Food Bioscience 27 (2019) 1–5

Contents lists available at ScienceDirect

Food Bioscience
journal homepage: www.elsevier.com/locate/fbio

Effect of ultrasonication time on the functional properties of giant squid T

(Dosidicus gigas) mantle protein concentrate
S. Valdez-Hurtadoa, L.S. López-Bermúdezb, O.A. Higuera-Barrazab, C.L. Del Toro-Sanchezb,
S. Ruiz-Cruzc, M.G. Suárez-Jiménezb, E. Marquez-Riosb,
⁎

a
Universidad Estatal de Sonora, Navojoa, Sonora, Mexico
b
Departamento de Investigación y Posgrado en Alimentos, Universidad de Sonora, 83000 Hermosillo, Sonora, Mexico
c
Departamento de Biotecnología y Ciencias Alimentarias, Instituto Tecnológico de Sonora, 85000 Obregón, Sonora, Mexico

ARTICLE INFO ABSTRACT

Keywords: The giant squid (Dosidicus gigas) might be used as a raw material for a protein concentrate. However, it has been
Gelling observed that colloidal systems formed from squid proteins have limited functionality. Therefore, several in-
Foams vestigations have been done to improve the functional properties of squid proteins. Recently ultrasound has been
Emulsions considered a technology for improving the functional properties of proteins. For this reason and considering that
Sonication time
jumbo squid is an important fishery in northwest Mexico, the purpose of this research was to determine the effect
Giant squid
of sonication time on the main functional properties of proteins. Sonication at 20 kHz and 20% amplitude were
Dosidicus gigas
used during 0, 30, 60, and 90 s for foam and emulsion evaluations, and for 0, 1, and 3 min to evaluate gelling
capacity. The emulsifying activity index was the highest at 60 s, while the emulsion stability index was the best
at 90 s. Foaming capacity was significantly higher at 60 and 90 s, while the foam stability was 100% for all
treatments. Finally, the water holding capacity and the texture profile analysis of gels showed an improvement.

1. Introduction Recently, sonication has been used to improve the functional

Giant squid (Dosidicus gigas) is one of the most abundant and large
squid species found in the pelagic zone of the eastern Pacific Ocean,
from Chile to the Oregon coasts (Tolano-Villaverde et al., 2018). The
commercial appeal of this species lies in its great abundance, low cost,
and high yield (~ 75%) after evisceration; in addition, its low-fat con-
tent as well as the tastelessness and whiteness of its meat make it
commercially attractive (Encinas-Arzate et al., 2014). Due to the
overexploitation of the traditional sources for surimi production and
the inherent characteristic of squid muscle, this species has been con-
sidered a possible alternative for producing protein concentrates or
surimi. This could generate value added products, which could be used
in the formation of foams, emulsions, and gels, as well as a food in-
gredient. Some studies have evaluated the gelling, foaming, and
emulsifying properties of giant squid proteins (Dihort-Garcia et al.,
2011; Lopez-Enriquez, Ocano-Higuera, Torres-Arreola, Ezquerra-
Brauer, & Marquez-Rios, 2015; Tolano-Villaverde et al., 2013), showing
that they have appropriate functional properties but are not as good
when compared with fish species. This has led to the assumption that
the cause of the weak gels obtained from this species is due to the in-
trinsic properties of the myofibrillar proteins.
properties of proteins (Higuera-Barraza, Del Toro-Sanchez, Ruiz-Cruz,
& Márquez-Ríos, 2016). Different frequency ranges can be used but
frequencies above the threshold of human hearing (> 16 kHz) are
commonly used (Mirmoghtadaie, Shojaee, & Marzieh, 2016). Sonica-
tion can be classified into two categories: low intensity (1 W/cm2) with
5–10 MHz frequency and high intensity (10–1000 W/cm2) with
20–100 kHz frequency (Higuera-Barraza et al., 2016). It is known that
sonication promotes cavitation, which consists in the formation,
growth, and collapse of air bubbles. This phenomenon is related to
heating, dynamic agitation, shear stress, and turbulence (Knorr, Zenker,
Heinz, & Lee, 2004; O`Donnelle, Tiwari, Bourke, & Cullen, 2010). The
waves create regions of high and low pressure; this variation of acoustic
pressure is directly proportional to the amount of energy applied to the
system. Nevertheless, sonication has not been used to improve the
functional properties (foam, emulsion, and gelling properties) of pro-
tein from giant squid. Therefore, this study evaluates the effect of so-
nication time on the main functional properties of proteins. Sonication
at 20 kHz and 20% amplitude were used at different times for the
evaluation of foams, emulsions, and gelling capacity, with the aim of
improving these functional properties.

⁎
Corresponding author.
E-mail address: enrique.marquez@unison.mx (E. Marquez-Rios).

https://doi.org/10.1016/j.fbio.2018.11.003
Received 11 January 2018; Received in revised form 24 October 2018; Accepted 4 November 2018
Available online 13 November 2018
2212-4292/ © 2018 Elsevier Ltd. All rights reserved.
S. Valdez-Hurtado et al.
2. Materials and methods
2.1. Raw materials
Frozen (− 20 °C) jumbo squid (Dosidicus gigas) were commercially
obtained at a local fish market (Fish Market Alvarez, Hermosillo,
Sonora, México). Specimens had an average weight and length of
9.5 ± 0.2 kg and 79 ± 2 cm, respectively. The mantles (experimental
samples) were placed in plastic bags and stored at the Laboratory of
Conservation and Processing of Marine Products, University of Sonora,
Sonora, Mexico, and stored at − 20 °C until use (Tolano-Villaverde
et al., 2013), a maximum of 4 wk.
2.2. Preparation of the protein concentrate
Frozen squid mantles were thawed at 4–5 °C for 12 h. Each mantle
was considered as a repetition of the experiment; therefore, the com-
plete mantle was chopped into small pieces using a knife, and mixed
with cold distilled water (≤ 4 °C) with a mantle-to-water ratio of 1:3.
The mixture was then homogenized at 1000 rpm for 2 min using a tissue
homogenizer (Wisd, WiseTis HG-15D, Witeg, Germany). The homo-
genate was centrifuged at 12,000 × g for 20 min at 4 °C (Thermo
Scientific, Sorvall Biofuge Stratos, Hanau, Germany). The supernatant
was discarded and the precipitate, regarded as the protein concentrate
(insoluble protein). This was analyzed for protein using the method of
Lowry, Rosebrough, Farr, and Randall (1951) using bovine serum al-
bumin (BSA) as the standard assuming it to be 100% pure. (The protein
content in the insoluble protein was 12 ± 4%).
2.3. Sonication treatment
The sonication equipment with a 0.636 cm diameter titanium probe
(Digital Sonifier 250; Branson, México) was used at 20 kHz and 20%
amplitude (17 W). For emulsion and foam experiments, the protein
concentration was adjusted to 5 mg/mL. Then, 20 mL of protein solu-
tions were sonicated for 0, 30, 60, and 90 s. While, for gelling capacity
studies, 80 mL of homogenate at a ratio of 1:3 (mantle:water) were
sonicated for 0, 1, and 3 min. During the sonication, samples were
maintained in an ice bath and the temperature was maintained within
the range of 0–3 °C.
2.4. Functional properties
2.4.1. Emulsifying activity index (EAI) and emulsion stability index (ESI)
The emulsifying activity index (EAI) and emulsion stability index
(ESI) were determined using the turbidimetry technique of Pearce and
Kinsella (1978). The protein concentration used was 5 mg/mL, which
was mixed with canola oil at a ratio of 1:1 in a final volume of 10 mL
and homogenized at 12,000 rpm for 1 min, using the tissue homo-
genizer. After 1 min the emulsion was formed. The EAI was evaluated
by taking an aliquot of 100 μL from the aqueous layer and diluted 1:40
with 0.1% of sodium dodecyl sulfate (SDS). The absorbance of the re-
sulting solution was measured at 500 nm using a spectrophotometer
(Cary 50; Varian, Walnut Creek, CA, USA). EAI was calculated using the
following equations:
2.303 × A500 × F
=
l strength, fracture, cohesiveness, and elasticity (Tolano-Villaverde
2
EAI (m2g 1) =
C
where τ is the turbidity, A500 is the absorbance at 500 nm, F is the
dilution factor (40), l is the length of the light path (1 cm). The volume
fractions of oil emulsions (φ) were 0.5, C is the protein concentration in
mg/mL.
The ESI was determined 10 min after the formation of the emulsion
2
Food Bioscience 27 (2019) 1–5
(10 mL aliquots of the fresh emulsions were taken and stored); 100 μL
were taken from the lower layer and the determination was done in the
same manner as that of the EAI. The results were determined using the
following equation:
× t
ESI (mm) =
t
2.4.2. Foaming capacity (FC) and foam stability (FS)
Foaming capacity (FC) was determined using the method of
Coffman and Garcia (1977). A total of 50 mL of 1% (w/v) protein so-
lution was used. The solution was mixed at high speed for 2 min in a
domestic blender (Osterizer, Sunbeam Corp. Ltd., Toronto, Ont, Ca-
nada). Next, it was immediately poured into a graduated cylinder. FC
was calculated by measuring foam volume at zero time. Foam stability
(FS) was evaluated by monitoring foam volume after 60 min. FC and FS
were calculated using the following equations:
% Foaming capacity
vol. after homogenization–vol. before homogenization
= × 100
vol. before homogenization
foam volume after time(t)
%Foaming stability = × 100
initial from volume
2.4.3. Gel-forming ability (GFA)
2.4.3.1. Gel preparation. Sols from each protein concentrate were
prepared by adding 2.5 g NaCl/100 g to obtain a moisture and
protein content of 86.0% and 11.5%, respectively. This mixture was
homogenized for two min at short intervals in a Cuisinart Food
Processor (Model DLC-8 Plus; Cuisinart, Greenwich, CT, USA). Each
sol was packed into a Petri dish (1 cm in height) and vacuum-sealed in
moisture/vapor-proof film bags (Cryovac Corp., Duncan, SC, USA) with
a Smith Supervac Vacuum Machine (Smith Equipment Co., Clifton, NJ,
USA). Then, the sols were heat-set in a water bath at 90 °C for 30 min.
Heat-set gels were immediately chilled at 5–10 °C in an ice-water
mixture and maintained at 2‒4 °C overnight, prior to functional
evaluation.
2.4.3.2. Water holding capacity (WHC). The WHC was measured using
the methodology used by Jiang, Ho, and Lee (1985). A 5 g portion of
each gel was centrifuged in the refrigerated centrifuge at 3000 × g for
20 min at 4 °C. The WHC was estimated as g of water retained/g of
protein without accounting for any protein lost in the supernatant. The
weight of the pellet corrected for the 1 g of protein was used as the
amount of water.
2.4.3.3. Texture profile analysis (TPA). The gels were tempered for
60 min at room temperature (25 °C) prior to analysis. The TPA was done
on uniform cylindrical shaped samples (1 cm diameter and 1 cm
height), which were obtained with a small plastic cylinder, and with
the help of a calibrator vernier, with a minimum resolution of 0.05 mm
(Dihort-Garcia et al., 2011). Texture was measured using a TA.XT2 Plus
Texturometer (Food Technology Corp., Sterling, VA, USA) with a
3.8 cm diameter compression plunger (attached to a 100 N load cell)
at a speed of 1 mm/s. A double compression test at 75% of the original
gel sample height was used to obtain compression hardness, gel
et al., 2013) using the software provided with the instrument. Every
test was replicated a minimum of 4 times and mean values for each
parameter were calculated. Hardness was defined as the maximum
force during the first compression; gel strength, as the area under the
curve during the first compression (from zero distance to the point of
maximum hardness); fracture, as the force at which a fracture occurs
during the first compression; cohesiveness, as the area of work during
the second compression divided by the area of work during the first
S. Valdez-Hurtado et al.
compression; and elasticity, as the distance of the height (even if the
sample had broken apart) during the second compression divided by
the original compression distance (Bourne, 1978).
2.5. Statistical analysis
The experiment was done three times (n = 3) and each determina-
tion was done in triplicate. Data analysis was carried out using the JMP
ver. 5.0.1 software (SAS Institute, Chicago, IL, USA). Descriptive sta-
tistics (mean and standard deviation, SD) and one-way analysis of
variance (ANOVA) were done to determine differences among treat-
ments. Variance analysis was done using Tukey-Kramer using a 5%
significance level (Cochran & Cox, 1992).
3. Results and discussion
3.1. Emulsifying activity index (EAI)
The EAI is related to the surface area stabilized by the protein. This
represents the ability of proteins to be absorbed at the interface of fat
globules and the aqueous phase (Pearce & Kinsella, 1978). The effect of
sonication time on the EAI is shown in Fig. 1. A significant increase
(p < 0.05) was found with increasing sonication time, with the 60 s
treatment showing the highest value. Similar results have been reported
by Yanjun et al. (2014), who evaluated the sonication effect on the
functional properties of the proteins of a reconstituted milk protein
concentrate (MPC). These researchers used sonication (12.5 ± 0.3 W
and 50% amplitude) at different times (0.5, 1, 2, and 5 min), reporting
that EAI increased significantly as sonication time increased. The in-
crease of EAI in the present experiment could be attributed to possible
conformational changes in the structure of the proteins, due to dena-
turation and polydispersity, increasing surface hydrophobicity and
molecular flexibility, which leads to an increase in solubility, affecting
the adsorption of protein molecules at the oil-water interface
(Guilmineau & Kulozik, 2007). However, the EAI after 90 s of sonica-
tion was significantly reduced. This suggests that treatments > 60 s are
unfavorable. Similar results have been reported by Qiu-Ting et al.
(2014) with peanut protein isolate using ultrasound at different level of
power from 0 to 30 min who found better EAI at 2 than 3 min.
3.2. Emulsion stability index (ESI)
The ESI provides a measure of the stability of the emulsion over
time; it reflects the protein's ability to interact with the oil-water
Fig. 1. Effect of sonication on the emulsifying activity index (EAI) of giant
squid mantle concentrate (Dosidicus gigas). Data shows the mean ± standard
deviation (n = 3). Different letters on the bars indicate significant differences
(p < 0.05).
3
Food Bioscience 27 (2019) 1–5
Fig. 2. Effect of sonication on the emulsion stability index (ESI) of giant squid
mantle concentrate (Dosidicus gigas). Data shows the mean ± standard devia-
tion (n = 3). Different letters on the bars indicate significant differences
(p < 0.05).
interface after the emulsion is stored or heated (Higuera-Barraza et al.,
2016). Generally, emulsion instability comes from insufficient surfac-
tant to cover the interface created (Dalgleish, 1997).
The ESI was significantly different (p < 0.05) at 90 s, as seen in
Fig. 2. The ESI value obtained for the giant squid protein concentrate
(Dosidicus gigas) without being sonicated (control) was significantly
less. Similar results have been reported by Yanjun et al. (2014), who
evaluated the effect of sonication on the ESI of the proteins of a re-
constituted milk protein concentrate (MPC) (5%). These researchers
reported that ESI increased at up to 1 min of sonication, but subse-
quently decreased when the time was prolonged. On the other hand,
Zhang et al. (2014) evaluated the sonication effect (600 W at 20 °C) on
the ESI of a peanut protein isolate at different times, which increased
significantly (p < 0.05) after 1 min of sonication. This increase could
be explained by a more favorable orientation of the proteins, resulting
from the turbulent effect (cavitation) of the sonication, integrating the
proteins at the interface of the oil droplets. However, after 1 min there
is a decrease in ESI, possibly due to the aggregation of the proteins,
promoting the phase separation of the emulsion.
3.3. Foaming capacity (FC)
The FC of a protein at the interfacial area is affected by the rate of
adsorption, flexibility, and hydrophobicity (Damodaran, 2008). This
determination is based on the relationship between the foam volume
formed (after the protein solution was mixed) and the final volume of
the solution (Singh, Benjakul, & Kijroongrojana, 2018). The effect of
sonication time on the FC is shown in Fig. 3. The FC increased slightly
(p < 0.05) as sonication time increased, with the highest FC found
with the 60 and 90 s treatments. This increase in FC could be the result
of the partial denaturation of the proteins. Similar results have been
reported by Jambrak, Mason, Lelas, Herceg, and Herceg (2008), who
evaluated the effect of sonication on the foaming properties of whey
protein, using whey protein concentrate (WPC), whey protein isolate
(WPI), and whey hydrolyzed protein (WPH), all at 10% (w/v). These
protein systems were sonicated (20 kHz) for 15 and 30 min, resulting in
high FC in the three protein systems. In another study, Morales,
Martínez, Ruiz-Henestrosa, and Pilosof (2015), studying soy protein,
evaluated the effect of sonication (20 kHz at 20% amplitude) for dif-
ferent times (5, 10, 15, and 20 min). They found that the FC of soy
protein without treatment was 153%, which significantly increased
when the treatment time increased; during the first 5 and 20 min of
treatment, the FC increased by 62% and 75%, respectively. This was
attributed to a partial denaturation of the protein, increasing its flex-
ibility and hydrophobicity due to cavitation (Jambrak et al., 2008).
S. Valdez-Hurtado et al. Food Bioscience 27 (2019) 1–5

Table 1
Effect of sonication on the WHC and TPA of gels obtained from giant squid
(Dosidicus gigas) mantle protein concentrate.
Time of sonication (min)

Parameter 0 1 3

WHC (g H2O/g protein) 10.7 ± 0.4b 13 ± 1b 22 ± 2a

Gel strength (N × cm/g protein) 37 ± 1b 30 ± 1c 49 ± 5a
Hardness (N/g protein) 0.56 ± 0.0ab 0.50 ± 0.0b 0.62 ± 0.1a
Elasticity 0.67 ± 0.1b 0.78 ± 0.1ab 0.85 ± 0.0a
Cohesiveness 0.25 ± 0.0b 0.24 ± 0.0b 0.52 ± 0.0a

Different letters in the same row indicate significant differences (p < 0.05).

adequate balance between flexibility and rigidity, probably due to the

Fig. 3. Effect of sonication on the foaming capacity (FC) of giant squid mantle
protein concentrate (Dosidicus gigas). Data shows the mean ± standard devia-
tion (n = 3). Different letters on the bars indicate significant differences
(p < 0.05).
partial denaturation of the protein induced by the sonication, allowing
the formation of cohesive interactions in the interface (Damodaran,
2008)
3.5. Gel forming ability (GFA)

3.4. Foam stability (FS)
FS depends of the proteins ability to stabilize a foam against me-
chanical or gravitational stresses (Damodaran, 2008); FS depends on
the protein to form a strong, flexible, and cohesive film, to reduce gas
permeability and inhibit bubble coalescence (Dickinson, 1997). The
application of high frequency ultrasound did not show a significant
effect (p ≥ 0.05) since FS was maintained at 100% in all treatments
(Fig. 4). This suggested that the foams obtained with squid mantle
proteins have excellent stability. On the other hand, it also suggested
that sonication does not affect the stability that these proteins already
have. Similar results were reported by Morales et al. (2015), who
evaluated the sonication effect (20 kHz at 20% amplitude) on soybean
protein for different times (5, 10, 15, and 20 min), finding that FS was
not affected by treatment (p ≥ 0.05). In another study, Jambrak et al.
(2008) evaluated the sonication effect on the foaming properties WPC,
WPI, WPH, all at 10% (w/v). These protein systems were sonicated
(20 kHz) for 15 and 30 min, resulting in high FS in the three protein
systems. This could be attributed to increased flexibility and surface
activity on the interface, which can produce proteins more capable of
stabilizing foams. Based on the results of FC and FS, the squid protein
showed good foaming ability and foaming stabilization, thus having an
Myosin is the main myofibrillar protein responsible for functional
properties such as gelation, as it contributes to water holding capacity
(WHC), gel hardness, cohesiveness, and elasticity, among other prop-
erties (Encinas-Arzate et al., 2014). Thus, the effect of sonication time
on the gelling ability of the proteins was evaluated by determining the
WHC and the TPA.
3.5.1. WHC
After sonication, thermal gelation was carried out, and the WHC of
the gels was measured. Significant differences (p < 0.05) were ob-
tained in the WHC (Table 1). Samples that were sonicated for 3 min
showed the highest value. This could be attributed to the partial un-
folding of the protein, which favors the formation of a better-structured
network during the gelation process. Therefore, giving a greater ex-
posure of polar amino acid side chains, which could interact more ea-
sily with water. Normally, this functional property is increased as
protein increases and it is related to greater protein water interactions
(Tolano-Villaverde, Torres-Arreola, Ocaño-Higuera, & Marquez-Rios,
2016). Similar results were reported by Li, Kang, Zhao, Xu, and Zhou
(2014), who evaluated the sonication effect (20 kHz at 60% amplitude)
and pulsation time (0, 3, and 6 min) on prepared chicken breast sus-
pensions, at 7.5% protein. These investigators found a significant in-
crease in WHC when 3 and 6 min of sonication were used.

3.5.2. Texture profile analysis (TPA)

Fig. 4. Effect of sonication on the foam stability (FS) of giant squid mantle
protein concentrate (Dosidicus gigas). Data shows the mean ± standard devia-
tion (n = 3). Different letters on the bars indicate significant differences
(p < 0.05).
Table 1 shows the TPA parameters, showing a significant effect
(p < 0.05) on all parameters evaluated. None of the three systems
showed fracture, and the parameters evaluated were improved due to
sonication. Gel strength and hardness increased 32% and 10%, re-
spectively, the former is an important attribute of gels. On the other
hand, elasticity and cohesiveness increased 27% and 108%, respec-
tively. Similar results were obtained by Li et al. (2014), who reported
significant differences (p < 0.05) after the application of high fre-
quency ultrasound for 3 min, increasing the gel strength of chicken
breast suspensions. The results obtained suggested that the unfolding of
proteins caused by sonication improves the gelling property of squid
proteins. An increase of hardness and gel strength are indicative of a
better consistency of the gelled product, while the increase in elasticity
and cohesiveness suggested that the gel was more stable, tending to
retain its structure during the compression processes, which is intended
to simulate biting or chewing. This could be due to an increase of
crosslinks in the protein network, resulting in harder, more elastic, and
cohesive gels.

4
S. Valdez-Hurtado et al.
4. Conclusion
It was found that application of sonication (20 kHz) affected the
functional properties of the protein concentrate obtained from squid
mantle. However, in relation to the foam stability, there were no sig-
nificant differences due to sonication, showing that the proteins of the
giant squid alone have good foam stability. On the other hand, it was
observed that sonication time comprises an important variable, which
must be established to obtain desirable results depending on the func-
tional property being studied. This study showed that the application of
ultrasound can be a good alternative to improve the functional prop-
erties of giant squid mantle proteins, thus providing new options to add
value. Nevertheless, it may be beneficial to learn more about the
structural changes caused by ultrasonication with the aim of explaining
at the structural level the improved functional properties.
Acknowledgements
The authors of this research thank the University of Sonora, espe-
cially the Departamento de Investigación y Posgrado en Alimentos for
providing their facilities to carry out the thesis of López-Bermúdez LS
(second author). The authors acknowledge the support of Consejo
Nacional de Ciencia y Tecnología through Project 222150.
Conflict of interest
The authors confirm that they have no conflicts of interest with
respect to the work described in this manuscript.
References
Bourne, M. C. (1978). Texture profile analysis. Food Technology, 32, 62–66.
Cochran, W. G., & Cox, G. M. (1992). Experimental designs (2nd ed.). New York, NY, USA:
John Wiley & Sons (ISBN: 978-0-471-54567-5).
Coffman, C. W., & Garcia, V. V. (1977). Functional properties and amino acid content of
protein isolate from mung bean flour. Journal of Food Technology, 12, 473–484.
Dalgleish, D. G. (1997). Adsorption of protein and the stability of emulsions. Trends in
Food Science & Technology, 8, 1–6.
Damodaran, S. (2008). Amino acids, peptides, and proteins. In S. Damodaran, K. L.
Parkin, & O. R. Fennema (Eds.). Food chemistry (pp. 322–425). New York, NY, USA:
Dekker.
Dickinson, E. (1997). Properties of emulsion stabilized with milk proteins: Overview of
some recent developments. Journal of Dairy Science, 80, 2607–2619.
Dihort-Garcia, G., Ocano-Higuera, V. M., Ezquerra-Brauer, J. M., Lugo-Sanchez, M. E.,
Pacheco-Aguilar, R., Barrales-Heredia, S. M., & Marquez-Rios, E. (2011). Production
and functional evaluation of a protein concentrate from giant squid (Dosidicus gigas)
obtained by alkaline dissolution. CyTA-Journal of Food, 9, 171–179.
Encinas-Arzate, J. J., Ezquerra-Brauer, J. M., OcañoHiguera, V. M., Ramirez-Wong, B.,
Food Bioscience 27 (2019) 1–5
Armenta-Villegas, L., Torres-Arreola, W., & Marquez-Rios, E. (2014). Effect of ionic
strength on soluble protein removal from giant squid mantle (Dosidicus gigas) and
functional evaluation of protein recovery. Food Science and Technology, 23, 401–407.
Guilmineau, F., & Kulozik, U. (2007). Influence of thermal treatment on the functionally
of hens egg yolk in mayonnaise. Journal of Food Engineering, 78, 648–654.
Higuera-Barraza, O. A., Del Toro-Sanchez, C. L., Ruiz-Cruz, S., & Márquez-Ríos, E. (2016).
Effects of high-energy ultrasound on the functional properties of proteins. Ultrasonics
Sonochemistry, 31, 558–562.
Jambrak, A. R., Mason, T. J., Lelas, V., Herceg, Z., & Herceg, I. L. (2008). Effect of ul-
trasound treatment on solubility and foaming properties of whey protein suspensions.
Journal of Food Engineering, 86, 281–287.
Jiang, S. T., Ho, M. L., & Lee, T. C. (1985). Optimization of the freezing conditions on
mackerel and amberfish for manufacturing minced fish. Journal of Food Science, 50,
727–732.
Knorr, D., Zenker, M., Heinz, V., & Lee, D. (2004). Applications and potential of ultra-
sonics in food processing. Trends in Food Science & Technology, 15(5), 261–266.
Li, K., Kang, Z. L., Zhao, Y. Y., Xu, X. L., & Zhou, G. H. (2014). Use of high-intensity
ultrasound to improve functional properties of batter suspensions prepared from PSE-
like chicken breast meat. Food and Bioprocess Technology, 7, 3466–3477.
Lopez-Enriquez, R. L., Ocano-Higuera, V. M., Torres-Arreola, W., Ezquerra-Brauer, J. M.,
& Marquez-Rios, E. (2015). Chemical and functional characterization of sarcoplasmic
proteins from giant squid (Dosidicus gigas) mantle. Journal of Chemistry, 1–10.
Lowry, O. H., Rosebrough, N. J., Farr, A. L., & Randall, R. J. (1951). Protein measurement
with the folin phenol reagent. Journal of Biological Chemistry, 193, 265–275.
Mirmoghtadaie, L., Shojaee, A. S., & Marzieh, H. S. (2016). Recent approaches in physical
modification of protein functionality. Food Chemistry, 199, 619–627.
Morales, R., Martínez, K. D., Ruiz-Henestrosa, V. M. P., & Pilosof, A. M. (2015).
Modification of foaming properties of soy protein isolate by high ultrasound in-
tensity: Particle size effect. Ultrasonics Sonochemistry, 26, 48–55.
O`Donnelle, C. P., Tiwari, B. K., Bourke, P., & Cullen, P. J. (2010). Effect of ultrasonic
processing on food enzymes of industrial importance. Trends in Food Science &
Technology, 21, 358–367.
Pearce, K. N., & Kinsella, J. E. (1978). Emulsifying properties of proteins: Evaluation of a
turbidimetric technique. Journal of Agricultural and Food Chemistry, 26, 716–723.
Qiu-Ting, Z., Zong-Cai, T., Hui, X., Hui, W., Xiao-Qin, H., Guang-Xian, L., ... (2014).
Influence of ultrasonic treatment on the structure and emulsifying properties of
peanut protein isolate. Food and Bioproducts Processing, 92, 30–37.
Singh, A., Benjakul, S., & Kijroongrojana, K. (2018). Effect of ultrasonication on physi-
cochemical and foaming properties of squid ovary powder. Food Hydrocolloids, 77,
286–296.
Tolano-Villaverde, I. J., Ezquerra-Brauer, J. M., Ocano-Higuera, V. M., Ramirez-Wong, B.,
Armenta-Villegas, L., Herrera-Urbina, R., & Marquez-Rios, E. (2013). A jumbo squid
(Dosidicus gigas) protein concentrate obtained by alkaline dissolution and its con-
formational changes evaluation. Food Science and Technology Research, 19, 601–608.
Tolano-Villaverde, I. J., Ocaño-Higuera, V. M., Ezquerra-Brauer, J. M., Santos-Sauceda, I.,
Santacruz-Ortega, H., Cardenas-Lopez, J. L., ... Marquez-Rios, E. (2018).
Physicochemical characterization of actomyosin-paramyosin from giant squid mantle
(Dosidicus gigas). Journal of the Science of Food and Agriculture, 98, 1787–1793.
Tolano-Villaverde, I. J., Torres-Arreola, W., Ocaño-Higuera, V. M., & Marquez-Rios, E.
(2016). Thermal gelation of myofibrillar proteins from aquatic organisms. CyTA-
Journal of Food, 14, 502–508.
Yanjun, S., Jianhang, C., Shuwen, Z., Hongjuan, L., Jing, L., Lu, L., & Jiaping, L. (2014).
Effect of power ultrasound pre-treatment on the physical and functional properties of
reconstituted milk protein concentrate. Journal of Food Engineering, 124, 11–18.
Zhang, Q. T., Tu, Z. C., Xiao, H., Wang, H., Huang, X. Q., Liu, G. X., & Lin, D. R. (2014).
Influence of ultrasonic treatment on the structure and emulsifying properties of
peanut protein isolate. Food and Bioproducts Processing, 92, 30–37.