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Food Hydrocolloids: Yuying Wang, Anqi Zhang, Xibo Wang, Ning Xu, Lianzhou Jiang
Food Hydrocolloids: Yuying Wang, Anqi Zhang, Xibo Wang, Ning Xu, Lianzhou Jiang
Food Hydrocolloids
journal homepage: http://www.elsevier.com/locate/foodhyd
A R T I C L E I N F O A B S T R A C T
Keywords: For the first time, the irradiation technology combined with Maillard reaction were used to improve the freeze -
Soy protein isolate thaw stability of soybean protein emulsion. The freeze-thaw stability of emulsions prepared with soy protein
Irradiation isolate (SPI), soy protein isolate and maltose mixture (SPI þ M) or glycosylated soy protein isolate with maltose
Maillard reaction
formed by irradiation of 7.5 kGy and 12.5 kGy (named SPI-M7.5 and SPI-M12.5, respectively) was compared.
Emulsion
Freeze-thaw stability
Fourier transform infrared spectroscopy, fluorescence spectroscopy and ultraviolet spectroscopy confirmed the
change of the structure of soy protein isolate, indicating that maltose was covalently linked to soybean protein
isolate. Scanning electron microscopy showed that the modified protein particles were more loose, uniform in
size, and significantly reduced in molecular aggregation than untreated protein. The freeze-thaw stability of SPI,
SPI þ M, and SPI-M7.5 and SPI-M12.5 emulsions was evaluated. It was found that after three freeze-thaw cycles,
the creaming index, oiling off, particle size, coalescence degree and flocculation degree of emulsions prepared
with irradiated SPI samples were all lower than those prepared with SPI and SPI þ M. Zeta potential, laser
confocal and optical microscopy showed that the emulsion was still in a relatively stable state, and the SPI-M7.5
emulsion after freeze-thaw treatment was more stable than the SPI-M12.5 emulsion.
1. Introduction between the free amino group of the amino acid side chain of the protein
molecule and the carbonyl group at the reducing end of the saccharide
Due to its amphiphilic nature, soy protein isolate can be adsorbed at molecule, which belongs to the category of chemical modification,
the oil-water interface, providing electrostatic repulsion and steric namely the protein-saccharide grafting polymerization. It not only re
hindrance between oil droplets to stabilize the emulsion, so it is often tains the surface activity of protein but also has the hydrophilic property
used as an emulsifier (Diftis, Biliaderis, & Kiosseoglou, 2005; Puppo, of saccharide, which is one of the ideal methods for protein modification
Beaumal, & Chapleau, 2008). However, protein-stabilized emulsions are (Dickinson, 1999). Irradiation is an emerging cold treatment method,
susceptible to instability under the influence of external conditions such which can ensure the original flavor of food to the maximum extent, and
as pH, ionic strength, and temperature (Dickinson, 2008; Pongsa has the characteristics of low energy consumption, high efficiency, and
watmanit, Harnsilawat, & Mcclements, 2006). When a little damage to nutrients (Kuan, Bhat, Patras, & Karim, 2013). In 2003,
protein-stabilized emulsion is freeze-thawed, a series of physicochem the Codex Alimentarius Commission stipulated that the irradiation dose
ical changes occur due to the formation of ice crystals. Sharp ice crystals could be could be more than 10 kGy under the condition of ensuring the
will penetrate into the droplets to destroy the interface film, and the integrity, functionality and safety of the food structure, which provided
protein will adsorb onto the ice crystals at the same time, resulting in the guarantee for the application of irradiation technology in the food
insufficient protein adsorption. Further, when the emulsion is thawed, industry (Farkas & Moha �csi-Farkas, 2011). In addition to its application
flocculation, coalescence, unstable oil release, and even complete sep in food sterilization and preservation, irradiation can also change the
aration of the oil phase and the water phase may occur (Gu, Decker, & structure of protein molecules and thus change their functional prop
Mcclements, 2007; Magnusson, Christer Ros� en, & Nilsson, 2011). erties. Research has shown that irradiation changed the conformation of
The glycosylation reaction is mainly based on the carbonyl reaction protein molecules and improved the solubility, emulsifying properties
* Corresponding author. College of Food Science, Northeast Agricultural University, Harbin, 150030, Heilongjiang, China.
** Corresponding author. College of Food Science, Northeast Agricultural University, Harbin, 150030, Heilongjiang, China.
E-mail addresses: [email protected] (Y. Wang), [email protected] (A. Zhang), [email protected] (X. Wang), [email protected] (N. Xu),
[email protected] (L. Jiang).
https://doi.org/10.1016/j.foodhyd.2020.105684
Received 24 July 2019; Received in revised form 10 January 2020; Accepted 16 January 2020
Available online 20 January 2020
0268-005X/© 2020 Elsevier Ltd. All rights reserved.
Y. Wang et al. Food Hydrocolloids 103 (2020) 105684
and foam stability of soybean protein isolate (Pednekar, Das, Rajalaksh, 7.5 kGy, 10 kGy, 12.5 kGy), and the optimal irradiation dose was 7.5
& Sharma, 2010). After irradiation, changes in the structure of peanut kGy. In order to prove that the higher dose would affect the freeze-thaw
protein led to changes in its properties, the protein molecular structure stability of the emulsion, the experimental group with the irradiation
was unfolded, hydrophobic groups were exposed, and various functional dose of 12.5 kGy was added (Wang et al., 2019). The irradiated reaction
properties were improved. However, when the irradiation dose was solution was freeze-dried to prepare the lyophilized powder. The
further increased, the antigenicity of allergenic protein decreased (Luo, lyophilized powder obtained was the glycosylated soy protein isolate
Hu, Gao, Li, Wu, & Yang et al., 2013). It could be seen that the irradi formed by irradiation treatment at 7.5 and 12.5 kGy, which were named
ation mainly caused a series of reactions such as deamination, decar as SPI-M7.5 and SPI-M12.5, respectively.
boxylation, amino acid oxidation, cleavage or reconstitution of disulfide
bonds, degradation or cross-linking of peptide chains. The advanced 2.4. Degree of grafting
structure of protein molecules changed, which influenced on the func
tional characteristics of protein molecules (Kuan et al., 2013; Wihodo & The free amino group was determined by the OPA method (Jiang,
Moraru, 2013). Wang, Wu, & Wang, 2013; Vigo, Malec, Gomez, & Llosa, 1992). After
There are currently few studies on the combination of radiation and dissolving 40 mg of o-phthalaldehyde (OPA) in 1 mL of methanol, the
glycosylation modifications. Due to the influence of irradiation on pro 25 mL of 0.1 mol/L sodium tetraborate, 2.5 mL of 20% (w/v) SDS and
tein structure and properties, it has been gradually developed into a 100 μL β-mercaptoethanol were added, respectively, and then the mixed
modification method (Kuan, Bhat, Patrasn, & Karim, 2013) and glyco solution was diluted to 50 ml with distilled water, which was OPA re
sylation modification is also one of the commonly used methods for agent. During the measurement, 4 mL of OPA reagent was transferred to
protein modification (Zhang et al., 2017). There are few studies on the a test tube, and 200 μL of 5 mg/mL sample solution was injected, mixed
combination of irradiation and glycosylation modification. In this in a vortex mixer, and reacted in a water bath at 35 � C for 2 min. With
experiment, irradiation combined with Maillard reaction was used to distilled water as the blank, the absorbance was read at 340 nm. The
improve the freeze-thaw stability of soybean protein isolate. The struc grafting degree (DG) was calculated as follows:
ture and properties of the modified product were analyzed by Fourier
transform infrared spectroscopy, fluorescence spectroscopy, ultraviolet DG ¼
A1 A2
� 100%
spectroscopy, scanning electron microscopy, emulsification index, oiling A1
off, particle size, flocculation and coalescence, zeta potential, optical
microscopy and laser confocal microscopy. The study will enrich and Where, A1 is the absorbance of the sample before the graft reaction; A2 is
develop the protein modification system, providing a theoretical basis the absorbance of the sample after the graft reaction.
for the application of comprehensive modification technology in food
processing. 2.5. Browning degree
2. Materials and methods A 2 mg/ml sample solution was prepared, and water was used as a
blank control. The absorbance was measured at a wavelength of 420 nm,
2.1. Materials and the degree of browning of soybean glycoprotein was expressed by
absorbance (Kato & Fujimaki, 1968).
Low temperature defatted soy flour (Soybean variety was Nannong
86–4), Shandong Yuwang Company; maltose, Beijing Chemical Reagent 2.6. Fourier transform infrared spectrum (FTIR)
Factory; Jiu San soybean oil, commercially available; all other reagents
were analytically pure. An appropriate amount of sample was mixed with a certain amount
of potassium bromide, ground into powder, and pressed into thin slices
2.2. Preparation of soy protein isolate under the pressure of 20 MPa. Resolution was set at 4 cm 1, and 32 times
of scanning were performed. Then FTIR-8400S Fourier transform
100 g of defatted soy flour was dissolved in 1000 ml of deionized infrared spectrometer was used for full-band (4000-400 cm 1) scanning
water by the magnetic stirring (600 rpm, 2 h, 25 � C) and mixed well. The (Du, Huang, Wang, & Xiao, 2018).
pH of the mixed solution was adjusted to 8.5 with 2 mol/L NaOH, and
the mixed solution was then centrifuged (3170�g, 20 min, 4 � C). The
supernatant was adjusted to pH 4.5 with 2 mol/L HCl, and allowed to 2.7. Fluorescence spectroscopy
stand overnight at 4 � C. The supernatant was discarded and the pellet
was centrifuged (3170�g, 20 min, 4 � C), and washed three times with The sample was dissolved in 0.01 mol/L pH 7.0 sodium phosphate
deionized water. After the precipitate was redissolved, the pH was buffer solution and prepared into a sample solution with a protein
adjusted to 7.0 with 2 mol/L NaOH, and then lyophilized to obtain the concentration of 0.5% (w/v). The excitation wavelength was set at 347
soy protein isolate, and the protein mass fraction was determined to be nm and the scanning range of emission wavelength was 375–550 nm
90.23% by Kjeldahl method (Yu et al., 2018). (Morales & Jim�enez-P�erez, 2001). The sample solution was then diluted
20 times to 0.025% (w/v). The excitation wavelength was set to 290 nm,
2.3. Preparation of irradiated glycosylated soybean protein isolate and the scanning range of emission wavelength was 300–400 nm. Both
excited and emitted slits were 5.0 nm, and the scanning speed was 240
Soy protein isolate (SPI) and maltose (M) were dissolved in 0.01 nm/min (Taboada, Barbosa, Castro, Guti� errez-Pichel, & Mosquera,
mol/L pH 7.0 sodium phosphate buffer at a ratio of 4:1, and stirred at 25 2007).
�
C for 4 h to prepare a solution with a protein concentration of 4%. The
0.02% (w/v) sodium azide was added to the mixture solution to prevent 2.8. UV–visible spectroscopy
microbial growth and to prevent spoilage. The mixture solution was
hydrated overnight in a refrigerator at 4 � C. After the next day, it was The sample was dissolved in 0.01 mol/L pH 7.0 sodium phosphate
taken out and stirred until the liquid temperature reached 25 � C. 100 mL buffer solution to prepare a sample solution with a protein concentration
of the mixture solution was placed in an irradiation apparatus of 60Coγ of 0.02% (w/v), and then subjected to ultraviolet spectrum scanning, the
radiation source to carry out an irradiation treatment. We selected wavelength range was 190–500 nm, and the scanning rate was 100 nm/
irradiation doses according to our previous research (2.5 kGy, 5 kGy, min. The resolution is 0.2 nm (Liang & Tang, 2013).
2
Y. Wang et al. Food Hydrocolloids 103 (2020) 105684
3
Y. Wang et al. Food Hydrocolloids 103 (2020) 105684
B DG
35 0.40
OA
A 0.35
30
0.30
25 a
Degree of grafting(%)
Browning index
0.25
20
0.20
15
0.15
10
0.10
5 0.05
0 0.00
SPI-M7.5 SPI-M12.5
Samples
Fig. 1. Grafting degree and browning index of SPI-M7.5 and SPI-M12.5. Different
letters indicate significant differences between different samples, P < 0.05.
4
Y. Wang et al. Food Hydrocolloids 103 (2020) 105684
Table 1 groups, thereby increasing the contact probability of free amino and
Secondary structure contents of SPI, SPI þ M, SPI-M7.5, and SPI-M12.5. maltose carbonyl groups, and accelerating the Maillard reaction of
Sample α-helix/% β-sheet/% β-turn/% random coil/% protein and saccharide.
c a a Protein spatial structure reflected the aggregation state of protein
SPI 18.87 � 0.21 43.14 � 0.25 17.51 � 0.26 20.48 � 0.56a
SPI þ M 18.79 � 0.18c 43.96 � 0.13b 17.70 � 0.32a 19.55 � 0.58a molecules and played an important role in protein function. Fig. 3
SPI-M7.5 15.77 � 0.06a 43.85 � 0.21b 18.74 � 0.14b 21.64 � 0.10b showed the scanning electron micrograph of SPI, SPI þ M, and SPI-M7.5
SPI-M12.5 16.11 � 0.17b 44.02 � 0.41b 18.39 � 0.02c 21.48 � 0.02c and SPI-M12.5 lyophilized powder at 250 � and 8000 � magnification. It
Note: Different lowercase letters in the same column indicated significant dif could be seen from Fig. 3 that the unmodified SPI particles had compact
ferences (P < 0.05). structure, sharp edges and different sizes. When sugar molecules were
added, the small molecules of sugar tightly surrounded the protein
SPI-M7.5 and SPI-M12.5 had maximum fluorescence intensity at 425 nm molecule to make the structure more compact. The irradiated SPI-M7.5
and 430 nm, respectively. The λmax (Absorption wavelength with and SPI-M12.5 particles were more loose, fuzzy and even uniform. After
maximum absorption peak) shifted to the short wavelength direction, a 8000 times magnification, it was found that SPI-M7.5 and SPI-M12.5 were
blue shift occurred, and the fluorescence intensity of the reaction loose and porous, and the evacuation was uniform and network-like. It
product was higher than SPI, indicating that the Maillard reaction might be because the irradiation promoted the protein structure
occurred. Tryptophan mainly affected the endogenous fluorescence of unfolding (Kuan et al., 2013; Wihodo & Moraru, 2013), the access of the
SPI and was very sensitive to environmental changes, so it reflected the sugar molecule caused the surface of the protein molecule to be covered
conformational changes of proteins faster (Matiacevich & Buera, 2006). with the thick layer of sugar coating, the original rigid structure of the
It could be seen from Fig. 2(c) that when the excitation wavelength was protein molecule disappeared, and the degree of aggregation between
290 nm, the λmax was shifted to the long-wavelength direction of the proteins was significantly reduced.
SPI-M7.5 and SPI-M12.5 compared with SPI, and different degrees of red
shift occurred, indicating that the isolated soy protein and the maltose
underwent a deep Maillard reaction with a decrease in fluorescence 3.3. Creaming index and oiling off analysis of modified products
intensity. It might be that the irradiation caused the protein structure to
open, exposing more chromophores to fluorescence quenching and When the emulsion was frozen, crystallization occurred in the oil and
reducing the fluorescence intensity. water phases. After thawing, the droplets gathered together, and insta
The ultraviolet absorption spectrum of proteins was mainly due to bility phenomena such as droplet coalescence, oil phase separation and
the absorption of ultraviolet light by tryptophan and tyrosine residue sedimentation occurred (Ghosh & Coupland, 2008). Freeze-thaw sta
side chain groups, and the conformational changes of proteins could be bility of emulsion referred to the stability of emulsion during
inferred from the differences in the absorption of ultraviolet spectrum of freeze-thaw process, which was an important property of protein
proteins (Wang, Sun, Pu, & Wei, 2017). It could be seen from Fig. 2(d) emulsion. The creaming index was one of the important indexes of
that the SPI and SPI þ M ultraviolet spectra almost overlapped, showing freeze-thaw stability, the lower the creaming index, the more stable
two characteristic absorption peaks in the range of 220–240 nm and freeze-thaw stability (Xiaodan et al., 2018). It could be seen from Fig. 4
260–280 nm. They were the absorption peaks of peptide bonds and the (a) that the creaming index of both SPI and SPI þ M emulsions increased
absorption peaks of phenylalanine, tryptophan and tyrosine, respec sharply after the freeze-thaw cycles, indicating that the simple addition
tively, indicating that simple mixed sugar did not change the structure of of sugar did not improve the freeze-thaw stability of the emulsion. The
the protein (Yu, Zhao, Hu, Zeng, & Bai, 2012). The absorption peaks of SPI-M7.5 and SPI-M12.5 emulsions had relatively stable creaming index
SPI-M7.5 and SPI-M12.5 at 260–280 nm almost disappeared, indicating after undergoing freeze-thaw cycles, showing good freeze-thaw stabil
that new compounds might be formed, and soy protein isolate and ity. After the emulsion freeze-thaw treatment, the separation of the oil
maltose were already in the state of bonding. The addition of the sugar phase and the water phase occurred due to the difference of density
chain enlarged the spatial structure of the reaction product, resulting in between the fat globule and the continuous phase, and the stability of
weak absorption of tryptophan and tyrosine, and no obvious charac the emulsion was characterized by oiling off (Oliver et al., 2009). Ac
teristic absorption peak. At the same time, the absorption peak at cording to Fig. 4(b), after freeze-thaw cycles, the oiling off of SPI and
220–240 nm was shifted to around 200 nm. The absorption peak was SPI þ M emulsion was significantly increased. Although SPI þ M
blue-shifted, and the absorption intensity was weakened. Irradiation decreased compared with SPI, the overall improvement was not signif
made the protein structure unfold, increasing the content of free amino icant. The emulsions prepared with irradiated SPI samples had lower
oiling off, but SPI-M7.5 emulsion was more stable than SPI-M12.5
Fig. 3. Scanning electron microscopy (SEM) images of SPI (a) (e), SPI þ M (b) (f), SPI-M7.5 (c) (g) and SPI-M12.5 (d) (h). (a–d) at magnification of 250 � , (e–h) at
magnification of 8.00k � .
5
Y. Wang et al. Food Hydrocolloids 103 (2020) 105684
Cycle1 Cycle1
(a) 80 Cycle2 (b) 40 Cycle2
Cycle3 Cycle3
Dc
Dc
Db Cc Cc
Cb
60 30
Da Db
Ca
Cb
Creaming index(%)
Bc
Oiling off(%)
40
Bb
Ba 20
Ab Ac
Aa
Da
Ca Bc
20 10 Ac Bb
Ab Ba
Aa
0 0
SPI SPI+M SPI-M7.5 SPI-M12.5 SPI SPI+M SPI-M7.5 SPI-M12.5
Samples Samples
Fig. 4. Creaming index (a) and oiling off (b) of SPI, SPI þ M, SPI-M7.5 and SPI-M12.5 emulsions after freeze-thaw treatment. Different uppercase letters indicated
significant differences between different samples at the same cycle number and different lowercase letters indicated significant differences between the different
cycles of the same sample, P < 0.05.
emulsion. While the emulsion prepared by SPI-M7.5 and SPI-M12.5 5.8 � 0.2c, 2.3 � 0.3a,
A A
experienced a small increase in particle size after the freeze-thaw cycles,
Cycle 1 SPI 28.8 � 18.6 � 34.0 � 0.6c,B 82.8 � 0.3d,A
and the stability of SPI-M7.5 emulsion was better than that of SPI-M12.5 SPI þ M 0.6d,B 0.2c,B 33.9 � 0.2c,B 81.9 � 0.1c,A
emulsion. Compared with the SPI control group, the volume-weighted of SPI- 16.8 � 16.8 � 20.1 � 0.3a,B 27.3 � 0.6a,A
SPI-M7.5 emulsion decreased by 19.3 μm, 21.2 μm and 43.4 μm after M7.5 0.9c,B 0.8b,B 23.6 � 0.3b,B 28.5 � 0.2b,A
three times freeze-thaw cycles, which was consistent with the results of SPI- 9.5 � 0.2a, 2.9 � 0.3a,
B B
M12.5
the creaming index. The D4,3 was more sensitive to the process of 11.8 � 3.1 � 0.3a,
emulsion droplet aggregation than the D3,2, so the change of D4,3 was 0.2b,B B
used to evaluate the degree of flocculation and coalescence of the Cycle 2 SPI 32.2 � 25.8 � 70.0 � 0.8c,C 100.7 � 0.6d,
emulsion (Fioramonti, Arzeni, Pilosof, Rubiolo, & Santiago, 2015; SPI þ M 0.8d,C 0.3c,C 68.4 � 1.0c,C B
SPI-M emulsions showed the FD of 20.7% and 14.6%, respectively, while 12.7 � 3.3 � 0.6a,
the SPI-M7.5 and SPI-M12.5 emulsions only had the FD of 10.7% and 0.5b,C B
of flocculation and the degree of coalescence increased continuously. SPI- 51.5 � 29.7 � 38.5 � 0.2a,D 130.4 � 0.3c,
After three freeze-thaw cycles, SPI-M7.5 and SPI-M12.5 emulsions still M7.5 1.0c,D 0.4b,D 39.1 � 0.2b,D C
maintained good freeze-thaw stability relative to the control. It might be SPI- 11.0 � 2.7 � 0.2a, 41.6 � 0.4a,C
M12.5 0.5a,C B
43.8 � 0.5b,C
because the irradiation made the tight structure of SPI unfold, the
13.2 � 3.4 � 0.5a,
flexibility was increased, the emulsifying property was improved, the 1.0b,C B
thick adsorption layer could be formed, and the spatial barrier was
Note: a-d represents the significant differences between same freeze-thaw cycles
formed between the droplets, thereby weakening the droplet
of the different samples; A-D represents the significant differences between
flocculation.
different freeze-thaw cycles of the same samples (p < 0.05).
3.5. Potential and microstructure analysis of modified products emulsions, had a similar microstructure. After the freezing-thawing
cycles, SPI and SPI þ M emulsion gradually appeared large and round
Fig. 5 showed the optical microstructures of SPI, SPI þ M, SPI-M7.5 oil droplets and irregular clumps, showing poor freezing-thawing
and SPI-M12.5 initial emulsions and emulsions after three cycles of characteristics. When the emulsion was frozen, the water phase
freeze-thawing. It could be seen that the four initial, unfrozen,
6
Y. Wang et al. Food Hydrocolloids 103 (2020) 105684
Fig. 5. Optical microstructure of SPI, SPI þ M, SPI-M7.5 and SPI-M12.5 emulsions before and after freeze-thaw treatment. The scale bar was 50 μm in length.
Magnification was 400 times.
formed ice crystals puncturing membrane, which caused the fat crystals freeze-thaw stability of emulsions (Kuan, Bhat, & Karim, 2011).
to penetrate each other between the oil droplets, and the oil droplets Laser confocal microscopy could visually represent the particle size,
gathered after thawing (Aoki, Decker, & Mcclements, 2005). The irra dispersion and stability of the emulsion. Fig. 6 showed the laser confocal
diated SPI-M7.5 and SPI-M12.5 emulsions produced only a small amount microstructure of SPI, SPI þ M, SPI-M7.5 and SPI-M12.5 emulsions before
of oil droplets, probably because irradiation promoted the soy protein and after freezing and thawing. The initial emulsions droplet distribu
molecular structure to unfold and increased the Maillard reaction rate tion of the four samples were uniform and the microstructure were not
with maltose. The flexibility of the molecules was increased, and more significantly different. After the freezing-thawing cycles, the oil droplets
hydrophobic groups were exposed at the same time, which enhanced the were observed in SPI and SPI þ M protein emulsions. It might be due to
adsorption of the oil-water interface, so that the protein molecules could the poor solubility of untreated SPI and SPI þ M, and the protein fraction
rapidly develop at the interface to form the solid viscoelastic layer, and could not quickly adsorb to the oil-water interface, and could not form
the interfacial tension was also rapidly reduced, thereby increasing the the thick protective film (Palazolo et al., 2011). Irradiation treatment
Cycle 0
Cycle 3
Fig. 6. Laser confocal microstructure before and after freeze-thaw of SPI, SPI þ M, SPI-M7.5 and SPI-M12.5 emulsions. The scale bar was 50 μm in length. The
excitation wavelength was set to 488 nm.
7
Y. Wang et al. Food Hydrocolloids 103 (2020) 105684
made the soy protein isolate form the complex with maltose. The Cycle 0 Cycle 1 Cycle 2 Cycle 3
emulsion particles of SPI-M7.5 and SPI-M12.5 complex were evenly 0
ZETA/mV
between oil droplets at low temperature state, thereby improving the -20 Cd Cd
freeze-thaw stability of the emulsion. Cc Cc
The potential was an important index for judging the stability of the -25
emulsion. The smaller the dispersed particles, the higher the absolute Cb Bb
Ca Ca Bc
value of the potential, the greater the repulsive force between the par -30 Ab Bb Ac
ticles, and the more stable the system. Moreover, the emulsion with the Aa
Ba Aa Aa
SPI
absolute value of zeta potential exceeding 30 mV was stable, indicating -35 SPI+M
that there was a large electrostatic repulsion between particles (Mar SPI-M7.5
kiewicz, Mrozik, & Rezwan, 2013; Vallar, Houivet, El Fallah, Kervadec, -40
SPI+M12.5
& Haussonne, 1999). In Fig. 7, the initial emulsions prepared from SPI,
SPI þ M, SPI-M7.5, and SPI-M12.5 had potentials of 26.5 mV, 26.6 mV, Fig. 7. Zeta potential of SPI, SPI þ M, SPI-M7.5 and SPI-M12.5 emulsions before
30.2 mV, and 29.4 mV, respectively. As the number of freeze-thaw and after freeze-thaw treatment. Different uppercase letters indicated signifi
cycles increased, the absolute potential value of the emulsion system cant differences between different samples at the same cycle number and
with SPI and SPI þ M mixture decreased gradually, showing instability. different lowercase letters indicated significant differences between the
The absolute values of the irradiated SPI-M7.5 and SPI-M12.5 emulsions different cycles of the same sample, P < 0.05.
remained stable, and the SPI-M7.5 emulsion exhibited better freeze-thaw
stability than the SPI-M12.5 emulsion. The microstructure analysis of the Conceptualization, Writing - review & editing. Ning Xu: Resources.
emulsion also showed that the soy protein emulsion obtained by Mail Lianzhou Jiang: Project administration, Funding acquisition.
lard reaction promoted by irradiation had good freeze-thaw stability.
Acknowledgements
4. Conclusion
This paper was founded by the National Key R&D Program of China
In this paper, the soy protein isolate was modified by irradiation (2018YFD0400600), Heilongjiang Province Key S&T Program
technology and glycosylation technology to improve its freeze-thaw (2019ZX08B01) and National Soybean Industrial Technology System of
stability. Fourier transform infrared spectroscopy, fluorescence spec China (CARS-04-PS28). The authors are grateful to the editors and
troscopy and ultraviolet spectroscopy confirmed the change of the anonymous reviewers for their valuable comments and suggestions.
structure of soy protein isolate, which proved that the soy protein isolate
reacted with maltose. The freeze-thaw stability of SPI, SPI þ M, SPI-M7.5 References
and SPI-M12.5 emulsions was evaluated by creaming index, oiling off,
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Declaration of competing interest
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