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. 2020 Aug 25;58(6):2258–2264. doi: 10.1007/s13197-020-04736-4

The effects of sodium chloride on proteins aggregation, conformation and gel properties of pork myofibrillar protein Running Head: Relationship aggregation, conformation and gel properties

Zhuang-Li Kang 1,✉, Xue-hua Zhang 1, Xiang Li 1, Zhao-jun Song 1, Han-jun Ma 1, Fei Lu 1, Ming-ming Zhu 1, Sheng-ming zhao 1, Zheng-rong Wang 1
PMCID: PMC8076348  PMID: 33967322

Abstract

The objective of this study was to evaluate relationship with aggregation, secondary structures and gel properties of pork myofibrillar protein with different sodium chloride (1%, 2% and 3%). When the sodium chloride increased from 1 to 3%, the active sulfhydryl, surface hydrophobicity, hardness and cooking yield of myofibrillar protein were increased significantly (p < 0.05), the particle size, total sulfhydryl and Zeta potential were decreased significantly (p < 0.05), these meant the aggregations of pork myofibrillar protein were decreased. The changes of proteins aggregation induced the strongest intensity band of Amide I shifted up from 1660 cm−1 to 1661 cm−1, meanwhile, the β-sheet structure content was increased significantly (p < 0.05) with the sodium chloride increased. From the above, the lower proteins aggregation and higher β-sheet structure content could improve the water holding capacity and texture of pork myofibrillar protein gel.

Keywords: Myofibrillar, Sodium chloride, Aggregation, Texture, Gel properties

Introduction

Myofibrillar protein accounts for 50–55% of the total protein content of muscle, mainly composes of myosin and actin, which is the main function of the protein in processing, and the changes of the structure and conformation of the myofibrillar protein are largely affected the textural and structural properties of meat and meat products (Zhang et al. 2017a, b; Shen et al. 2019a, b; Li et al. 2020a, b). The formation of heat-induced myofibrillar protein gel needed to undergo three processes, such as degeneration, aggregation and cross-linking. The first is non-covalent bond dissociation causes by heating the proteins, then altering the conformation of proteins, causing denaturation of proteins and forming a larger molecule of gel by cross-linking and aggregation (Feng et al. 2017; Guo and Xiong 2019).

Sodium chloride played an important role in emulsion meat products, which promoted dissolution and swelling of myofibrillar protein, improved the water holding capacity and oil-preserving performance of the gel, enhanced yield, texture and shelf life of the meat products (Zhang et al., 2017a, b; Paula et al., 2019). In addition, sodium chloride affected protein aggregation, such as soy protein accelerate the aggregation rate after adding sodium chloride, the degree of hydrolysis unchanged, which was due to rapid increase of short-chain elastin after heated (Marín, Alemán et al. 2018). Thorarinsdottir et al. (2011) have reported that the different pre-salting methods could change the degree of fish meat protein aggregation during salting, and the changes in denaturation or aggregation were assigned to between myosin and collagen. Gao et al. (2018) studied the heat-induced aggregation of bighead carp myosin was induced by L-His in low/high sodium chloride solution, whose found that L-His prompted the myosin to form finer aggregates and good gel network during heating, also suppressed the aggregation via weaken hydrophobic interaction. Some researchers reported that the driving force of protein aggregation originated from the interaction between proteins. The interaction of non-covalent bonds (hydrophobic, hydrogen and electrostatic) and covalent bonds (disulfide bonds) was considered to be the main factor of protein aggregation, and its mechanism was based on the decomposition and aggregation of different attribute subunits (Ruan et al. 2014). Proteins aggregation affected the conformational of protein molecules, such as a higher degree of aggregation could increase the β-sheet structure, which was the basis for forming gels (Marín et al. 2018). The thermal induced the aggregation of myofibrillar proteins to form the thermal induce gel, and the secondary and tertiary structures were changed, such as more β-sheet structure formed and more aliphatic amino acids exposure to the polar environment (Herrero et al., 2008). As far as we know, there were many studies on the effect of sodium chloride on the processing properties of meat protein, but the effect of myofibrillar protein on the aggregation was little (Zheng et al., 2019; Feng et al., 2018). Therefore, the objective of this experiment was to investigated the effect of sodium chloride on proteins aggregation, conformation and gel properties of pork myofibrillar protein, for lowering the sodium chloride of emulsion meat products without sacrificing the quality.

Materials and Methods

Materials

Pork leg meat (semitendinosus, biceps femoris, mesoglutaeus; 180 ± 3 day old; 100 ± 5 kg; after 24–48 h of slaughtering; pH, 5.70 ± 0.02; moisture, 71.05 ± 0.31%; protein, 20.52 ± 0.25%; fat, 7.28 ± 0.17%) were purchased from a local slaughterhouse (Xinxiang Gaojin Food co. LTD, China), and the core temperature was 2 ± 2 °C. Tris, EDTA, KCl, MgCl2, NaCl, K2HPO4, KH2PO4, EGTA, NaN3, Triton, urea, glycine were analytical grade.

Extraction of myofibrillar protein

The myofibrillar protein was extracted from pork leg meat carried out as described by Doerscher et al. (2004) with some modification. After removing of the connective and fat tissue, the 200 g pork meat was cut into small pieces and homogenized (speed, 15,000 rpm) in 800 g buffer (pH 8.3, 10 mmol/L EDTA, 100 mmol/L Tris) in homogenizer (T25, IKA, Germany). The homogenates were centrifuged at 1000 × g for 20 min at 2 ± 2 °C (Sorvall LYNX4000, Thermo Fisher Scientific, Germany). After decanting the supernatant, the precipitate were dispersed in four volumes of a buffer (pH 7.0, 1 mmol/L NaN3, 1 mmol/L EGTA, 2 mmol/L MgCl2, 20 mmol/L K2HPO4/KH2PO4, 100 mmol/L KCl) and centrifuged at 1000 × g for 10 min under the same conditions above for another twice. And then the sample was resuspended in four volumes of another buffer (pH 7.0, 1% Triton X-100, 1 mmol/L NaN3, 1 mmol/L EGTA, 2 mmol/L MgCl2, 20 mmol/L K2HPO4/KH2PO4, 100 mmol/L KCl), and then centrifuged at 1500 × ggfor 10 min under the same conditions above for another once. After decanting the supernatant, pellets were resuspended in four volumes of a 0.1 mol/L KCl solution, and centrifuged at 1500 × g for 10 min under the same conditions above for another once. After that, the sample was resuspended in four volumes of 0.1 mol/L NaCl solution, and centrifuged at 1500 × g for 10 min under the same conditions above repeated once again. The protein content was measured by the Biuret methodusing bovine serum albumin (BSA) as the standard (Gornall et al. 1949).

Preparation of myofibrillar protein gel

Two milliliter myofibrillar protein solutions (pH 6.5, 60 mg/mL) with 1%, 2% and 3% (weight/weight) sodium chloride was loaded in a 5 mL capped plastic centrifuge tube, respectively. And then the solutions were heated at 65 °C for 30 min in a water bath (the core temperature was 65 °C). After that, the tubes were cooled to room temperature and then kept overnight at 2 ± 2 °C until testing.

Total and reactive sulfhydryl (SH) groups

The total and reactive sulfhydryl groups were measured according to the methods of Ellman (1959). Three replicates were performed for each sample.

Surface hydrophobicity

The surface hydrophobicity (S0) of myofibrillar protein was measured according to the methods of Yongsawatdigul and Park (2003).

Zeta potential and particle size

One milliliter myofibrillar protein solution (1 mg/mL) with 1%, 2% and 3% (weight/weight) sodium chloride was encased in a Zeta cell, respectively. The Zeta potential and particle size were measured by a zetasizer (Zetasizer v7.11, Malvern Instruments Ltd. UK).

Cooking yield

After at 2 ± 2 °C overnight, the loss water of cooked myofibrillar protein was separated. The cooking yield of myofibrillar protein was calculated using the following formula:

Cooking yield of myofibrillar protein (%) = Weight of myofibrillar protein before cooking—Weight of loss water/Weight of myofibrillar protein before cooking × 100%.

Textural measurement

After at 2 ± 2 °C overnight, the cooked myofibrillar protein gels were stay 2 h at room temperature, then the gels were cut into the cylindrical-shaped (diameter, 6 mm; height, 6 mm). The texture profile analysis was measured by the TA-XT plus texture analyzer with a probe P/36R (Stable Micro Systems, UK) at room temperature. The parameters were as follows: test speed, 2.0 mm/s; trigger type, auto-5 g; and strain, 50%. Five replicates were performed for each sample.

Raman spectroscopic

Raman experiments were determined according to the method of Kang et al. (2017) and Zhu et al. (2018). Spectra were smoothed, baselines corrected and normalized against the phenylalanine band at 1003 cm−1 (Herrero et al. 2008) using Labspec version 3.01c (Horiba/Jobin. Yvon, Long-jumeau, France). The secondary structures of the cooked pork myofibrillar protein were determined as percentages of α-helix, β-sheet, β-turn, and random coil or unordered conformations (Alix et al. 1988). With this aim, the water spectrum was subtracted from the spectra by following the same criteria as that described previously (Alix et al. 1988; Herrero et al. 2008).

Statistical analysis

The experiment was four replications. The data was analyzed by a one-way analysis of variance program using the SPSS v.18.0 for windows. Significant differences between means were identified by Duncan’s multiple range test (p < 0.05).

Results and discussion

SH group

Sulfhydryl group is the most reactive functional group in myofibrillar protein. It is the major functional key to maintain the three levels structures of proteins, and the changes of SH group is closely related to protein denaturation (Omana et al. 2011). Figure 1 shows the effect of total and reactive SH groups of myofibrillar protein with different sodium chloride. It can be seen that the content of reactive SH group was increased significantly (p < 0.05) with the increase of sodium chloride, but the reactive SH groups of 2% and 3% treatments were not difference significant (p > 0.05). Meanwhile, the total SH groups were not difference significant (p > 0.05) in all treatments. Increased the sodium chloride, resulting in a decrease of the repulsive force between the protein molecules, which leaded to the solubility of myofibrillar protein was increased. The force between the inter-molecular protein molecules was destroyed, more buried active SH groups were exposed through protein unfolding, resulting in the increase of reactive SH content (Omana et al. 2011; Zhang et al. 2015).

Fig.1.

Fig.1

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Effect of sodium chloride on total and reactive sulfhydryl (SH) of pork myofibrillar protein. 1%: 1% sodium chloride; 2%: 2% sodium chloride; 3%: 3% sodium chloride. Each value represents the mean ± SD, n = 4. a−cDifferent parameter superscripts in the figure indicate significant differences (p < 0.05)

Surface hydrophobicity

Surface hydrophobicity is an important factor which could reflect the changes of myofibrillar protein conformation and structure from its original structure (Nyaisaba et al. 2019). Omana et al. (2011) reported that the higher of S0 value suggested the stronger hydrophobic interaction of protein molecules. The effect of sodium chloride on surface hydrophobicity of myofibrillar protein is shown in Table1. The surface hydrophobicity of 1% and 2% treatments were not significant difference (p > 0.05), and the 3% treatments had the largest surface hydrophobicity. The possible reason was that more myofibrillar protein was unfolded with the sodium chloride increased, which influenced the exposes of amino acids. Then the exposure of interior hydrophobic residues in protein molecules leaded to increase protein hydrophobicity (Guo and Xiong 2019) Zhang et al. (2017a, b.) found that the increase of hydrophobicity of myofibrillar protein was induced through strong electrostatic interactions, which could prevent aggregation. The result was agreement with Zhang et al. (2009), whose showed that the surface hydrophobicity of the chickpea protein isolate increased with the increase of ionic strength (from 0.2 to 1.0 mol/L). Kaewmanee et al. (2011) reported that higher content of sodium chloride had a positive effect on surface hydrophobicity. The other reason was possible that the protein dissolved and unfolded with the increase of salt concentration, the non-polar amino acid was exposed, and the hydrophobicity of myofibrillar protein increased (Jia et al. 2015).

Table 1.

Effect of sodium chloride on surface hydrophobicity, particle size, Zeta potential and cooking yield of pork myofibrillar protein

Sample Surface hydrophobicity Zeta potential (mV) Particle size (nm) Cooking yield (%)
1% 11.52 ± 0.47b -7.37 ± 1.62b 1460.22 ± 363.70a 50.41 ± 1.26c
2% 12.44 ± 0.38b -5.35 ± 0.80a 962.36 ± 125.65b 65.27 ± 1.75b
3% 21.51 ± 1.71a -5.23 ± 0.95a 411.80 ± 54.39c 69.57 ± 1.52a
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1%: 1% sodium chloride; 2%: 2% sodium chloride; 3%: 3% sodium chloride. Each value represents the mean ± SD, n = 4

a−c Different parameter superscripts in the table indicate significant differences (p < 0.05)

Zeta potential and particle size

The effects of different sodium chloride on the Zeta potential and particle size of the myofibrillar protein are shown in Table 1. Compared with the 1% sodium chloride, the Zeta potential absolute values of 2% and 3% were decreased significantly (p < 0.05), but they were not significant difference (p > 0.05) between 2 and 3%. The result was agreement with Zhang et al. (2015), who found that the Zeta potential absolute values of myofibrillar protein gel were decreased with the increase of sodium chloride. The decrease of Zeta potential absolute values implied that the electrostatic interaction of the myofibrillar protein was reduced under the higher ionic strength, and facilitated the interaction of the protein molecular. The results showed that ionic strength could alter the charge of the protein and play an important role in it, which could be lower or enhance the properties of myofibrillar protein (Shen et al. 2019a, b).

High sodium chloride influenced the aggregation behaviors of meat proteins. The particle size could reflect the aggregation degree of myofibrillar protein with different sodium chloride. The particle sizes of myofibrillar protein were decreased from 1460.22 to 411.80 nm with the sodium chloride increased from 1 to 3%. Electrostatic interactions were usually repulsive in the process of protein aggregation, and the Zeta potential was negative, indicating that myofibrillar protein was negatively charged. Thus, the solubility was increased with the increase of sodium chloride.

Cooking yield

Cooking yield is reflect of the ability of myofibrillar protein to bind water during heating, which has an important impact on their process ability. As shows in Table 1, the changes observed in cooking yield of myofibrillar protein were mainly related to various amounts of sodium chloride. The cooking yield was significantly increased (p < 0.05) with the increase of sodium chloride. That indicated that the increase of sodium chloride was obviously improved the water holding capacity of myofibrillar protein gel. Because the myofibrillar protein is salt soluble protein of muscle, the solubility was increased with the increase of sodium chloride, and formed good gel structure during heated (Kang et al. 2016). The result was similar to Bertram et al. (2004), whose reported that the cooking yield of the myofibrillar protein gel was significantly increased with the ionic strength increased from 0.29 and 0.71 mol/L. At low salt concentration (< 0.2 mol/L), the myofibrillar protein is mainly in filament state and protein solubility was poor, which caused the cooking yield of gel was lower. On the contrary, myofibrillar protein dissolved from the filament state into monomeric at high salt concentration.

Texture

Texture profile analysis parameters of myofibrillar protein gel were effected by the various amounts of sodium chloride is showed in Table 2. The texture profile analysis parameters of myofibrillar protein gels were difference significant (p < 0.05) with the increase of sodium chloride. The hardness and springiness were increased significantly (p < 0.05) from to 68.44 ± 1.52 g to 451.27 ± 27.37 g, 0.72 ± 0.03 to 0.95 ± 0.02, respectively, but the springiness of 2% and 3% were not difference significantly (p > 0.05). Hong et al. (2017) reported that the hardness and springiness of the pork myofibrillar protein gels were improved with the increase of salt concentration. The changes of cohesiveness had a similar trend with the springiness. The possible reason was that added 2% sodium chloride could be sufficient to extract myofibrillar protein and form the gel structure. The chewiness was increased significantly (p < 0.05) with the sodium chloride increased. Geun and Koo (2010) reported that the texture of the porcine myofibrillar protein gel was improved with the increase of salt level. Due to the solubility of myofibrillar protein was increased with the increase of sodium chloride, and the dissolution of the protein could be better to participate in the formation of the gel, resulting in improving the texture of the gel (Ke and Hultin 2005). In addition, the stability of the myosin might be reduce by the addition of sodium chloride, which made it easier to form a thermal induced gel.

Table 2.

Effect of sodium chloride on texture characteristics of heat-induced pork myoflbrillar protein gel

Sample Hardness (g) Springiness Cohesiveness Chewiness (g mm)
1% 68.44 ± 1.52c 0.72 ± 0.03b 0.39 ± 0.01b 18.90 ± 1.79c
2% 236.23 ± 17.81b 0.92 ± 0.01a 0.43 ± 0.06b 93.10 ± 17.95b
3% 451.27 ± 27.37a 0.95 ± 0.02a 0.67 ± 0.00a 285.10 ± 21.44a
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1%: 1% sodium chloride; 2%: 2% sodium chloride; 3%: 3% sodium chloride. Each value represents the mean ± SD, n = 4

a−cDifferent parameter superscripts in the table indicate significant differences (p < 0.05)

Raman spectroscopic analysis

The percentages of secondary structures and the bands of Amide I of cooked myofibrillar protein gels with different sodium chloride is shown in Fig. 2 and Table 3. The strongest intensity bands of Amide I in the Raman spectra of 1%, 2% and 3% sodium chloride were the 1660 cm−1, 1660 cm−1, and 1661 cm−1, respectively. The β-sheet structure was significantly increased (p < 0.05) when the sodium chloride increased from 2 to 3%, but the 1% and 2% were not difference significant (p > 0.05). The content of the α-helix, β-turn and random coil structures were significantly decreased (p < 0.05), that implied the α-helix, β-turn and random coil structures were sensitive to the changes of sodium chloride. The main reason was that more myofibrillar protein were dissolved, more buried residues in the protein molecules were exposed to the water molecules and formed new hydrogen bonds when the sodium chloride was increased, those induced the α-helix structure transformed into β-sheet structure during the protein denaturation (Kang et al. 2014). The result was agreement with the result of particle size (Table 1), the lower degree of aggregation was to the benefit of forming hydrogen bonding between protein–protein, thus, more α-helix structure changed into β-sheet structure during protein denaturation with sodium chloride increased (Li et al. 2020a, b). The β-sheet structures were the base on myofibrillar proteins aggregate and gel form (Zhu et al. 2018). Therefore, the result implied when increased the sodium chloride could change the secondary structural, especial increased the β-sheet structure content.

Fig. 2.

Fig. 2

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Raman spectra of cooked pork myofibrillar protein gels with different sodium chloride content in the region 1600–1700 cm−1. 1%: 1% sodium chloride; 2%: 2% sodium chloride; 3%: 3% sodium chloride

Table 3.

Effect of sodium chloride on percentages of protein secondary structures content (%) and normalized intensities of the 760 cm−1 (tryptophan) band and tyrosyl doublet at 850/830 cm−1 of heat-induced pork myoflbrillar protein gel

Sample α-Helice S β-Turn Random coil
1% 27.26 ± 2.39a 44.52 ± 1.29b 14.32 ± 0.45a 13.36 ± 0.38a
2% 26.17 ± 2.16a 45.63 ± 1.31b 14.64 ± 0.43a 12.82 ± 0.41a
3% 24.73 ± 2.27ab 47.50 ± 1.43a 15.03 ± 0.41a 12.63 ± 0.39a
Open in a new tab

1%: 1% sodium chloride; 2%: 2% sodium chloride; 3%: 3% sodium chloride. Each value represents the mean ± SD, n = 4

a−b Different parameter superscripts in the table indicate significant differences (p < 0.05)

Conclusion

The proteins aggregation and conformation were significantly affected the cooking yield and texture property of pork myofibrillar protein gel with different sodium chloride. When the sodium chloride was increased, the surface hydrophobicity, total SH, β-sheet structure, cooking yield and hardness of pork myofibrillar were significantly increased, and the particle size and α-helix structure were significantly decreased. The results indicated that smaller particle size, lower α-helix structure content, more surface hydrophobicity, total SH and β-sheet structure content were beneficial to form a better gel of pork myofibrillar protein during heating.

Acknowledgements

This study was supported by China Postdoctoral Science Foundation (no. 2016M602237) and Henan province key young teachers training program (no. 2018GGJS114), National Natural Science Foundation of China (NSFC, Grant No. 31501508).

Compliance with ethical standards

Conflicts of interest

The authors declare that they have no conflict of interest involved in this work.

Ethical review

This study does not involve any human or animal testing.

Informed consent

All the authors, who contributed to this work, have reviewed the final version of the manuscript, and agree to submit it for consideration in the journal.

Footnotes

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