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New Advances in Antifreeze Peptides∣ Professor Wang Shaoyun, Fuzhou University: Research and application of 3D structure of antifreeze polypeptide surimi

 Last Update: 2022-11-26
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Abstract analyzes the effect of freeze-thaw (F-T) cycling on the shape retention of
3D structure of surimi ink (ASI) based on antifreeze polypeptides.
The results show that the ASI 3D structure has good shape retention ability, and its width, height, weight and water holding capacity are 22.
42 mm, 21.
07 mm, 9.
99 g and 68.
30%,
respectively, even after F-T 4 times.
The average area of ice crystals in the ASI 3D structure was only 0.
001 mm2 to 0.
015^mm2, and the equivalent diameter was expanded from 0.
040 mm to 0.
139 mm
.
The α-helix and β-fold of myofibrillar protein in the ASI 3D structure decreased slightly from (44.
16±0.
98)% to (33.
33±0.
92)%, (18.
28±4.
45)% to (24.
43±1.
60)%, respectively
.
The interaction of chemical bonds and proteins has changed
to some extent.
AFPs prevent deformation and juice loss
of surimi 3D structures after F-T.
These results provide theoretical guidance
for maintaining frozen 3D food structures.
IntroductionAs a rapidly developing new technology, 3D printing has been widely used in the food field
due to the advantages of customization possibilities, personalized nutrition, easier swallowing, the use of plant "meat" and real meat, reduced food waste, unconventional food consumption and space travel.
At present, meat-based ink in 3D printing has become one of
the most prominent research hotspots.
This is because it can replace traditional kitchen processing methods, and 3D printing fish, chicken, beef, cultured meat, etc.
has practical application value
.
3D printed meat is rich in protein and water, and is prone to deterioration due to microbial growth at room temperature
.
With the maturity of 3D printing technology using meat-based inks, the storage problem of 3D printed meat (prepared dishes) is becoming a bottleneck
.
Cryopreservation technology is widely used
because of its inhibitory effect on microbial reproduction.
However, freeze-thaw (F-T) cycling is inevitable during the storage and transportation of 3D printed meat, which can lead to severe frostbite and loss of juice as well as the ability to
maintain shape.
This greatly limits the development of
3D printing technology.
Therefore, it is very urgent to prevent and solve the problem of 3D printed meat from declining shape retention during frozen storage
.
Silver carp is a freshwater fish
that is widely distributed around the world.
It is popular
with consumers for its delicious taste and high nutritional value.
Favored by customers for its taste and nutrition, silver carp derived products are becoming an indispensable daily nutrient
.
Obviously, silver carp as a raw material for 3D printing is commercially promising
.
Antifreeze peptides (AFPs), which prevent ice crystal growth and recrystallization, have become effective antifreeze agents for frozen foods such as frozen vegetables, frozen meat, and ice cream
.
In our previous study, AFPs were screened out from foodborne proteins by enzymatic hydrolysis, which protects surimi proteins from freeze destruction
.
Therefore, it is of great significance to prepare the 3D structure of surimi based on AFPs and study the retention of
its 3D structure after F-T.

This study aimed to analyze the effect of F-T on the shape retention of 3D structure of
surimi.
First, surimi ink (SI) and AFPs-based surimi ink (ASI) were prepared as 3D printing materials
.
The printed 3D structure then undergoes an F-T cycle
at -20 ºC and 25 ºC.
The microstructure (determined by SEM), protein secondary structure (obtained from CD spectroscopy), interaction, chemical bonds, degree of protein denaturation (determined by DSC), weight and water holding capacity of the two groups of inks were compared to illustrate the effect of F-T cycling on the shape retention of the 3D structure of
surimi products.
Results and Discussion shows the shape-holding capabilities of SI and ASI 3D structures after 0, 1, 2, 3, and 4 F-T cycles, as well as SEM images
.
The F-T cycle significantly affects the shape-preserving ability
of 3D structures.
Prior to F-T, the vertical and frontal widths and heights of the SI 3D structure were 25.
03 mm and 24.
87 mm, respectively, and the ASI 3D structure was 25.
43 mm and 24.
62 mm
。 In addition, the ASI 3D structure retains its shape even under 4 F-T cycles, it can be seen that after 4 F-T cycles, the width and height of the SI 3D structure are 10.
36 mm and 12.
07 mm, respectively, and the width and height of the ASI 3D structure are 22.
42 mm and 21.
07 mm, and after 4 F-T cycles, the ASI 3D structure presents better shape retention
than the SI 3D structure.
SEM showed that as the number of F-T cycles increased, the pore size of SI and ASI 3D structures increased and protein networks aggregated
.
In the ASI 3D structure, the average area and equivalent diameter of the aperture changed from 0.
001 mm2 and 0.
040 mm to 0.
015^mm2 and 0.
139 mm
, respectively.
In addition, when the SI 3D structure undergoes 1 F-T cycle, crosslinking and collapse of the protein network surface are clearly observed, and AFPs can inhibit the growth of ice crystals and their extrusion
of surimi proteins.
Therefore, ASI 3D structures show a smaller pore size after F-T compared to SI 3D structures, and no significant agglomeration and cross-linking are observed
.

A, SI 3D structure, B, ASI 3D structure
.
Fig.
1 Evaluation of retention force and SEM image of surimi 3D structure after 0, 1, 2, 3 and 4 F-T cycles In Figure 2, A1 and B1 show the changes
of CD spectra of myofibrillar proteins of SI and ASI 3D structures after 0, 1, 2, 3 and 4 F-T cycles.
With the increase of the number of F-T cycles, the intensity of the CD spectral negative band (222 nm and 208 nm) of myofibrillar protein in the ASI 3D structure did not increase or decrease significantly, and the SI 3D structure was significantly enhanced and decreased
.
This suggests that under the action of F-T, ice crystal extrusion induces changes in the protein secondary structure in the 3D structure of surimi, which can be alleviated
by AFPs.
The secondary structures of all groups are shown in A2 and B2 in Figure 2, and after 4 F-T cycles, the α-helix content in the ASI 3D structure decreased significantly (P<0.
05), while the β-corner content did not change significantly (P>0.
05).

。 The contents of β-turn angle and irregular curl did not improve significantly (P>0.
05), while the contents of α-helix and β-turn angle in SI 3D structure decreased significantly (P<0.
05), while the content of β-turn angle and irregular curl increased significantly (P<0.
05), indicating that the contents of α-helix, β-turn angle and irregular curl of myofibrillar protein could be changed by F-T, while AFPs could prevent the change<b146> of secondary structure to some extent.

A1 and B1 represent the circular dichroic spectra of SI and ASI 3D structures, respectively, A2 and B2 represent the secondary structure content of SI and ASI 3D structures, respectively, and the different letters of the secondary structure of the same sample indicate significance (P<0.
05).
<b148> 。 Fig.
2 Changes in the secondary structure of myofibroprotein in the 3D structure of surimi after 0, 1, 2, 3 and 4 F-T cycles As shown in Figures 3A1 and B1, for SI and ASI 3D structures, the G* value increases with the increase of the number of F-T cycles, and the G* value of the ASI 3D structure is not obvious
compared with the SI 3D structure.
This means that the physical and chemical properties of the surimi 3D structure are changed due to the F-T cycle, the overall deformation strength increases, and the 3D structure is destroyed
by AFPs.
G* grows with cross-linking between protein molecules, so surimi protein interactions
can be observed.
Figures 3A2 and B2 show typical chemical bond changes
in SI and ASI 3D structures after 0, 1, 2, 3, and 4 F-T cycles.
After the F-T cycle, the chemical bonds of the ASI 3D structure show small changes
compared to the chemical bonds of the SI 3D structure.
Explain that after F-T, chemical reactions and denaturation occur between proteins in the 3D structure of surimi, which can be prevented
by AFPs.
In addition, the F-T cycle enables enhanced hydrophobic action in
proteins.
Therefore, as the number of F-T cycles increases, the juice loss becomes more severe
.
Figure 3 A1 and B1 represent the relationship between the composite modulus (G*) and angular frequency (ω) of SI and ASI 3D structures after F-T cycles 0, 1, 2, 3 and 4 times, the frequency is 1~100 rad/s, at room temperature 25 °C, A2 and B2 indicate that SI and ASI 3D structures are in F-Intermolecular forces of proteins after cycles 0, 1, 2, 3 and 4 of T cycles, and different letters of intermolecular forces for the same sample indicate significant (P<0.
05) Figure 4 shows the normalized nonisothermal DSC curves of SI and ASI 3D structures after 0, 1, 2, 3, and 4 F-T cycles during heating from 25 ºC to 50 ºC at a rate of 5 ºC/min<b157>.
Peak heat flow after 0, 1, 2, 3 and 4 F-T cycles in both structures occurs at 33 ºC
.
The peak area of the SI 3D structure decreased from 0.
4609 to 0.
1478 after 4 F-T cycles, while the peak area of the ASI 3D structure decreased from 0.
4602 to 0.
3213
.
Compared to SI 3D structures, ASI 3D structures show a larger peak area after 4F-T cycles, indicating that the enthalpy value (ΔH) of the protein is larger, which better maintains the integrity of the protein, indicating that AFPs have a good protective effect
on the 3D structure.
A, SI 3D structure, B, ASI 3D structure
.
Figure 4 DSC heat map obtained from surimi 3D structure after 0, 1, 2, 3 and 4 F-T cycles at a rate of 5 °C/min between 25 ºC and 50 ºC As shown in Figures 5A and B, the weight and water holding capacity (WHC) of SI and ASI 3D structures decrease
after 0, 1, 2, 3 and 4 F-T cycles.
For SI 3D structures, their weight was reduced from (15.
65±0.
06) g to (6.
16±0.
16) g, and the WHC was reduced from (83.
00±0.
47) % to (53.
95±0.
51)
%.
For ASI 3D structures, weight decreased from (15.
65±0.
06) g to (9.
99±0.
54) g and WWHC decreased from (72.
67±0.
00) % to (68.
30±1.
81)%.

In contrast, the weight and WHC of SI 3D structures drop more pronounced
during the F-T cycle.
It is stated that protein denaturation and exposure to hydrophobic groups in the F-T cycle lead to a decrease in the ability to bind water, which allows proteins to form larger ice crystals during subsequent freezing, and AFPs can inhibit the growth of ice crystals, preventing protein denaturation as well as loss of juice
.
As a result, the ASI 3D structure has better results for cryostorage
.
Figure 5A and B represent the weight (g) and WHC (%) of the surimi 3D structure after F-T cycles 0, 1, 2, 3 and 4 times, respectively, and different letters indicate significance (P<0.
05)<b168>

of the same sample
。 Due to the disruption of hydrogen bonds, the α helical structure of myofibrillar protein in surimi will unfold and expose hidden hydrophobic groups inside, thereby improving hydrophobicity
.
The improvement of hydrophobicity will promote irreversible chemical crosslinking and denaturation of surimi protein, and also reduce the ability
of protein to bind to water.
In the following freezing process, the water inside the surimi 3D structure forms larger ice crystals
.
Once the large ice crystals melt, sap loss occurs, causing the SI 3D structure to collapse
.
AFPs inhibited the growth of ice crystals in surimi protein, preventing protein denaturation and juice loss
.
Finally, ASI 3D structures exhibit good shape retention
in the F-T cycle.
In addition, AFPs show great application potential in the frozen storage of 3D printed protein foods, promising to provide a promising cryoprotectant for low-sweetness and low-calorie foods, especially for upcoming prepared dishes
.

Corresponding author

Shaoyun Wang, Ph.
D.
, second-level professor, doctoral supervisor, executive dean of the School of Biological Science and Engineering of Fuzhou University, postdoctoral fellow at the University of Wisconsin (UW-Madison) and UC-Davis, was selected as a leading talent in scientific and technological innovation of the National "10,000 Talents Program", a leading talent in scientific and technological innovation for young and middle-aged people of the Ministry of Science and Technology, a provincial A high-level talent, a provincial high-level innovation talent, and a provincial scientific and technological innovation leader
。 He is also the director of the Chinese Society of Food Science and Technology, the vice chairman of the Fujian Health Engineering Society, the vice chairman of the Fujian Food Science and Technology Society, the editorial board member of Food Science and Human Wellness, Journal of Future Foods, Hans Journal of Food and Nutrition Science, Food Science, Food Industry Science and Technology, and the first batch of translation experts of "Chinese and Foreign Food Technology"
。 He has presided over more than 30 projects at the provincial and ministerial level, compiled 8 books, authorized 69 invention patents, and published 300 academic papers, including 230 in SCI/EI
.
The achievements he presided over won the International ICOFF Academic Conference Award, the first prize of China's industry-university-research cooperation innovation achievements, the first prize of National Food Industry-University-Research Excellent Scientific Research Achievements, the first prize of Science and Technology Progress Award of China Federation of Chemical Industry, the first prize of Provincial Science and Technology Progress Award, the second prize of Provincial Science and Technology Progress Award, and the second prize of Provincial Natural Science Award
.
He has won the Baosteel Outstanding Teacher Award, the Provincial Excellent Teacher Award, the Provincial Outstanding Scientific and Technological Worker Award, the Lu Jiaxi Outstanding Mentor Award and the Famous Teacher Award
.
He was invited to serve as the "Changjiang Scholar" Distinguished Professor of the Ministry of Education and the review expert
of the National Natural Science Foundation of China.

Analysis of the shape retention ability of antifreeze peptide-based surimi 3D structures: potential in freezing and thawing cycles

Han Tian^a,b, Xu Chen^b, Congrong Chen^b, Jinhong Wu^c, Jianlian Huang^f,g, Lei Zhao^{d.
e,*}, Shaoyun Wang^b,*

^a College of Chemical Engineering, Fuzhou University, Fuzhou 350108, China

^b College of Biological Science and Engineering, Fuzhou University, Fuzhou 350108, China

^c Department of Food Science and Engineering, School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai 200240, China

^d College of Food Science, South China Agricultural University, Guangzhou 510642, China

^e Guangdong Laboratory for Lingnan Modern Agricultural, Guangzhou 510642, China

^f Key Laboratory of Refrigeration and Conditioning Aquatic Products Processing of Ministry of Agriculture and Rural Affairs, Xiamen 361022, China

^g Fujian Anjoy Foods Co.
Ltd.
, Xiamen 361022, China

Correspondence to:

scauzl@scau.
edu.
cn

shywang@fzu.
edu.
cn

Abstract

The effects of freeze–thaw (F-T) cycles on the shape retention of antifreeze peptides-based surimi ink (ASI) 3D structures were analyzed.
The results showed that the ASI 3D structure has good shape retention ability, and the width, height, weight, and water holding capacity were 22.
42 mm, 21.
07 mm, 9.
99 g, and 68.
30 % even after F-T 4 times, respectively.
The average area and equivalent diameter of ice crystals in ASI 3D structures only expand from 0.
001 mm²and 0.
040 mm to 0.
015 mm² and 0.
139 mm, respectively.
The α-helix and β-sheet of myofibrillar protein in ASI 3D structure were slightly decreased by 44.
16 ± 0.
98 % to 33.
33 ± 0.
92 % and increased by 18.
28 ± 4.
45 % to 24.
43 ± 1.
60 %, respectively.
The chemical bond and protein interaction have changed to some extent.
AFPs can prevent denaturation and juice loss of surimi 3D structures after F-T.
The results provide theoretical guidance for maintaining the shape retention of frozen 3D food structures.

Reference:

TIAN H, CHEN X, CHEN C R, et al.
Analysis of the shape retention ability of antifreeze peptide-based surimi 3D structures: potential in freezing and thawing cycles[J].
Food Chemistry, 2023, 405: 134780.
DOI:10.
1016/j.
foodchem.
2022.
134780.

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