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. 2025 Dec 5;32:103383. doi: 10.1016/j.fochx.2025.103383

Multispectral study on the effects of capsaicin on myofibrillar proteins structure and functional characteristics in Litopenaeus vanname

Yuchen Deng a,b, Shiyuan Chen a, Jie Feng a, Chuandong Fang a, Jiancong Huo a, Huimin Lin a,⁎, Shucheng Liu c, Soottawat Benjakul d, Bin Zhang a,b,⁎
PMCID: PMC12752521  PMID: 41477630

Abstract

Study on the effect of capsaicin (CAP) on the structural changes of myofibrillar proteins (MPs) in Litopenaeus vannamei. In this experiment, the effects of different concentrations of CAP (5, 10, 15, 20 mg/L) on the structural changes of MPs in L. vannamei were investigated through turbidity, surface hydrophobicity, particle size and zeta potential, Raman spectroscopy, ultraviolet spectroscopy, fluorescence spectroscopy, infrared spectroscopy, etc. The results of UV and fluorescence spectroscopy showed that the peak intensities of both UV and fluorescence spectra increased with increasing CAP concentration, and infrared spectroscopy indicated that CAP exerted no significant effect on the secondary structure of MPs. The results of the electronic tongue showed that CAP had a certain effect on the presentation of MPs of L. vannamei. The results of this experiment provide guidance for the application of CAP in the production and processing of L. vannamei.

Keywords: Litopenaeus vannamei, Capsaicin, Myofibrillar proteins, Protein structure, Protein characteristic

Highlights

  • •

    Use of multispectroscopy to study the effect of CAP on the structure of MPs.

  • •

    Application of CAP to aquatic product preservation provides new ideas for preservation of Litopenaeus vannamei.

  • •

    Litopenaeus vannamei was chosen as the raw material, it is cheap and readily available, reducing production costs.

1. Introduction

The Pacific white shrimp (Litopenaeus vannamei) is one of the most important aquaculture shrimp species in the world. L. vannamei is a well-known shrimp for its nutritional and economic value. L. vannamei is popular with consumers because of its delicious meat and rich nutrition. Myofibrillar proteins (MPs) are the major contributors to muscle mass. The MPs of L. vannamei account for about 50 %–60 % of muscle composition, MPs are primarily composed of myosin, actin, actin-binding filaments, and troponin (Zhang et al., 2024). During processing, MPs determine their the main functional properties of proteins, such as gel properties and emulsification properties, which affect the quality of the final processed gels and emulsions (Zhao, Jiang, et al., 2025).

Capsaicin (CAP), chemically known as trans-8-methyl-N-vanillyl-6-nonenamide with the molecular formula C₁₈H₂₇NO₃, is a lipophilic vanilloid alkaloid found in the berries of plants belonging to the genus Capsicum within the nightshade family (Zhang et al., 2025). CAP is the main active substance in chili peppers and one of the major components in their fruit, with a wide range of bioactivities. CAP has analgesic, anti-inflammatory, antioxidant, intestinal dysbiosis reduction, anticancer, antibacterial properties, high blood pressure improvement, cardiovascular and digestive system protection and holds great application potential. As a condiment, chili is loved by people, especially young people. Zhao, Yin, et al. (2025) investigated the antioxidant mechanism of beef MPs binding to CAP, and Wu et al. (2023) investigated the mechanism of MPs-CAP interaction using multispectroscopy. CAP causes changes in the amino acid microenvironment and induces changes in the secondary structure of MPs, with structural de-folding occurring during CAP incorporation, exposing more hydrophobic groups. Wang et al. (2023) investigated the interaction between MPS and CAP, discovering that CAP exhibits high affinity for porcine MPS and can bind to them spontaneously via hydrophobic interactions. Zhan et al. (2020) examined the interaction between β-lactoglobulin and CAP, and revealed that both hydrophobic interactions and van der Waals forces are involved in their binding process.

Therefore, in this paper, the effect of CAP on the structure of MPs was investigated using MPs from L. vannamei through turbidity, surface hydrophobicity, measurement of sulfhydryl groups, particle size and zeta potential, Raman spectroscopy, ultraviolet spectroscopy, fluorescence spectroscopy, and infrared spectroscopy, in order to provide guidance for the production and processing of L. vannamei.

2. Materials and methods

2.1. Reagents and materials

The fresh L. vannamei were purchased from Zhoushan International Aquatic City (Zhoushan, China) in March 2024; CAP (HPLC≥98 %) was purchased from Jiangxi Bai Cao Yuan Biotechnology Co.; potassium phosphate buffer was purchased from Codow, Guangzhou Hewei Pharmaceutical Technology Co., the total sulfhydryl group kit and Coomassie Brilliant Blue Protein kit were purchased from Nanjing Jiancheng Bioengineering Institute.

2.2. MPs extraction method

The experimental method was slightly modified according to the method of Wang et al. (2023). After crushing the shrimp, the meat was blended with potassium phosphate buffer (PSB) in a 1:9 ratio. The PSB (pH 7.0) comprised 0.1 M NaCl, 2 mM MgCl2 and 1 mM ethylenediaminetetraacetic acid (EDTA), and the mixture was then homogenized (10,000 r/min, 30 s) using a homogenizer. The homogenate was centrifuged (10,000 r/min, 4 °C, 10 min), and this step was repeated twice, with the supernatant discarded and the precipitate retained. The precipitate was mixed with nine times its volume of 10 mM potassium phosphate buffer (pH 7.4, containing 0.6 M KCl), homogenized (10,000 r/min, 30 s) with a homogenizer (Shanghai Li-Chen Bang Xi Instrument Technology Co., Ltd., FJ200-S), and further extracted in an ice bath for two hours, followed by centrifugation (10,000 r/min, 4 °C, 10 min). The mixture was filtered through double-layered gauze, and the resulting filtrate was the L. vannamei MPs stock solution. The protein concentration (mg/L) of MPs was determined using the Coomassie Brilliant Blue kit (Nanjing Jiancheng Bioengineering Institute, China).

2.3. CAP binding methods to MPs

According to the method of Wang et al. (2023), with slight modification. CAP was dissolved in 10 % ethanol and then mixed with MPs extract in a 1:1 ratio. The solution prepared by mixing MPs extract and potassium phosphate buffer in a 1:1 ratio was designated as the blank group, while the 1:1 mixture of the MPs extract and CAP solution was formulated into compound solutions containing 5, 10, 15, and 20 mg/L of MPs-CAP.

2.4. Surface hydrophobicity of MPs

Surface hydrophobicity of MPs from L. vannamei was determined using bromophenol blue (BPB) as a hydrophobic chromophore according to the method of Lv et al. (2018), with slight modifications. The MPs-CAP complex (2 mg/mL) was mixed with 200 μL of 1 mg/mL BPB and incubated at room temperature for 10 min. After centrifugation (3000 r/min, 15 min), 10 mM potassium phosphate buffer (pH 7.4, containing 0.6 M KCl) was used as an internal control instead of MPs. All samples were stirred at room temperature for 10 min and then centrifuged at 7000 r/min for 15 min. The absorbance was measured at 595 nm after diluting by 10 times. The amount of BPB bound in the sample, calculated according to the following formula, was used as the hydrophobicity index:

BPBboundμg=200A0−A/A0 (1)

where A0 is the absorbance of the blank sample and A is the absorbance of the experimental sample.

2.5. Total sulfhydryl content of MPs

The extracted MPs solution was diluted to 2 mg/mL, and the total sulfhydryl content was measured using a total sulfhydryl kit from Nanjing Jiancheng Bioengineering Institute.

2.6. Determination of MPs turbidity

According to the method of Xu et al. (2018). With slight modification. The MPs solution after binding with CAP was diluted to 2 mg/mL, equilibrated for 20 min, and the absorbance at 340 nm was measured.

2.7. Determination of foaming properties

Foaminess was determined with reference to the method of Chen, Wang, Liu, et al. (2025). The initial solution volume was 30 mL, and the solution washomogenized at 10,000 r/min for 60 s using a high-speed homogenizer (Shanghai Li-Chen Bangxi Instrument Technology Co., Ltd., FJ200-S). After homogenization, the initial foam volume (V0) and the foam volume 60 s after homogenization (V1) were calculated using the following equations:

Foam capacity%=V1−V0/V0×100% (2)

2.8. Particle size and zeta potential

The particle size and ζ-potential of MPs were measured using a particle size potential analyzer (ZS90 Malvern, UK). The mixture contained MPs at a concentration of 2 mg/mL.

2.9. Ultraviolet spectrum

Fluorescence ultraviolet two-in-one (Duetta, Japan) was used to obtain the UV–visible absorption spectrum at the wavelength range of 235–320 nm, and the method used by Wu et al. (2023) was slightly modified. In the mixture of CAP and MPs, the concentration of CAP was 5, 10, 15, 20 mg/L, and the concentration of MPs was 0.5 mg/mL.

2.10. Fluorescence spectra

The method for determining fluorescence spectra was slightly modified with reference to the method of Liu et al. (2025). Fluorescence spectra of the sample solution were recorded using a fluorescence-ultraviolet two-in-one spectrometer (Duetta, Japan). The excitation wavelength was set to 280 nm, and the emission wavelength range was 280–475 nm. The widths of both the excitation and emission slits were set to 10 nm. CAP concentrations were 5, 10, 15 and 20 mg/L, and the concentration of MPs was 0.5 mg/mL.

2.11. Raman spectroscopy

Following the method of Wang et al. (2023), a confocal Raman microscope (XploRA Plus, Japan) was used to focus the laser light on the MPs-CAP complex samples on the slides using a 50× long-focus lens. An excitation wavelength of 532 nm was used. Raman spectra were scanned over a range of 600–2300 cm−1 at a resolution of 1 cm−1, and each sample was scanned three times.

2.12. Fourier infrared spectroscopy

The secondary structure of MPs was analyzed by FTIR spectroscopy (Nloolet is50, USA) by referring to the method of Sun et al. (2023). Freeze-dried powdered samples (1 mg) were mixed with potassium bromide (100 mg), pressed into pellets, and scanned from 4000 to 400 cm−1.

2.13. SDS-page

The method was slightly modified from that described by Lu et al. (2025). Briefly, a mixture of 40 μL of MPs solution was mixed with 10 μL of non-denaturing, non-reducing sample buffer (5×, Biotronik) heated at 95 °C in a water bath for 10 min, and then subjected to electrophoretic analysis. Both the standard protein marker and the sample was loaded at 10 μL. Electrophoresis was performed at a constant voltage of 60 V for approximately 30 min, followed by 120 V for approximately another 30 min. The Rainbow 245 broad-range protein marker (11–250 kDa, Solebold) was used as a reference. The precast gel was stained with Coomassie Brilliant Blue staining solution for 3 h and then decolored. After destaining, the gel was imaged and analyzed using an automatic gel imaging analyzer (GenoSens).

2.14. MPS-CAP electronic tongue measurement

MPs-CAP was measured using an electronic tongue (Zhejiang Zheke Instrument Equipment Co., Ltd., iTongue20). The experiment was repeated three times and PCA analysis was performed.

2.15. Data analysis

All data were collected and repeated 6 times. The results were processed and analyzed using Origin 2025, and the significance level was set at P < 0.05.

3. Results and analysis

3.1. Surface hydrophobicity analysis of MPs

Surface hydrophobicity can be used to characterize changes in the distribution of hydrophobic groups on the proteins surface, which reflects the degree of denaturation and hydrolysis (Wang, Cao, et al., 2024). It also reflects the number of hydrophobic residues on the surface of proteins exposed to the external environment, serving as an important indicator for characterizing protein microstructure (Xiang et al., 2025).

As shown in Fig. 1(A), there was little difference between the blank group and the 10 mg/L treatment group, and little difference between the 5 mg/L and 20 mg/L treatment groups. The highest surface hydrophobicity was observed at a CAP addition of 15 mg/L. It is hypothesized that at 15 mg/L CAP, most hydrophobic groups were exposed, leading to a significant increase in sulfhydryl content. Upon CAP addition, surface hydrophobicity first increased, then decreased, and then increased again. This trend suggests that MPs undergo structural unfolding during CAP treatment, exposing more hydrophobic groups. At 10 mg/L CAP, aggregation occurred, masking some exposed hydrophobic groups and reducing hydrophobicity. With a further increase in CAP concentration, MPs aggregates unfolded or degraded, enhancing surface hydrophobicity—similar results were reported in Wang et al. (2025). When treated with a high concentration of CAP (20 mg/L), hydrophobic interactions between protein molecules favored the formation of protein aggregates due to overexposure of hydrophobic groups, which were re-embedded, leading to a decrease in surface hydrophobicity, and similar results were found by Jiang et al. (2021).

Fig. 1.

Fig. 1

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(A) Changes in surface hydrophobicity of MPs of L. vannamei (B) Changes in total sulfhydryl groups of MPs of L. vannamei.

3.2. Analysis of total sulfhydryl content of MPs

Sulfhydryl groups are important for maintaining the spatial structure of proteins, as they can be converted to disulfide bonds in the environment, thereby reducing their content (Yin et al., 2024). Fig. 1(B) shows the changes in total sulfhydryl groups in MPs of L. vannamei before and after CAP addition. The total sulfhydryl group content exhibited an increasing-decreasing-increasing trend with increasing CAP concentration. It is hypothesized that at lower CAP concentrations, CAP acts as a protector of sulfhydryl groups; as the concentration increases, CAP reacts with some sulfhydryl groups, leading to a slight decrease in total sulfhydryl groups; and at higher CAP concentrations, the antioxidant properties of CAP predominate (Akyuz et al., 2018), thereby promoting an increase in total sulfhydryl group content.

3.3. MPs turbidity analysis

Turbidity can reflect the degree of aggregation and dispersion of protein. The turbidity changes of MPs before and after CAP addition are shown in Fig. 2(A). Upon CAP addition, the turbidity of MPs changed. Compared with untreated MPs, CAP-treated samples exhibited an increasing-decreasing-increasing trend. We hypothesize that low CAP concentrations induce subtle structural rearrangements in MPs, leading to a marginal decrease in solution turbidity. When CAP concentration increases further, turbidity rebounded, presumably due to the formation of small molecule aggregates from MPs molecules as CAP concentration rises, thereby increasing solution turbidity. It may also be because the phenolic hydroxyl group of capsaicin binds to the hydrophobic regions (aromatic amino acids) of MPs, thereby weakening the hydrophobic interactions between proteins. Similar results were obtained in the study by Zhan et al. (2025). It is also possible that the increase in turbidity due to colloidal molecules formation between CAP and MPs—a similar phenomenon was observed by Li et al. (2021), in which proanthocyanidins interacts with lactoferrin, leading to increased turbidity.

Fig. 2.

Fig. 2

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(A) Changes in turbidity of MPs of L. vannamei. (B) Effect of foaming properties of MPs in L. vannamei.

3.4. Foamability analysis

The foaming properties of proteins are related to their film-forming ability at the gas-liquid interface (Han et al., 2022; Ventureira et al., 2012). Fig. 2(B) shows the effect of CAP on the foaming properties of MPs in L. vannamei. It can be seen from the figure that the foaming properties of MPs showed a tendency to increase and then decrease with the concentration of CAP, which is speculated to be due to low concentrations of CAP exposed part of MPs groups, thereby improving the foaming properties of MPs. When the CAP concentration was further increased, MPs formed small molecular aggregates, leading to a decrease in the foaming properties of MPs. These results indicated that an appropriate concentration of CAP can enhance the efficacy of MPs in preventing bubble contraction, aggregation or migration, which is similar to the conclusion drawn by Qu et al. (2025) in the foaming property test of quinoa protein-tannic acid interaction. This can also be attributed to reduced intermolecular interactions leading to decreased viscoelasticity, a conclusion similar to that reached by Yu et al. (2018) in their experiments.

3.5. Particle size and zeta potential analysis

Particle size and zeta potential are important indexes of MPs, as shown in Fig. 3(A), the particle size of MPs in L. vannamei MPs gradually decreased with increasing of CAP concentration, which is in agreement with the results of the study of Zhan et al. (2020). The reason for this phenomenon may be that with the increase of CAP concentration, the large aggregated particles of the CAP-MPs complexes were transformed into small aggregated particles, which made the particle size of MPs in L. vannamei decrease continuously.

Fig. 3.

Fig. 3

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(A) Changes in particle size of MPs of L. vannamei. (B) Changes in zeta potential of MPs of L. vannamei.

Zeta potential is a measure of the repulsive force between particles, which is related to the stability of colloidal dispersion (Jia et al., 2023). Fig. 3(B) shows the changes in the zeta potential of the MPs of L. vannamei before and after the addition of CAP. From the figure, it can be seen that all the groups are negatively charged. The absolute value of the zeta potential reflects the stability of the sample solution. The absolute value corresponds to the size of the mutual repulsive force between the particles and is positively correlated with it. The particle size distribution of proteins can reflect the changes within protein molecules in the physical environment, such as aggregation and depolymerization. As shown in the figure, the particle sizes of all treated groups were larger than those of the untreated group, and are less than 10 mV. Wu et al. (2023) studied the binding of capsaicin to porcine myofibrillar protein, the zeta potential also ranged between −1 and − 10 mV. This may be attributed to interactions between CAP and MPs, which alter the MPs structure, expose the protein's negative charges, and ultimately modify the zeta potential. The addition of CAP strengthens its interaction with MPs and helps maintain a stable complex structure through the formation of hydrogen bonds.

3.6. Ultraviolet spectral analysis

UV–Vis absorption spectroscopy is a simple and effective method for determining the binding mechanism of protein-small molecule complexes (Xiao et al., 2025). UV spectroscopy was used to reveal changes in protein conformation and side chains of aromatic amino acids, including tryptophan (Trp), tyrosine (Tyr) and phenylalanine (Phe) (Zheng et al., 2025). As shown in Fig. 4(A), the untreated MPs solution, the maximum absorption peak was at 274 nm. The increase in the complex's absorbance is due to the binding of CAP with the aromatic amino acids present in MPs (Wu et al., 2023). In addition, the absorption intensity of the sample increased with the processing treatment concentration, indicating an increasing trend of reaggregation of CAP-treated proteins compared to untreated proteins (Ekezie et al., 2019).

Fig. 4.

Fig. 4

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(A) Changes in UV spectra of MPs of L. vannamei. (B) Changes in fluorescence spectra of MPs of L. vannamei.

3.7. Fluorescence spectral analysis

The fluorescence generated by aromatic amino acid residues in MPs at specific excitation wavelengths can indicate the tertiary structural changes of proteins. In Fig. 4(B), it can be observed that the fluorescence intensity of MPs reached its highest peak at 330 nm. With the increase of CAP concentration, the wavelength was gradually blue-shifted to 312 nm, A blue shift with increasing CAP concentration suggests that partial refolding of the protein occurs during thawing (Cai et al., 2018) and the fluorescence intensity gradually increased. The increase in fluorescence intensity was attributed to the unfolding of the protein structure, which enhanced the exposure of aromatic amino acids, and the increase in fluorescence intensity with increasing CAP concentration indicated that the protein underwent an unfolding process (Wang et al., 2025). The fluorescence profiles were consistent with the UV results, suggesting that CAP has an effect on the tertiary structure of MPs in L. vannamei.

3.8. Raman spectral analysis

As shown in Fig. 5, the CAP-added group showed an increase in multiple peaks compared to the non-CAP group, with peaks at 1075 cm−1 attributed to C—C stretching, 1260 cm−1 representing C—H in-plane bending, 1298 cm−1 for CH2 bending, and 1440 cm−1 corresponding to C—H shear (Wu et al., 2024). The amide I band (1600–1700 cm−1) is commonly used to characterize the secondary structure of proteins (Chen et al., 2024), and different secondary structures cause shifts in the frequency and intensity of the amide I band (Wang, Zhao, et al., 2024). The changes in Raman peak intensities for the CAP-added group indicate that CAP has more or less influence on the secondary structure of proteins, which is consistent with the conclusion drawn from infrared spectroscopy.

Fig. 5.

Fig. 5

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Changes in Raman spectra of MPs of L. vannamei.

3.9. Fourier infrared spectral analysis

FTIR plays a crucial role in analyzing the structural changes of proteins, and it is often used to reflect the structural changes of MPs before and after processing. As shown in Fig. 6, although the secondary structure exhibited slight fluctuations with increasing CAP concentration, the changes were not significant. Wang et al. (2023) investigated the effect of CAP on the secondary structure of porcine MPs and found that the secondary structure of MPs did not change significantly with increasing CAP concentration. Romano et al. (2021). studied the interaction between bovine α-lactalbumin and CAP complexes and found that CAP had almost no effect on the secondary structure of holo-ALA, a finding that is consistent with the results of the present study.

Fig. 6.

Fig. 6

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Changes in the secondary structure of MPs of the L. vannamei.

3.10. SDS-PAGE analysis

SDS-PAGE is a key method for analyzing proteins, by which various components can be separated according to their molecular weights (Tao et al., 2024), thus determining the composition of the proteins. Primary bands of MPs include myosin heavy chain (MHC, 200 kDa), actin (42 kDa), troponin T (37 kDa), promyosin (34–36 kDa), and myosin light chain (MLC, 15–25 kDa) (Chen, Wang, Zhao, et al., 2025). Fig. 7 reveals the changes in electrophoretic bands of L. vannamei before and after the addition of CAP. As shown in Fig. 7, there were no obvious changes in the protein bands before and after the addition of CAP, indicating that CAP did not destroy the protein bands within the range of 0–20 mg/L, which demonstrates that CAP is a stable additive within a certain concentration range, indicating that CAP does not affect MPs composition (Mi et al., 2022), this indicates that the interaction between CAP and MPs is non-covalent. During heating, these non-covalent interactions are disrupted, resulting in no significant changes in the SDS electrophoresis bands, and corroborates the feasibility of applying CAP in food processing.

Fig. 7.

Fig. 7

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SDS-PAGE of MPs of L. vannamei.

3.11. Electronic tongue analysis

Electronic tongues are often used to mimic the human sense of taste to compensate for the lack of human sensory evaluation. An electronic tongue was used to analyze MPs in L. vannamei before and after CAP addition. Fig. 8 shows that upon CAP addition. When CAP was added, there were almost no overlapping parts with the MPs and CAP samples before the addition, and the four CAP-added groups had similar regions and some overlapped with each other, which indicated that the CAP-added groups had some differences compared with the blank groups. CAP influences the flavor of MPs in L. vannamei, providing a theoretical basis for its application in food processing. Among the studies related to the effect of chili peppers on flavor presentation, Yao et al. (2024) demonstrated that chili peppers have a certain effect on the flavor of roasted lamb.

Fig. 8.

Fig. 8

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Electronic tongue of MPs of L. vannamei.

4. Conclusion

This paper reveals the effects of CAP on MPs of L. vannamei through the determination of a series of indicators before and after CAP addition, as well as the use of multispectroscopic techniques (UV spectroscopy, fluorescence spectroscopy, infrared spectroscopy, Raman spectroscopy). The results show that CAP affects the structure of the MPs of the L. vannamei, and that CAP of different concentrations has different effects. This study reveals the effect of CAP interaction with MPs of L. vannamei, and provides guidance for regulating of spicy flavor during shrimp processing to improve the sensory characteristics of shrimp products. CAP binds to myofibrillar protein, affecting the microenvironment of amino acids, MPs underwent structural unfolding during the addition of CAP, exposing more hydrophobic groups, the right amount of concentration of CAP can be enhanced by MPs to prevent the contraction of bubbles, aggregation or migration, and a high concentration of CAP will disrupt the hydrogen bonds in the protein. CAP also affects the tertiary structure of MPs, and SDS-PAGE showed that CAP in the experimental group did not significantly damage the molecular bands, the interaction between CAP and MPs is non-covalent, further supporting the feasibility of CAP's application to the food processing of L. vannamei. Further investigation into the interaction mechanism between CAP and MPs is needed to provide a more solid theoretical basis for applying CAP to seafood products.

CRediT authorship contribution statement

Yuchen Deng: Writing – review & editing, Writing – original draft, Methodology, Formal analysis, Data curation. Shiyuan Chen: Writing – review & editing. Jie Feng: Writing – review & editing, Data curation. Chuandong Fang: Writing – review & editing, Supervision. Jiancong Huo: Supervision, Writing – review & editing. Huimin Lin: Writing – review & editing, Supervision. Shucheng Liu: Writing – review & editing, Supervision. Soottawat Benjakul: Writing – review & editing, Supervision. Bin Zhang: Writing – review & editing, Supervision, Methodology.

Declaration of competing interest

The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Acknowledgments

This study was funded by the National Natural Science Foundation of China (Grant No. U23A20263, 32502306), and the Zhejiang Natural Science Foundation Project (Grant No. LRG25C200001), and the National Key Research and Development Program of China (Grant No. 2023YFD2401500).

Contributor Information

Huimin Lin, Email: lin.huimin@zjou.edu.cn.

Bin Zhang, Email: zhangbin@zjou.edu.cn.

Data availability

Data will be made available on request.

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