sausage. While ADSP pro-
duced the greatest increase in the texture index of the emulsified sau-
sages, it also reduced product cohesiveness, which means that the
tightness of the combination between the components in the emulsified
sausage is decreased. Jimenez-Colmenero et al., 2010 found that
frankfurters produced with emulsified olive oil had better structure.
They suggested that textural improvements were related to the dis-
persion of fat globules. We speculated that pre-emulsification (using our
three emulsifiers) would modify the distribution of oil droplets, leading
to the formation of a different structure.
3.2. WHC and emulsification stability
The WHC refers to the ability of the surimi gel to bind water, and is
an important parameter determining the gel's stability. Emulsified
surimi sausages with high WHC values can lock in a large amount of
water, thus reducing water loss in the heating process (Wang et al.,
2010). The WHC can also reflect the three-dimensional network struc-
ture inside the product. A denser and more uniform structure produces
higher WHC values. As can be seen from Table 2, the WHC values in-
crease significantly for the emulsified SPI, KGM, and ADSP sausages
(p < 0.05), indicating that denser network structures are formed in
samples that undergo a pre-emulsification process. The pre-emulsifi-
cation process using peanut oil produces a surimi sol having improved
stability, smaller fat globule particles, better fat globule distributions in
the protein matrix, and larger protein-film-packaged fat globule cov-
erage. These characteristics improve the WHC values during the heating
process (Youssef and Smith, 2011).
The total expressible fluids (TEF%) and fat content are important
indicators for evaluating the emulsion stability of the emulsified
X. Liu et al. Journal of Food Engineering 247 (2019) 30–37

Table 1
Effects of pre-emulsification by different exogenous additives on TPA properties of emulsified surimi sausage.
Sample Hardness (N) Cohesiveness Springiness Adhesiveness Chewiness (N)

Control 131.37 ± 3.12 b

0.44 ± 0.03 a
0.68 ± 0.06a
−0.57 ± 0.05 b
39.31 ± 1.03a
SPI 111.13 ± 1.23a 0.58 ± 0.04c 0.80 ± 0.02c −1.56 ± 0.40d 51.56 ± 1.34b
KGM 147.17 ± 4.84c 0.59 ± 0.02c 0.80 ± 0.03c −1.17 ± 0.15c 69.46 ± 2.13d
ADSP 148.60 ± 3.70d 0.53 ± 0.04b 0.77 ± 0.02b - 0.37 ± 0.04a 60.64 ± 1.78c

a-d Different letters in the same column indicate significant differences (p < 0.05) among them.

Table 2 that changes in the gel color of surimi are mainly related to the color
Effects of pre-emulsification by different exogenous additives on the WHC and and amount of the additive itself. In this case, the three pre-emulsifiers
emulsification stability properties of emulsified surimi sausage. are white powders themselves, such that adding them would improve
Sample WHC(%) Emulsification stability sample whiteness.

TEF (%) Fat (%) 3.4. Particle size distribution in the cooking liquor
a d d
Control 94.83 ± 0.41 7.19 ± 0.05 3.98 ± 0.08
SPI 95.69 ± 0.68c 6.63 ± 0.23c 3.15 ± 0.09c The cooking liquid refers to the liquid liberated from the emulsified
KGM 95.82 ± 0.59d 6.25 ± 0.35a 2.54 ± 0.06a surimi sausage during heating. Its main components are water, free
ADSP 95.26 ± &#x202F;0.03b 6.37 ± 0.67b 2.78 ± 0.13b protein, and free fat droplets. The water component includes free water
and movable water. By measuring the average particle size of the
a-d Different letters in the same column indicate significant differences
cooking liquor, we can better understand the porosity and order of the
(p < 0.05) among them.
gel network in the emulsified surimi sausage.
The particle size measurement results for the cooking liquids can be
sausages. As can be seen from Table 2, the TEF% decreases from 7.19%
seen in Fig. 2. Two signal peaks were detected in the experiment: one
(control) to 6.63% (SPI), 6.25% (KGM), and 6.37% (ADSP), indicating
for free oil droplets (small size), and one for free protein (large size).
that the three pre-emulsifiers effectively improve the emulsion stability
Compared with the control group (2138 nm), the particle sizes for the
of the sausages. During the pre-emulsification process, the oil and water
SPI (1873 nm), KGM (1392 nm), and ADSP (1267 nm) groups decrease
were pre-emulsified before being added to the surimi, which caused the
significantly (p < 0.05), and the spacings between the two signal
oil droplets to form an emulsified film. The myofibrillar (MF) protein
peaks decrease, indicating that all three emulsifiers effectively reduce
began to compete with the food-grade emulsifier for emulsification,
the sizes of the oil droplets in the emulsified surimi sausage, leading to
transforming the emulsified film into MF-SPI, MF-KGM, or MF-ADSP.
the more even dispersion of oil droplets in the network structure. At the
The substituted exogenous additive either combines with the protein in
same time, the specific surface areas of the oil droplets increase, and
the protein matrix or becomes a filler in the network pores, effectively
strengthen binding to the protein skeleton. Krog et al., 1987 found that
improving the network structure density of the emulsified sausages and
macromolecular surfactants such as proteins produce larger fat globules
increasing their emulsion stability.
than small-molecule emulsifiers. SPI, KGM, and ADSP have lower mo-
lecular weights than myosin. Based on the measurements for the in-
3.3. Whiteness tegrated particle size and inter-peak distances, we can speculate that all
three pre-emulsifiers compete for emulsification with the myofibrillar
Whiteness is an important indicator used to judge the color of the proteins. However, their emulsifying abilities are different. When more
emulsified surimi sausage (Alipour et al., 2018). The frequency of light myofibrillar proteins participate in emulsification, the sizes of the oil
absorbed by a material is related to its internal structure, and thus, the droplets increase, and the myofibrillar protein involved in the forma-
structure of a material greatly affects its color. Changes in color can tion of the gel matrix decreases, resulting in a larger and more unevenly
directly reflect structural changes inside a sample. In general, a larger distributed network structure. With respect to macroscopic reactions,
L* value and lower b* value indicate a whiter and better-quality pro-
duct.
The effects of the three pre-emulsifiers on the whiteness of the
emulsified sausages are presented in Table 3. The whiteness increases
from 84.28 ± 0.12 (control) to 84.50 ± 0.08 (SPI), 84.92 ± 0.09
(KGM), and 85.45 ± 0.12 (ADSP), respectively, indicating that the
three pre-emulsifiers can improve the internal coagulation of the
emulsified sausage. The results correspond to those for WHC. Emulsi-
fied sausages with high WHC values have strong light-reflecting abil-
ities that enhance whiteness. In addition, Benjakul et al., 2010 reported

Table 3
Effects of pre-emulsification by different exogenous additives on the whiteness
of emulsified surimi sausage.
Sample L* a* b* Whiteness

Control 88.25 ± 0.05a −0.06 ± 0.01a 10.45 ± 0.03c 84.28 ± 0.12a

SPI 88.64 ± 0.01b −0.06 ± 0.01a 10.54 ± 0.01d 84.50 ± 0.08b
KGM 88.64 ± 0.03b −0.13 ± 0.02b 9.91 ± 0.01b 84.92 ± 0.09c
ADSP 89.24 ± 0.01c −0.11 ± 0.01c 9.79 ± 0.01a 85.45 ± 0.12d

a-d Different letters in the same column indicate significant differences

(p < 0.05) among them. Fig. 2. Particle size of cooking liquor in the emulsified surimi sausage.

33
X. Liu et al.
Fig. 3. Changes in viscoelastic modulus (G′ and G″, a), and loss factor (Tan δ, b)
during temperature sweep of emulsified surimi sausage at 1 Hz and 1% strain
after emulsification by three emulsifiers.
the particle sizes of the cooking liquid increase and the signal peaks
become more dispersed.
3.5. Rheology measurements
3.5.1. Temperature sweep
The linear viscoelastic (LVE) region of the samples was determined
by strain sweep tests from 0.01% to 100% and at 1 Hz in subsequent
tests, because the viscoelastic material only maintains its viscoelastic
properties in the LVE. Emulsified surimi sausage exhibits a stable sto-
rage modulus (G′) and loss modulus (G″) in the 0.1%–5% strain region
(the data are not shown); thus, all the tests were conducted at strains
within this region.
The effects of temperature on the properties of the emulsified surimi
sausage are shown in Fig. 3a. Changes in the viscoelastic modulus va-
lues (G′ and G″) are closely related to protein denaturation. Wu et al.,
2009 found that myosin was sequentially unfolded and then cross-
linked during the heating process. The G′ value of the control group
slowly rises during the initial heating stage, starts to fall after reaching
the first peak at 26 °C, continues to fall to the lowest point at 47.1 °C,
and then reaches another peak at 79 °C. Peak 1 corresponds to the
denaturation of the myosin head (Tornberg, 2005). The changes in G′
for the SPI, KGM, and ADSP groups are more severe than for the control
group in the initial stage, mainly because the emulsifier participates in
34
Journal of Food Engineering 247 (2019) 30–37
the emulsification process and more myosin is preserved. The myosin
head is oleophilic, encapsulated inside the droplet, and is less prone to
denaturation. Peak 2 corresponds to the unfolding of the myosin tail
(Xiong, 1997a,b). Changes in G′ and G″ in the KGM and ADSP groups
show similar trends to the control, while G′ and G″ in the SPI group
begin to decrease sharply at approximately 80 °C, which may be related
to the denaturation of SPI itself.
The dependence of rheological changes on temperature can also be
expressed by the loss factor, tan delta (Fig. 3b), which represents the
relative ratio of viscosity to elasticity. Compared with the control
group, the three pre-emulsified groups produce a distinct peak at ap-
proximately 40 °C, which is closely related to the expansion of myosin.
The higher the myosin content in the protein matrix, the more sig-
nificant the change in tan delta. Thus, after pre-emulsification by the
three food-grade emulsifiers, more myosin is preserved for participation
in the gelation process, and the emulsification efficiency of myosin also
improves (Hoogenkamp, 1987). As the temperature continues to rise,
the unfolded proteins expose their active groups and begin to interact
with adjacent proteins. The elasticity of the entire system begins to rise
sharply, and so, tan delta drops sharply. Finally, a 3D network structure
is formed by covalent or non-covalent bonds (Yoon et al., 2004). In
addition, the tan delta of the SPI group decreases continuously with
temperature after 40 °C, which is related to the denaturation of SPI. We
speculate that the substituted emulsifiers also participate in the gelation
process, but in different ways. KGM emulsifiers have been observed as
aggregate inserts in proteins, contributing to the formation of poly-
saccharide-protein networks (Ji et al., 2017). ADSP acts as a type of
modified starch that swells during the heating process, thus exerting
pressure on the protein matrix and causing the gel matrix to become
more compact and firmer (Kong et al., 2016). For SPI, we obtained
results contrary to those of Berghout and Goot (2015), who found that
frankfurter hardness increased as the SPI content improved. We believe
that SPI exhibits higher gelling and structuring behavior than myosin in
frankfurters, but lower gelling and structuring behavior in emulsified
surimi sausage. The continuous change of tan delta indicates that it
does not form a stable network structure. This result corresponds to the
low hardness of the emulsified surimi sausage in the SPI group.
3.5.2. Frequency sweep
The spectrum obtained from the frequency sweep, shown in Fig. 4,
provides valuable information regarding the structural characteristics
of the emulsified surimi sausage. The viscoelastic moduli between the
different samples exhibit the same trend (i.e., G′ is significantly larger
Fig. 4. Viscoelastic moduli versus angular frequency at 10 °C for emulsified
surimi sausage.
X. Liu et al. Journal of Food Engineering 247 (2019) 30–37

Table 4
Power law parameters G0′, n′ from Eq. (4), G0″, n′′ from Eq. (5) after different treatments. Experiments were performed at 10 °C.
Sample G0′ n′ G0″ n″ r2

Control 1.042 ± 0.062b 0.107 ± 0.002d 0.196 ± 0.022a 0.116 ± 0.005d 0.99
SPI 0.842 ± 0.049a 0.104 ± 0.002c 0.216 ± 0.033b 0.102 ± 0.005c 0.99
KGM 1.208 ± 0.026c 0.102 ± 0.001b 0.223 ± 0.023c 0.097 ± 0.004b 0.99
ADSP 1.348 ± 0.013d 0.096 ± 0.001a 0.250 ± 0.003d 0.091 ± 0.004a 0.99

a-d Different letters in the same column indicate significant differences (p < 0.05) among them.

than G″). Crossover points were not found in any of the samples
throughout the whole frequency interval, indicating that the four
sample groups formed a stable gel system. We used the power law
model to fit G′ and G″. The results are shown in Table 4. G0′ and G0″
represent the strength of the intramolecular interactions, while n′ and
n″ reflect 1) the degree of protein cross-linking and 2) the stability of
the network structure (Gabriele et al., 2001; Moresi et al., 2004). An n′
value of zero represents a physical gel that is sufficiently cross-linked by
chemical bonds. Lower values of n′ and n″ represent higher degrees of
cross-linking (Ross-Murphy, 1987). As is presented in Table 4, the G0′
values of the control, SPI, KGM, and ADSP group are 1.042 ± 0.062,
0.842 ± 0.049, 1.208 ± 0.026, and 1.348 ± 0.013, respectively,
indicating that SPI pre-emulsification reduces the strength of internal
interactions. This result is consistent with the texture determination
results. The n′ values of the control, SPI, KGM, and ADSP groups are
0.107 ± 0.002, 0.104 ± 0.002, 0.102 ± 0.001, and 0.096 ± 0.001,
respectively. The n″ values exhibit the same trend, indicating that all
three emulsifiers increase the degree of cross-linking between protein
molecules in the emulsified sausage. These results demonstrate that
more protein molecules are preserved because of the presence of the
three “emulsion membranes.” Most of this myosin participates in the
gelation process, thus forming a denser and more ordered gel network
structure.

3.6. Distribution and fractal dimensions of oil droplets

Optical microscopic analysis can truly discern the distribution of oil

droplets in the emulsified surimi sausage. The optical microscopy
images in Fig. 5 clearly show that the oil droplets in the control group
are relatively large and irregularly distributed. Additionally, areas of
accumulated oil droplets are present. After pre-emulsification using the
three emulsifiers, the oil droplets are evenly distributed in the con-
tinuous phase, and the area occupied by the oil droplets in the same
area increases significantly relative to the control group. The larger
specific surface areas of the oil droplets enhance their interactions with
the surrounding proteins.
We used ImageJ software to binarize the images. The fractal di-
mension (Df) was calculated using Eq. (7) and Eq (8). Df is a physical Fig. 5. Light micrographs of emulsified surimi sausage and corresponding
quantity that describes the complexity of an irregular protein network binary images.
(Dàvila and Parés, 2007). So Df was used to detail the distribution and
homogeneity of oil droplets. As shown in Fig. 6, the Df values for the
three food-grade emulsifiers (SPI, KGM, and ADSP) on the properties of
control, SPI, KGM, and ADSP groups are 2.77, 2.83, 2.89, and 2.91,
emulsified surimi sausage were evaluated. From TPA testing, we found
respectively. The addition of the three emulsifiers significantly in-
that the pre-emulsified SPI, KGM, and ADSP groups exhibited a sig-
creases the structural denseness of the emulsified surimi sausage,
nificant increase in the cohesiveness, springiness, and chewiness of the
mainly because they reduce the myosin content involved in the emul-
emulsified surimi sausage than the control group (p < 0.05). But SPI
sification process and promote more myosin participation in the gela-
softened the sausage relative to the control group, reducing the hard-
tion process, thereby contributing to the formation of a gel network
ness from 131.37 ± 3.12 N to 111.13 ± 1.23 N. The adhesiveness of
structure. At the same time, the emulsion film formed by the three
the product decreased from - 0.57 ± 0.05 to - 0.37 ± 0.04 after pre-
emulsifiers causes the oil droplets to become more uniformly dis-
emulsification by ADSP. The WHC and whiteness properties of the
tributed in the network structure, thus increasing binding to the surimi
samples were improved significantly after the addition of pre-emulsi-
protein.
fied peanut oil (p < 0.05). Furthermore, the TEF% decreased from
7.19% (control) to 6.63% (SPI), 6.25% (KGM), and 6.37% (ADSP) and
4. Conclusion thus demonstrated that the three pre-emulsifiers effectively improved
the emulsion stability of the sausages. Particle size measurements of the
In this study, the effects of the pre-emulsification of peanut oil by cooking liquids demonstrated that all three emulsifiers competed for

35
X. Liu et al.
Fig. 6. Example box count plots for the determination of Df from light micro-
graph binary images of emulsified surimi sausage.
emulsification with the myofibrillar proteins and reduced the sizes of
oil droplets in the emulsified surimi sausage. Temperature and fre-
quency-sweep rheological studies indicated that all three emulsifiers
participated in the emulsification process and thus preserved more
myosin for participation in the gelation process, thus forming a denser
and more ordered gel network structure. Optical microscopic analysis
showed that all three emulsifiers produced emulsion membranes
around the oil droplets and promoted their more uniform distribution
in the system. In conclusion, KGM is suggested as the ideal candidate
for the pre-emulsification of peanut oil for emulsified surimi sausage
products. These results provide a new method for the use of food
36
Journal of Food Engineering 247 (2019) 30–37
additives and will also provide technical support for the development of
new types of emulsified surimi sausage products.
Acknowledgements
This study is supported by the National Natural Science Fund of
China (No. 31571865), the Program for Changjiang Scholars and
Innovative Research Team in University (PCSIRT), and Ningbo
Agricultural Major Project (No. 2017C110006).
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