Ultrasonics Sonochemistry 88 (2022) 106105

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Ultrasonics Sonochemistry
journal homepage: www.elsevier.com/locate/ultson

Study on the quality and myofibrillar protein structure of chicken breasts

during thawing of ultrasound-assisted slightly acidic electrolyzed
water (SAEW)
Dewei Kong a, Chunli Quan a, Qian Xi b, Rongwei Han a, Shige Koseki c, Peng Li a, Qijing Du a,
Yongxin Yang a, Fereidoun Forghani d, Jun Wang a, *
a
College of Food Science and Engineering, Qingdao Agricultural University, Qingdao 266109, China
b
College of Food Science and Engineering, Tarim University, Alar 843300, China
c
Research Faculty of Agriculture, Hokkaido University, Sapporo 060-8589, Japan
d
Molecular Epidemiology, Inc, 15300 Bothell Way NE, Lake Forest Park, WA 98155, USA

A R T I C L E I N F O A B S T R A C T

Keywords: The effects of air thawing (AT), water thawing (WT), slightly acidic electrolyzed water (ET), ultrasound-assisted
Ultrasound thawing water thawing (WUT) and ultrasound-assisted slightly acidic electrolyzed water (EUT) on the quality and
Slightly acidic electrolyzed water myofibrillar protein (MP) structure of chicken breasts were investigated. The results showed that WUT and EUT
Quality
could significantly improve the thawing rate compared with AT, WT, and ET groups. The EUT group not only had
Myofibrillar protein
Chicken breasts
lower thawing loss, but also their immobilized and free water contents were similar to fresh sample according to
Thawing methods the low-field nuclear magnetic resonance (LF NMR) results. The EUT treatment had no adverse effect on the
primary structure of the protein. The secondary and tertiary structures of MP were more stable in the EUT group
according to Raman and fluorescence spectra. The muscle fibers microstructure from EUT group was neater and
more compact compared with other thawing methods. Therefore, EUT treatment could be considered as a novel
potential thawing method in the food industry.

1. Introduction in flavor, texture, color, protein degradation and aggregation. The time,
temperature and method of the thawing process are the main factors
In recent years, the production and consumption of chicken have affecting the meat quality change of thawed meat [8]. Currently, there
increased rapidly due to its advantages of low fat, low calorie, and high are several studies on the effect of traditional thawing methods on meat
protein [1]. According to the National Bureau of Statistics of China, the quality. These traditional methods are mainly based on water thawing
production growth rate of poultry meat, mostly chicken, has exceeded [9] and air thawing [10]. However, these methods may have a negative
25 % in the last five years [2]. Poultry meat production is expected to impact on meat quality to some extents [11]. Therefore, as a novel and
reach 28.61 million tons in 2020. Furthermore, per capita consumption efficient thawing method, ultrasonic thawing has been widely used in
of poultry meat in China has increased from 9.1 kg to 12.7 kg in the last meat thawing to speed up the thawing process and reduce the damage to
five years. Because of their high nutritional value and water content [3], meat quality.
as well as the presence of microorganisms and enzymes [4], fresh Recently, ultrasonic thawing technology has attracted more and
chicken breasts are prone to spoilage at room temperature. Therefore, more attention due to its advantages of safety and environmental pro­
they need to be frozen to increase their shelf-life for further processing, tection, uniform thawing, high efficiency and low cost [12]. Ultrasound
which is the most widely used method for all types of meat [5]. can effectively enhance various mass transfer processes [13]. Different
The thawing process is considered a crucial stage for frozen foods from the traditional thawing method from the outside to the inside, both
before further processing. The main goal of thawing is to return frozen the frozen and unfrozen tissues of food absorb the energy generated by
meat to its fresh, unthawed state and quality [6,7]. Improper thawing the attenuation of ultrasonic waves and frozen tissue can absorb more
can result in undesirable changes of meat quality, such as deterioration energy than thawed tissue, thus significantly improving the thawing

* Corresponding author.
E-mail address: [email protected] (J. Wang).

https://doi.org/10.1016/j.ultsonch.2022.106105
Received 25 May 2022; Received in revised form 11 July 2022; Accepted 26 July 2022
Available online 29 July 2022
1350-4177/© 2022 The Author(s). Published by Elsevier B.V. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-
nc-nd/4.0/).
D. Kong et al. Ultrasonics Sonochemistry 88 (2022) 106105

efficiency [14]. At present, ultrasonic thawing has achieved excellent MP was determined using the Biuret method [24].
results in the application for meat [3], fruits [14,15] and vegetables
[16]. Meanwhile, these studies have demonstrated that ultrasonic
thawing can be applied in the food industry. In addition, water is 2.2. Thawing process and curve
commonly used as the thawing media in ultrasonic thawing. However,
Liao et al. [17] found that slightly acidic electrolyzed water (SAEW), as a The frozen chicken breasts samples were thawed using five different
substitute for traditional thawing media water, can also be used as a new treatments: air thawing (AT, 4 ◦ C); water thawing (WT, 4 ◦ C distilled
thawing media. water); slightly acidic electrolyzed water thawing (ET, 4 ◦ C SAEW);
SAEW is made by electrolyzing sodium chloride solution using a ultrasound-assisted water thawing (WUT) and ultrasound-assisted
single chamber compartment without a membrane [18]. In recent years, SAEW thawing (EUT), thawed at applied in a ultrasonic bath (KQ-
SAEW has gained more attention due to its characteristics of antibac­ 400DB, Kunshan ultrasonic instrument Co., ltd, China) with a power of
terial activity and environmental friendliness. As a new thawing media, 200 W and frequency of 40 kHz using distilled water and SAEW in
its safety is unquestionable, because it can get back to its initial form thawing process, respectively. After removing the polyethylene bags,
when organic matter is existed [19]. In addition, as a food additive, each sample was placed into a beaker (500 mL) for thawing at 4 ◦ C by
SAEW has been applied in the U.S., Japan and Korea [17]. Xuan et al. adding ice.
found that SAEW ice could significantly inhibit myofibrillar protein During the thawing process, a temperature recorder (NAPUI ther­
degradation [20]. Liao et al. found that SAEW which was used as an mocouple, Mod. TR 230X-8, Guangdong, China) was used to continu­
active thawing media can better retard lipids and protein oxidation [17]. ously record the thawing time and sample temperature until the
Cichoski et al. observed that the combined treatment of ultrasound and geometric center temperature of the sample reached 0 ◦ C.
SAEW not only improved the microbial quality of chicken breasts, but
also effectively delayed myofibrillar protein (MP) oxidation [21].
2.3. pH and color
Although there are some studies available on the application of
ultrasound-assisted thawing in meat products, the effects of thawing
A 10 g sample of chicken breasts was added to 100 mL deionized
media on the quality and MP structure of chicken breasts were not
water and then homogenized (MiniMix 100, Interscience, France) for 5
previously done. Therefore, this research aimed to evaluate the effects of
min. The precipitated meat tissue was filtered off with filter paper. The
thawing methods on quality and MP structure of chicken breasts. The
filtrate was measured with a pH meter (FE20, Mettler-Toledo, Mettler
thawing rate, meat quality, microstructure, MP primary structure, sec­
Toledo Instruments Co., ltd., China) at room temperature. The pH
ondary and tertiary structure of chicken breasts under five thawing
electrodes were calibrated in pH 4.01 and pH 7.00 standard buffers at
methods were evaluated.
room temperature before measuring pH.
The color of chicken breasts was determined by a colorimeter (CR-
2. Materials and methods 400, Konica Minolta Inc., Osaka, Japan) with an 8 mm aperture, 2◦
observer and illuminant C. The color changes were described using the
2.1. Preparation of samples color space of L*, a*, and b*. The colorimeter was calibrated using a
white calibration plate before measurement.
2.1.1. Materials
Fresh chicken breasts were purchased in a local supermarket
(Qingdao, China). The chicken breasts were trimmed into samples of 2.4. Water holding capacity (WHC)
uniform size, shape and weight (3 × 3 × 3 cm3, 64 ± 5 g) after removing
fat, fascia and connective tissue, and then divided into 6 groups. One 2.4.1. Thawing loss
group, served as the control, and the remaining five groups were indi­ The thawing loss was determined following the method of Wang
vidually packed in polyethylene bag to prevent water loss during stor­ et al. [25]. Before thawing, the sample weight was quickly measured and
age, pre-cooled at 4 ◦ C for about 3 h and frozen at − 20 ◦ C for 4 weeks. expressed as M0. The sample was thawed until its geometric center
temperature reached 0 ◦ C, weighed again and expressed as M1.
2.1.2. SAEW preparation
Thawingloss(%) = (M0 − M1 )/M0 × 100%
SAEW was made by electrolyzing a mixture of NaCl and HCl solution
in a device (Anywhere-320 W, Beijing, China) with a voltage of 220 V
and a current of 8.0 A for 20 min at room temperature. The pH and 2.4.2. Cooking loss
oxidation reduction potential (ORP) of SAEW were determined by a pH The cooking loss was determined following the method of Liao et al.
meter (FE20, Mettler-Toledo, Mettler Toledo Instruments Co., ltd., [17] with minor modifications. The sample (M2) was placed in a
China). The available chlorine concentration (ACC) was measured by a centrifuge tube in an 80 ◦ C water bath for 30 min. Then, the samples
digital chlorine test kit (RC-3F, Saitama, Japan). SAEW was used as the were removed from the centrifuge tubes and cooled to room tempera­
thawing media with a pH of 6.25, ORP of 875 mV, and ACC of 35 mg/L. ture. After that, the sample weight was recorded as M3.
Cookingloss(%) = (M2 − M3 )/M2 × 100%
2.1.3. MP extraction
MP was extracted from chicken breasts following the methods of
Lefevre et al. [22] and Xiao et al. [23] with some modifications. The 2.5. Low-field nuclear magnetic resonance (LF-NMR)
samples were added to 10 times the volume of 20 mM buffer A (con­
taining 100 mM NaCl, 1 mM EDTA, pH 7.0) and then homogenized at The water distribution was performed by LF NMR analyzer (NIMI20-
15,000 rpm for 1 min at 4 ◦ C. Subsequently, the filtered liquid was 040 V-I, Suzhou, China). The LF NMR analyzer was firstly calibrated by
centrifuged at 6,000 rpm for 15 min at 4 ◦ C (5810R, Eppendorf, Q-Free Induction Decay (Q-FID) procedure with a standard oil sample.
Hamburg, Germany) and the supernatant was discarded. After that, the The chicken breasts (1 × 1 × 2 cm3) were placed in 40 mm tubes. The
same operation is repeated twice. The precipitate was homogenized and relaxation time (T2) was measured by the Carr-Purcell-Meiboom-Gill
centrifuged at 4 ◦ C after the addition of 4 times the volume of 0.1 M NaCl (CPMG) procedure. The image was obtained through inversion, and
solution. The above operation was repeated twice. The resulting pre­ further analysis was performed to obtain relaxation time and peak area
cipitates were purified MP. Purified MP precipitates were diluted with ratios using MultiExp Inv Analysis software (Suzhou Niumai Analytical
25 mM buffer B (containing 0.6 M NaCl, pH 7.0). The concentration of Instruments Co., ltd.).

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D. Kong et al. Ultrasonics Sonochemistry 88 (2022) 106105

Fig. 1. The temperature–time curve (A) and thawing time (B) under different thawing methods. AT, air thawing; WT, water thawing; ET, slightly acidic electrolyzed
water immersion thawing; WUT, ultrasound-assisted water thawing; EUT, ultrasound-assisted slightly acidic electrolyzed water thawing. Different letters for the
same index indicate significant differences (P ≤ 0.05).

2.6. Texture profile analysis (TPA) and shear force spectrum (DXR 2Xi, Thermo Fisher Scientific, USA), which was equip­
ped with a 50 × objective and a 532 nm laser to capture a full spectral
The TPA was determined following the method of Li et al. [3] with range of 400–3400 cm− 1. The sample was placed on a single concave
some modifications. The samples were tested in two-cycle compression slide for spectra scanning. Data acquisition of Raman spectra was per­
TPA mode using an analyzer (TA-XT plus C, SMS Co., ltd., UK). The formed using a 50 μm slit, 10.0 mW laser power, 0.25 s exposure time,
samples were cut into cubes (2 × 2 × 1 cm3). The P 50/R probe was used and 120 scans. Secondary structure was calculated by amide I spectra of
to determine the texture of the sample. The TPA determination condi­ Raman spectrum. The Raman spectrum of the sample was analyzed
tions are as follows: 50 % compression; 5 g trigger force; pre-test, test using Peakfit 4.12 software (San Rafael, CA, USA) to obtain protein
and post-test speed of 5 mm/s. The TPA parameters of the sample were secondary structure content. Secondary structure in Raman spectros­
automatically calculated by the supporting software. copy were shown as: 1615–1637 cm− 1 (β-sheet), 1637–1645 cm− 1
The shear force was determined on a tenderness analyzer (C-LM3B, (random coil), 1646–1664 cm− 1 (α-helix), 1664–1680 cm− 1 (β-turn),
Tenovo, Beijing, China). The samples were cut into cuboid (2 × 2 × 5 and 1680–1700 cm− 1 (β-sheet).
cm3) along the direction parallel to the muscle fibers.
2.9. Tertiary structure
2.7. MP primary structure
Intrinsic fluorescence spectra of MP solution (0.2 mg/mL) were
2.7.1. Total sulfhydryl content measured by a spectrophotometer (F-2700, Hitachi, Japan). The deter­
The total sulfhydryl content was measured following the method of mination conditions of fluorescence spectra were as follows: excitation
Benjakul et al. [26] with slight modifications. One mL of MP solution (1 wavelength of 280 nm and emission spectrum of 300 to 400 nm.
mg/mL) was added to 9 mL of 0.2 M Tris-HCl (containing 1 mM EDTA,
0.6 M KCl, 8 M urea, 2 % SDS, pH 6.8) and mixed well. The above 2.10. Scanning electron microscopy (SEM)
mixture of 4 mL was added with 0.4 mL of 0.1 % 5,5′ -dithiobis (2-nitro)
benzoic acid. Then, the mixture was kept for 25 min at 40 ◦ C. The Chicken breast samples were cut into slices (2 × 2 × 1.5 mm3) and
absorbance was determined by spectrophotometer (TU-1810, Beijing, placed in 2.5 % glutaraldehyde solution at 4 ◦ C for overnight fixation.
China) at 412 nm, and the blank was replaced by 0.6 M KCl solution. After fixation, the samples were washed three times using phosphate
Each group was measured in triplicate. The total sulfhydryl content was buffer. The samples were eluted using ethanol solutions (50, 70, 80, 90,
calculated as follows: and 100 %). Subsequently, the samples were put in the freeze-drying
(
Total sulfhydryl content (nmol/mg) = A412 × 106 / 1.36 × 104
) machine and coated with gold. Finally, the samples were observed
with SEM (S-3400 N, Hitachi, Tokyo, Japan) at 2000 × Magnification.
2.7.2. Carbonyl content
The carbonyl content was measured by the method of Sun et al. [27]. 2.11. Statistical analysis
Two mL of MP solution (2 mg/mL) was added to 2 mL of 10 mM DNPH at
37 ◦ C for 1 h. After that, the above mixture was centrifuged to obtain Data were analyzed by Duncan’s multiple range test using IBM SPSS
precipitate. The precipitate was washed by ethyl acetate-ethanol solu­ 23 (IBM Corporation, Armonk NY, USA). P ≤ 0.05 indicated a significant
tion and then added to 5 mL of 6 M guanidine hydrochloride solution difference in the data. All the experiments were carried out in triplicate.
and kept at 37 ◦ C until the precipitate was dissolved. The above mixture The data were expressed as mean ± standard deviation. All figures were
was centrifuged to get the supernatant. Finally, the absorbance of the generated using Origin 2018 (Origin Lab Corp., MA, USA).
supernatant was determined by a spectrophotometer (TU-1810, Beijing,
China) at 370 nm. The carbonyl content was calculated as follows: 3. Results and discussion
( )
Carbonyl content (nmol/mgs) = A370 × 106 / 2.2 × 104 3.1. Thawing curve

2.8. Secondary structure The thawing process and thawing time of the chicken breasts are
shown in Fig. 1A and Fig. 1B, respectively. The AT group had the longest
The secondary structure of the sample was measured using Raman thawing time among the five thawing methods, which reached 859.38

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D. Kong et al. Ultrasonics Sonochemistry 88 (2022) 106105

Table 1
Changes in the pH and color under different thawing methods. Control, fresh
chicken breasts; AT, air thawing; WT, water thawing; ET, slightly acidic elec­
trolyzed water immersion thawing; WUT, ultrasound-assisted water thawing;
EUT, ultrasound-assisted slightly acidic electrolyzed water thawing.
Thawing pH L* a* b* ΔE
methods

Control 6.02 ± 62.31 ± 2.24 ± 10.15 ± –

0.05a 0.39a 0.74a 0.47a
AT 6.04 ± 53.15 ± 2.21 ± 10.20 ± 45.26 ±
0.13a 1.68c 0.67a 1.42a 1.43a
WT 6.05 ± 60.32 ± 1.82 ± 10.56 ± 38.21 ±
0.05a 3.59ab 0.31a 1.52a 3.50b
ET 5.95 ± 60.59 ± 1.86 ± 10.49 ± 39.11 ±
0.05a 3.82ab 0.55a 3.08a 2.60b
WUT 6.09 ± 58.80 ± 1.94 ± 10.23 ± 40.16 ±
0.07a 1.40b 0.19a 0.87a 1.22b
EUT 6.03 ± 61.92 ± 1.99 ± 10.02 ± 38.36 ±
0.06a 2.44ab 0.77a 2.57a 1.47b

The results are mean ± SD. Different letters for the same index indicate signif­
icant differences (P ≤ 0.05). Fig. 3. The thawing loss and cooking loss under different thawing methods.
Control, fresh chicken breasts; AT, air thawing; WT, water thawing; ET, slightly
acidic electrolyzed water immersion thawing; WUT, ultrasound-assisted water
thawing; EUT, ultrasound-assisted slightly acidic electrolyzed water thawing.
Different letters for the same index indicate significant differences (P ≤ 0.05).

Table 2
Changes in the texture (hardness, springiness, chewiness, and resilience) and
shear force under different thawing methods. Control, fresh chicken breasts; AT,
air thawing; WT, water thawing; ET, slightly acidic electrolyzed water immer­
sion thawing; WUT, ultrasound-assisted water thawing; EUT, ultrasound-
assisted slightly acidic electrolyzed water thawing.
Thawing Hardness/g Springiness Chewiness Resilience Shear
methods force/
N

Control 8799.46 ± 0.95 ± 2926.91 ± 0.58 ± 15.08

827.39b 0.01a 565.32d 0.02a ± 0.67d
AT 11831.96 0.75 ± 4199.45 ± 0.36 ± 36.88
± 1083.48a 0.02cd 914.85c 0.02c ± 1.92a
WT 10926.36 0.69 ± 6556.17 ± 0.47 ± 21.00
± 974.04a 0.03e 126.93ab 0.06b ± 0.78b
ET 11054.84 0.72 ± 3972.55 ± 0.51 ± 19.25
± 1663.43a 0.02de 563.81c 0.01ab ±
1.69bc
WUT 12670.73 0.79 ± 7177.22 ± 0.55 ± 17.47
± 297.25a 0.03c 504.06a 0.05ab ± 1.25c
EUT 8018.95 ± 0.86 ± 5781.91 ± 0.57 ± 15.00
1089.60b 0.02b 78.74b 0.08a ± 0.72d

The results are mean ± SD. Different letters for the same index indicate signif­
icant differences (P ≤ 0.05).

thermal conductivity of ice is larger than water [29]. On the other hand,
the temperature difference between the samples and the thawing media
Fig. 2. The photographs of samples under different thawing methods. Control, is larger, thus the heat transfer rate is faster [30]. However, the thawing
fresh chicken breasts; AT, air thawing; WT, water thawing; ET, slightly acidic curve tends to flatten out and the thawing rate is low during the phase
electrolyzed water immersion thawing; WUT, ultrasound-assisted water thaw­ transformation stage. Because the phase change process needs to absorb
ing; EUT, ultrasound-assisted slightly acidic electrolyzed water thawing. more heat [31]. In addition, the thermal conductivity of the sample
decreases as the ice crystals are transformed into water. Application of
min. Compared to the AT group, the thawing times of the WT, ET, WUT ultrasonic thawing to improve thawing efficiency can be explained as
and EUT groups were reduced by 80.62 %, 85.56 %, 97.30 % and 97.23 follows: the ultrasound energy is mainly attenuated by the frozen tissue
%, respectively. The results showed that WUT and EUT treatments can and transferred from mechanical energy to thermal energy, thus
reduce the thawing time and improve the thawing efficiency. The speeding up the thawing process [4]. Ultrasonic waves are more atten­
thawing rate was defined as the ratio of the temperature difference uated in the freezing zone than in the thawing zone. The heat generated
before and after thawing to the thawing time [28]. The thawing process by the attenuation of ultrasonic waves is mainly applied to the boundary
can generally be grouped into two phases depending on the thawing of the thawing/freezing zone, thereby significantly improving thawing
rate, the endothermic phase (− 18 to − 5 ◦ C) and the phase change phase efficiency [14]. In addition, Kiani et al. [32] found that the micro-jet and
(− 5 to 0 ◦ C). In the endothermal stage, the temperature in the center of cavitation effect generated by ultrasonic waves during the media
all samples increases rapidly. On the one hand, this is because most of propagation can also increase the heat transfer rate, thus accelerating
the water in the samples exists in the form of ice crystals, and the the thawing process. In conclusion, the EUT and WUT thawing rates

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D. Kong et al. Ultrasonics Sonochemistry 88 (2022) 106105

Fig. 4. The moisture migration (A), relaxation times T2 (B) and the peak area ratio P2 (C) under different thawing methods. Control, fresh chicken breasts; AT, air
thawing; WT, water thawing; ET, slightly acidic electrolyzed water immersion thawing; WUT, ultrasound-assisted water thawing; EUT, ultrasound-assisted slightly
acidic electrolyzed water thawing. Different letters for the same index indicate significant differences (P ≤ 0.05).

were relatively faster compared to the WT and ET groups, suggesting

that it is mainly ultrasound that plays an important role in the thawing
process. In combination with ultrasound, both water and slightly acidic
potential water have less effect on the thawing rate.

3.2. pH and color

The pH value is an important indicator which can affect the meat

color, cooking loss, and shear force. Due to glycolysis, the acid sub­
stances produced in the muscle may cause a decrease in pH during the
thawing process [33]. In contrast, nitrogenous substances are broken
down into alkaline substances, causing an increase in the pH [34].
However, the pH of all groups was not significantly different (P > 0.05),
which indicated that the treatments had no negative impact on the pH of
chicken breasts.
Color has an important influence on the appearance and accept­
ability of frozen products. During freezing and thawing, protein dena­
turation, pigment degradation, and lipid oxidation all can lead to color
Fig. 5. The carbonyl content and total sulfhydryl content under different changes in meat. Yi et al. [35] found that lipid oxidation is the main
thawing methods. Control, fresh chicken breasts; AT, air thawing; WT, water reason for the increase in the b* value of meat. The color changes under
thawing; ET, slightly acidic electrolyzed water immersion thawing; WUT, different thawing methods are shown in Table 1. The L* of chicken
ultrasound-assisted water thawing; EUT, ultrasound-assisted slightly acidic
breasts was reduced under different thawing methods, and the L* from
electrolyzed water thawing. Different letters for the same index indicate sig­
AT and WUT groups had significant differences (P ≤ 0.05). Therefore,
nificant differences (P ≤ 0.05).
AT and WUT treatments may cause damage to the quality of chicken
breasts. The change of a* may be related to denaturation of myoglobin
and loss of pigment. The main reason for the change in b* is the for­
mation of yellow pigment due to lipid oxidation [35]. Guo et al. [36]

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D. Kong et al. Ultrasonics Sonochemistry 88 (2022) 106105

Fig. 6. Raman spectra (A), secondary structure content (B), and the second derivative fitted curve of the Amide I band (C) under different thawing methods. Control,
fresh chicken breasts; AT, air thawing; WT, water thawing; ET, slightly acidic electrolyzed water immersion thawing; WUT, ultrasound-assisted water thawing; EUT,
ultrasound-assisted slightly acidic electrolyzed water thawing. Different letters for the same index indicate significant differences (P ≤ 0.05).

also found that the increase in b* value may be related to lipid oxidation. %, which was the highest among all groups. Because the muscle fiber
The total color difference (ΔE) between the samples is mainly caused by structure of the AT group samples was severely damaged during the
the L*, a* and b* values during thawing process. The ΔE was the largest thawing process. However, WUT and EUT groups had the lowest
in the AT group, which was significantly different from the sample of thawing loss among all treatments. Because ultrasound treatment im­
other thawing groups (P ≤ 0.05). In addition, the color difference of the proves the structural characteristics of myosin and increases the water
samples can be visually represented by photographs (Fig. 2). We found holding capacity of muscle proteins [37]. In addition, EUT and WUT can
that the samples surface of WT and ET groups was paler than WUT and accelerate the thawing rate and reduce the degradation of muscle fibers,
EUT groups. Because the thawing rate of WT and ET groups was slow. thus improving the water holding capacity. The thawing loss from the
The samples were soaked in the thawing medium for a long time. It can EUT and WUT groups was not significantly different (P > 0.05), indi­
be concluded that the thawing methods did not change the color of the cating that the thawing media did not affect the thawing loss of chicken
samples, except for the AT group. The L*, a*, and b* between the EUT breasts. In addition, we believe that there is an important association
group and control group did not differ significantly (P > 0.05), which between thawing loss and thawing time of the sample. This can be
indicated that EUT treatment did not cause the change in the color of explained by the fact that the longer the thawing time, the more severely
chicken breasts. the muscle structure would be damaged due to protein oxidation and
degradation, resulting in hindered reabsorption of water [30].
Cooking loss includes the loss of a large portion of water and some
3.3. Water holding capacity (WHC) nutrients after heating. Thawed food may have better quality due to
lower cooking loss. AT group had the lowest cooking loss of 39.63 %
The WHC changes under different thawing methods are shown in among all thawing methods. However, the cooking loss was not signif­
Fig. 3. Ice crystals can damage the muscle tissue, thus leading to a icantly different among the WT, ET, WUT and EUT groups (P > 0.05).
decreased WHC of the muscle. The thawing loss from AT group was 4.29

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D. Kong et al. Ultrasonics Sonochemistry 88 (2022) 106105

compared with control group, the springiness from all thawed groups
was significantly lower (P ≤ 0.05), but the springiness between EUT
group and control group was the closest. The result may be explained as
follows: on the one hand, the ice crystals can damage the muscle tissue
structure of the chicken breasts. On the other hand, water reabsorption
of the sample was affected during thawing to some extents [30]. In terms
of chewiness, all thawed groups had significantly higher (P ≤ 0.05). The
deterioration of meat texture was associated with internal factors of
water loss and protein degradation [34] and external factors of thawing
time and thawing temperature.
Shear force is negatively correlated with meat tenderness. According
to Table 2, the shear force from AT, WT, ET, and WUT groups was
significantly increased than control group (P ≤ 0.05). We believe that
thawing loss is the main reason for the increased cutting force. However,
the shear force did not differ significantly between the EUT and control
groups. (P > 0.05), which indicated that EUT can maintain the tender­
ness of chicken breasts.
The results in Table 2 indicated that the texture and tenderness of the
Fig. 7. The MP intrinsic fluorescence under different thawing methods. Con­ EUT group were closer to the control group. The reasons can be
trol, fresh chicken breasts; AT, air thawing; WT, water thawing; ET, slightly explained as follows: ultrasonic power may improve the tenderness of
acidic electrolyzed water immersion thawing; WUT, ultrasound-assisted water meat [40]. In addition, the residual components in the SAEW were
thawing; EUT, ultrasound-assisted slightly acidic electrolyzed water thawing. effective in maintaining the tenderness of meat.
Different letters for the same index indicate significant differences (P ≤ 0.05).

3.5. LF-NMR
This may be explained by the AT group had the largest thawing loss.
Because the disruption of muscle protein structure can lead to an in­
The relaxation time (T2) under different thawing methods is shown
crease in thawing loss due to the loss of free water, which led to a
in Fig. 4A. T21 stands for bound water in samples. The bound water was
reduction in cooking loss [38].
not easily affected by heating or freeze–thaw process. T22 stands for
immobilized water intracellularly, which is located within the MP
3.4. Texture profile analysis (TPA) and shear force structure. T23 stands for free water that is easily lost outside the cell
[41]. According to Fig. 4B, T21 and T22 relaxation times were not
Textural characteristics are one of the main sensory indicators of significantly different for all groups (P > 0.05). Because bound water is
meat products. As seen in Table 2, the thawing methods had an tightly bonded to muscle proteins, which are not affected by mechanical
important effect on the variation of the texture of chicken breasts. The stress and microstructural changes during freeze-thawing [38]. The T23
hardness between EUT group and control group was not significantly relaxation time of AT group was significantly lower (P ≤ 0.05). This
different (P > 0.05). In combination with previous studies, the residual reason may be related to thawing time and thawing loss of AT group.
sodium chloride and other components of SAEW are beneficial in However, Li et al. [42] found that the higher T2 relaxation time indi­
maintaining the hardness of thawed meat products [39]. After thawing, cated higher mobility of water and a lower water holding capacity.

Fig. 8. The muscle fibers microstructure under different thawing methods (magnification: 2000 × ). Control, fresh chicken breasts; AT, air thawing; WT, water
thawing; ET, slightly acidic electrolyzed water immersion thawing; WUT, ultrasound-assisted water thawing; EUT, ultrasound-assisted slightly acidic electrolyzed
water thawing.

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D. Kong et al. Ultrasonics Sonochemistry 88 (2022) 106105

P21, P22, and P23 represent the proportions of peak areas of T21, T22, that the microenvironment of Trp and Tyr residues was altered in the
and T23, respectively. According to Fig. 4C, the bound water content did thawed groups. However, the λmax from the ET and EUT groups was
not differ significantly between all thawed groups and control group (P closest to the control group, probably because the hypochlorite ion in
> 0.05). The P22 of WT group was significantly lower (P ≤ 0.05) and the SAEW is an electron-absorbing group [17], which maintained the micro-
P23 was significantly higher (P ≤ 0.05), indicating that more immobi­ environment of amino acid residues in the groups to some extent. The
lized water was transferred to the outside of the cells and the thawing results indicate that EUT and ET treatments had less influence on protein
loss was severe in the WT group. P23 between the EUT group and control tertiary structure.
group did not differ significantly (P > 0.05). Therefore, the results
indicated that ultrasound-assisted thawing could maintain more 3.9. Scanning electron microscopy (SEM)
immobilized water and had better water holding capacity.
The microstructure of the longitudinal muscle tissues under different
3.6. Protein primary structure thawing methods is shown in Fig. 8. The muscle fibers from the control
group had a smooth surface and a tight structure. In the AT group, the
The change in the total sulfhydryl content under different thawing muscle fibers were cross-linked and bent, and the overall structure of the
methods is shown in Fig. 5. The sulfhydryl groups are easily converted to muscle surface was disorganized and rough. Compared with the other
disulfide bonds during muscle storage and processing [43]. Although the thawing methods, the muscle structure from AT group was most severely
total sulfhydryl content of the thawed groups was lower, the difference damaged. The reason may be related to the longer time required for the
was not significant between control group and thawed groups (P > thawing process in the AT group. This might be due to the longer time of
0.05). This suggests that all thawing methods can have a certain effect AT group during thawing. The muscle fiber’s surface from WT and ET
on the structure of the proteins. The sulfhydryl groups hidden in the groups was rough and the ordered structure was disrupted. In addition,
internal regions of the protein are exposed to the surface and oxidized to the muscle fibers from the WT and ET groups showed significant frac­
disulfide bonds [44]. tures and increased gaps between fibers. This may be related to the
The change in carbonyl content under different thawing methods is formation of large ice crystals, which led to the destruction of muscle
shown in Fig. 5. Carbonylation is one of the most significant chemical tissue [46]. Jiang et al. [47] found that the gaps between muscle fibers
modifications of protein oxidation. The carbonyl content from AT, WT were related to WHC. This is consistent with the result of thawing loss in
and WUT groups was significantly higher (P ≤ 0.05). However, the our study. Among all thawed groups, the muscle fibers structure from
difference between control group and EUT group was not significant (P WUT and EUT groups showed the least change compared with the
> 0.05). The result indicated that EUT treatments could better delay the control group. However, we found that the muscle fibers from the EUT
protein oxidation of chicken breasts during the thawing process. The group had a neater structure, more dense arrangement and smoother
SAEW components (HCl, Cl2, and HClO) can maintain the stability of the surface compared with the WUT group.
protein. Combined with the changes in carbonyl groups and total sulf­
hydryl groups, EUT treatment could better delay the oxidation and 4. Conclusions
degradation of chicken breasts proteins.
In this study, the effects of different thawing methods on the quality
3.7. Secondary structure and protein structure of chicken breasts were evaluated. We found that
WUT and EUT not only increased the thawing rate but also effectively
Fig. 6A and Fig. 6B show Raman spectra at 400–3400 cm− 1 and reduced the thawing loss of chicken breasts compared with other
second structure content of protein, respectively. Fig. 6C shows the thawing methods. According to LFNMR, the immobilized water and free
curve obtained by baseline correction, deconvolution, second-order water contents from WUT and EUT groups were closest to the control
derivation and iterative fitting of the Raman spectra in the range of group. The EUT treatment could maintain the color and pH of the
1600–1700 cm− 1. The α-helix content from AT, WT, ET, and WUT samples and effectively inhibit lipid oxidation. As for the TPA, shear
groups was significantly decreased (P ≤ 0.05). This is because the pro­ force, and SEM, the EUT group showed the least change in quality
tein structure is disrupted during thawing, resulting in the exposure of compared with other thawing methods. In addition, ET and EUT treat­
hydrophobic groups. Jia et al. [45] found that the stability of the α-helix ments did not negatively affect the primary structure of the proteins.
structure in proteins depends mainly on the hydrogen bonds. Therefore, According to Raman and fluorescence spectra, the secondary and ter­
this phenomenon may also be due to the disruption of hydrogen bonds tiary structures of MP were more stable in the EUT group. Compared
within the protein [42]. The β-sheet content from EUT group was with other thawing treatments, EUT treatment not only could better
significantly lower. This is due to protein aggregation caused by hy­ maintain the quality of chicken breasts but also effectively reduced the
drophobic interactions [38]. In addition, the content of the β-turn and protein structure changes during the thawing process. In conclusion,
random coil between EUT group and control group did not differ EUT has a positive impact on the quality and protein structure of thawed
significantly (P > 0.05), indicating that EUT treatment did not disrupt chicken breast. As a promising thawing method, EUT can provide a
the secondary structure of the proteins. In brief, the EUT group had more theoretical basis for the subsequent processing and utilization of chicken
stable protein structures compared with other thawing methods. breast in food industry.

3.8. Tertiary structure Declaration of Competing Interest

The intrinsic fluorescence spectra of MP under different thawing The authors declare that they have no known competing financial
methods is shown in Fig. 7. Intrinsic fluorescence is mainly generated interests or personal relationships that could have appeared to influence
from tryptophan residues (Trp) and tyrosine residues (Tyr) in proteins. the work reported in this paper.
The fluorescence intensities from AT, WT, ET, WUT, and EUT groups
were higher (P ≤ 0.05), but the fluorescence intensities from ET and EUT Data availability
groups were closer to the control group. The main reason is that the MP
structure was disrupted during the thawing process, resulting in the Data will be made available on request.
exposure of Trp and Tyr residues. The maximum fluorescence emission
peak (λmax) indicates the extent of conformational changes. The λmax
from AT, WT, ET, WUT, and EUT groups was blue-shifted, indicating

8
D. Kong et al. Ultrasonics Sonochemistry 88 (2022) 106105

Acknowledgments [21] A.J. Cichoski, D.R.M. Flores, C.R. De Menezes, E. Jacob-Lopes, L.Q. Zepka,
R. Wagner, J.S. Barin, E.M. de Moraes Flores, M. da Cruz Fernandes, P.C.
B. Campagnol, Ultrasound and slightly acid electrolyzed water application: An
This research was supported by a grant from National Natural Sci­ efficient combination to reduce the bacterial counts of chicken breast during pre-
ence Foundation of China (U2003117), Postgraduate Innovation Pro­ chilling, Int. J. Food Microbiol. 301 (2019) 27–33, https://doi.org/10.1016/j.
gram of Qingdao Agricultural University (QNYCX21036) and Science ijfoodmicro.2019.05.004.
[22] F. Lefevre, B. Fauconneau, J.W. Thompson, T.A. Gill, Thermal Denaturation and
and Technology Commissioner Action Plan Project of Shandong Prov­ Aggregation Properties of Atlantic Salmon Myofibrils and Myosin from White and
ince (2020KJTPY019). Red Muscles, J. Agric. Food Chem. 55 (2007) 4761–4770, https://doi.org/
10.1021/jf063045d.
[23] H. Xiao, Y. Wu, J. Liu, L. Zhou, X. Zeng, X. Zhao, Potential mechanism of different
References gelation properties of white and red muscle fibre from crocodile (Crocodylus
siamensis) meat: Study of myofibrillar protein, LWT–Food Sci. Technol. 143
[1] J.S. Lee, J.W. Han, M. Jung, K.W. Lee, M.S. Chung, Effects of Thawing and Frying (2021), 111045, https://doi.org/10.1016/j.lwt.2021.111045.
Methods on the Formation of Acrylamide and Polycyclic Aromatic Hydrocarbons in [24] A.G. Gornall, C.J. Bardawill, M.M. David, Determination of serum proteins by
Chicken Meat, Foods 9 (2020) 573, https://doi.org/10.3390/foods9050573. means of the biuret reaction, J. Biol. Chem. 177 (1949) 751–756, https://doi.org/
[2] National Bureau of Statistics of the PRC, CHINA STATISTICAL YEARBOOK, China 10.1016/s0021-9258(18)57021-6.
Statistics Press, Beijing, 2021. [25] Y.-Y. Wang, J.-K. Yan, M.T. Rashid, Y. Ding, F. Chikari, S. Huang, H. Ma, Dual-
[3] D. Li, H. Zhao, A.I. Muhammad, L. Song, M. Guo, D. Liu, The comparison of frequency sequential ultrasound thawing for improving the quality of quick-frozen
ultrasound-assisted thawing, air thawing and water immersion thawing on the small yellow croaker and its possible mechanisms, Innovative Food Sci. Emerging
quality of slow/fast freezing bighead carp (Aristichthys nobilis) fillets, Food Chem. Technol. 68 (2021), 102614, https://doi.org/10.1016/j.ifset.2021.102614.
320 (2020), 126614, https://doi.org/10.1016/j.foodchem.2020.126614. [26] S. Benjakul, T.A. Seymour, M.T. Morrissey, A. H., Physicochemical Changes in
[4] Y.Y. Wang, M. Tayyab Rashid, J.K. Yan, H. Ma, Effect of multi-frequency Pacific Whiting Muscle Proteins during Iced Storage, J. Food Sci. 62 (1997) 729-
ultrasound thawing on the structure and rheological properties of myofibrillar 733. 10.1111/j.1365-2621.1997.tb15445.x.
proteins from small yellow croaker, Ultrason. Sonochem. 70 (2021), 105352, [27] Q. Sun, Q. Chen, X. Xia, B. Kong, X. Diao, Effects of ultrasound-assisted freezing at
https://doi.org/10.1016/j.ultsonch.2020.105352. different power levels on the structure and thermal stability of common carp
[5] M. Zhang, F. Li, X. Diao, B. Kong, X. Xia, Moisture migration, microstructure (Cyprinus carpio) proteins, Ultrason. Sonochem. 54 (2019) 311–320, https://doi.
damage and protein structure changes in porcine longissimus muscle as influenced org/10.1016/j.ultsonch.2019.01.026.
by multiple freeze-thaw cycles, Meat Sci. 133 (2017) 10–18, https://doi.org/ [28] G. Jia, H. Liu, S. Nirasawa, H. Liu, Effects of high-voltage electrostatic field
10.1016/j.meatsci.2017.05.019. treatment on the thawing rate and post-thawing quality of frozen rabbit meat,
[6] J.S. Eastridge, B.C. Bowker, Effect of rapid thawing on the meat quality attributes Innovative Food Sci. Emerging Technol. 41 (2017) 348–356, https://doi.org/
of USDA select beef strip loin steaks, J. Food Sci. 76 (2011) S156–S162, https:// 10.1016/j.ifset.2017.04.011.
doi.org/10.1111/j.1750-3841.2010.02037.x. [29] S. Shan, D.R. Heldman, The Influence of Operation Parameters and Product
[7] A. Augustyńska-Prejsnar, M. Ormian, Z. Sokołowicz, Physicochemical and Sensory Properties on Time-to-Temper for Frozen Raw Meat Based on Simulation, Food
Properties of Broiler Chicken Breast Meat Stored Frozen and Thawed Using Various Eng. Rev. 13 (2020) 225–235, https://doi.org/10.1007/s12393-020-09247-8.
Methods, J. Food Qual. 2018 (2018) 1–9, https://doi.org/10.1155/2018/6754070. [30] Q. Sun, B. Kong, S. Liu, O. Zheng, C. Zhang, Ultrasound-assisted thawing
[8] S. Qian, X. Li, H. Wang, W. Mehmood, M. Zhong, C. Zhang, C. Blecker, Effects of accelerates the thawing of common carp (Cyprinus carpio) and improves its muscle
low voltage electrostatic field thawing on the changes in physicochemical quality, LWT–Food Sci. Technol. 141 (2021), 111080, https://doi.org/10.1016/j.
properties of myofibrillar proteins of bovine Longissimus dorsi muscle, J. Food Eng. lwt.2021.111080.
261 (2019) 140–149, https://doi.org/10.1016/j.jfoodeng.2019.06.013. [31] M. Zhang, N. Haili, Q. Chen, X. Xia, B. Kong, Influence of ultrasound-assisted
[9] E.J. Choi, H.W. Park, Y.B. Chung, S.H. Park, J.S. Kim, H.H. Chun, Effect of immersion freezing on the freezing rate and quality of porcine longissimus muscles,
tempering methods on quality changes of pork loin frozen by cryogenic immersion, Meat Sci. 136 (2018) 1–8, https://doi.org/10.1016/j.meatsci.2017.10.005.
Meat Sci. 124 (2017) 69–76, https://doi.org/10.1016/j.meatsci.2016.11.003. [32] H. Kiani, Z. Zhang, D.W. Sun, Experimental analysis and modeling of ultrasound
[10] F. Li, B. Wang, Q. Liu, Q. Chen, H. Zhang, X. Xia, B. Kong, Changes in myofibrillar assisted freezing of potato spheres, Ultrason. Sonochem. 26 (2015) 321–331,
protein gel quality of porcine longissimus muscle induced by its stuctural https://doi.org/10.1016/j.ultsonch.2015.02.015.
modification under different thawing methods, Meat Sci. 147 (2019) 108–115, [33] E. Indergård, I. Tolstorebrov, H. Larsen, T.M. Eikevik, The influence of long-term
https://doi.org/10.1016/j.meatsci.2018.09.003. storage, temperature and type of packaging materials on the quality characteristics
[11] Y. Li, Q.H. Zeng, G. Liu, Z. Peng, Y. Wang, Y. Zhu, H. Liu, Y. Zhao, J. Jing Wang, of frozen farmed Atlantic Salmon (Salmo Salar), Int. J. Refrig. 41 (2014) 27–36,
Effects of ultrasound-assisted basic electrolyzed water (BEW) extraction on https://doi.org/10.1016/j.ijrefrig.2013.05.011.
structural and functional properties of Antarctic krill (Euphausia superba) proteins, [34] D. Liu, L. Liang, W. Xia, J.M. Regenstein, P. Zhou, Biochemical and physical
Ultrason. Sonochem. 71 (2021), 105364, https://doi.org/10.1016/j. changes of grass carp (Ctenopharyngodon idella) fillets stored at -3 and 0 degrees
ultsonch.2020.105364. C, Food Chem. 140 (2013) 105–114, https://doi.org/10.1016/j.
[12] C. Zhang, H. Liu, X. Xia, F. Sun, B. Kong, Effect of ultrasound-assisted immersion foodchem.2013.02.034.
thawing on emulsifying and gelling properties of chicken myofibrillar protein, [35] G. Yi, V. Grabez, M. Bjelanovic, E. Slinde, K. Olsen, O. Langsrud, V.T. Phung,
LWT–Food Sci. Technol. 142 (2021), 111016, https://doi.org/10.1016/j. A. Haug, M. Oostindjer, B. Egelandsdal, Lipid oxidation in minced beef meat with
lwt.2021.111016. added Krebs cycle substrates to stabilise colour, Food Chem. 187 (2015) 563–571,
[13] Y. Tao, P. Wu, Y. Dai, X. Luo, S. Manickam, D. Li, Y. Han, P. Loke Show, Bridge https://doi.org/10.1016/j.foodchem.2015.04.002.
between mass transfer behavior and properties of bubbles under two-stage [36] Z. Guo, X. Ge, L. Yang, G. Ma, J. Ma, Q.L. Yu, L. Han, Ultrasound-assisted thawing
ultrasound-assisted physisorption of polyphenols using macroporous resin, Chem. of frozen white yak meat: Effects on thawing rate, meat quality, nutrients, and
Eng. J. 436 (2022), 135158, https://doi.org/10.1016/j.cej.2022.135158. microstructure, Ultrason. Sonochem. 70 (2021), 105345, https://doi.org/10.1016/
[14] Y. Liu, S. Chen, Y. Pu, A.I. Muhammad, M. Hang, D. Liu, T. Ye, Ultrasound-assisted j.ultsonch.2020.105345.
thawing of mango pulp: Effect on thawing rate, sensory, and nutritional properties, [37] B. Wang, X. Du, B. Kong, Q. Liu, F. Li, N. Pan, X. Xia, D. Zhang, Effect of ultrasound
Food Chem. 286 (2019) 576–583, https://doi.org/10.1016/j. thawing, vacuum thawing, and microwave thawing on gelling properties of protein
foodchem.2019.02.059. from porcine longissimus dorsi, Ultrason. Sonochem. 64 (2020), 104860, https://
[15] T. Ding, Z. Ge, J. Shi, Y.-T. Xu, C.L. Jones, D.-H. Liu, Impact of slightly acidic doi.org/10.1016/j.ultsonch.2019.104860.
electrolyzed water (SAEW) and ultrasound on microbial loads and quality of fresh [38] L. Cai, W. Zhang, A. Cao, M. Cao, J. Li, Effects of ultrasonics combined with far
fruits, LWT–Food Sci Technol. 60 (2015) 1195–1199, https://doi.org/10.1016/j. infrared or microwave thawing on protein denaturation and moisture migration of
lwt.2014.09.012. Sciaenops ocellatus (red drum), Ultrason. Sonochem. 55 (2019) 96–104, https://
[16] X.-F. Cheng, M. Zhang, B. Adhikari, Effects of ultrasound-assisted thawing on the doi.org/10.1016/j.ultsonch.2019.03.017.
quality of edamames [Glycine max (L.) Merrill] frozen using different freezing [39] Y. Shimamura, M. Shinke, M. Hiraishi, Y. Tsuchiya, S. Masuda, The application of
methods, Food Sci. Biotechnol. 23 (2014) 1095–1102, https://doi.org/10.1007/ alkaline and acidic electrolyzed water in the sterilization of chicken breasts and
s10068-014-0150-0. beef liver, Food Sci. Nutr. 4 (2016) 431–440, https://doi.org/10.1002/fsn3.305.
[17] X. Liao, Q. Xiang, P.J. Cullen, Y. Su, S. Chen, X. Ye, D. Liu, T. Ding, Plasma- [40] Y. Zou, K. Zhang, H. Bian, M. Zhang, C. Sun, W. Xu, D. Wang, Rapid tenderizing of
activated water (PAW) and slightly acidic electrolyzed water (SAEW) as beef goose breast muscle based on actomyosin dissociation by low-frequency
thawing media for enhancing microbiological safety, LWT–Food Sci Technol. 117 ultrasonication, Process Biochem. 65 (2018) 115–122, https://doi.org/10.1016/j.
(2020), 108649, https://doi.org/10.1016/j.lwt.2019.108649. procbio.2017.11.010.
[18] F. Forghani, J.H. Park, D.H. Oh, Effect of water hardness on the production and [41] C.K. McDonnell, P. Allen, E. Duggan, J.M. Arimi, E. Casey, G. Duane, J.G. Lyng,
microbicidal efficacy of slightly acidic electrolyzed water, Food Microbiol. 48 The effect of salt and fibre direction on water dynamics, distribution and mobility
(2015) 28–34, https://doi.org/10.1016/j.fm.2014.11.020. in pork muscle: a low field NMR study, Meat Sci. 95 (2013) 51–58, https://doi.org/
[19] D.R. Athayde, D.R.M. Flores, J.S. da Silva, A.L.G. Genro, M.S. Silva, B. Klein, 10.1016/j.meatsci.2013.04.012.
R. Mello, P.C.B. Campagnol, R. Wagner, C.R. de Menezes, J.S. Barin, A.J. Cichoski, [42] X.X. Li, P. Sun, Y. Ma, L. Cai, J.R. Li, Effect of ultrasonic thawing on the water-
Application of electrolyzed water for improving pork meat quality, Food Res. Int. holding capacity, physicochemical properties and structure of frozen tuna
100 (2017) 757–763, https://doi.org/10.1016/j.foodres.2017.08.009. (Thunnus tonggol) myofibrillar proteins, J. Sci. Food Agric. 99 (2019) 5083–5091,
[20] X.-T. Xuan, Y.-F. Fan, J.-G. Ling, Y.-Q. Hu, D.-H. Liu, S.-G. Chen, X.-Q. Ye, T. Ding, https://doi.org/10.1002/jsfa.9752.
Preservation of squid by slightly acidic electrolyzed water ice, Food Control 73
(2017) 1483–1489, https://doi.org/10.1016/j.foodcont.2016.11.013.

9
D. Kong et al. Ultrasonics Sonochemistry 88 (2022) 106105

[43] T. Yin, Y. He, L. Liu, L. Shi, S. Xiong, J. You, Y. Hu, Q. Huang, Structural and [46] X.F. Wu, M. Zhang, B. Adhikari, J. Sun, Recent developments in novel freezing and
biochemical properties of silver carp surimi as affected by comminution method, thawing technologies applied to foods, Crit. Rev. Food Sci. Nutr. 57 (2017)
Food Chem. 287 (2019) 85–92, https://doi.org/10.1016/j.foodchem.2019.02.066. 3620–3631, https://doi.org/10.1080/10408398.2015.1132670.
[44] B. Wang, B. Kong, F. Li, Q. Liu, H. Zhang, X. Xia, Changes in the thermal stability [47] Q. Jiang, R. Jia, N. Nakazawa, Y. Hu, K. Osako, E. Okazaki, Changes in protein
and structure of protein from porcine longissimus dorsi induced by different properties and tissue histology of tuna meat as affected by salting and subsequent
thawing methods, Food Chem. 316 (2020), 126375, https://doi.org/10.1016/j. freezing, Food Chem. 271 (2019) 550–560, https://doi.org/10.1016/j.
foodchem.2020.126375. foodchem.2018.07.219.
[45] N. Jia, L. Wang, J. Shao, D. Liu, B. Kong, Changes in the structural and gel
properties of pork myofibrillar protein induced by catechin modification, Meat Sci.
127 (2017) 45–50, https://doi.org/10.1016/j.meatsci.2017.01.004.

10