Gel Properties Of Myofibrillar Protein Research Articles

Effect of Different Addition Amounts of Capsaicin on the Structure, Oxidation Sites, and Gel Properties of Myofibrillar Proteins under Oxidative Conditions.

This study aimed to explore the mechanism influencing different addition amounts of capsaicin on the gel characteristics and microstructure of myofibrillar protein (MP) gels under conditions induced by hydroxyl free radicals (•OH). Results indicate that adding capsaicin can improve the gelling characteristics of the MPs. With an increased amount of capsaicin added, the oxidation of MPs by •OH decreased, and the number of oxidation sites decreased. Peptides located around residues 651-851 in the head domain SH1 and S2 subunits of the myosin heavy chain were susceptible to oxidation. Capsaicin primarily interacted with amino acids in SH1 (residues 1-151 and 601-651), reducing the effect of •OH on MPs and consequently decreasing the occurrence of MP aggregation. Capsaicin protected the structure and oxidation sites of MPs under oxidative conditions, ensuring the formation of an MP gel with uniformly dense pores during heating, thereby improving the texture characteristics and water-holding capacity of the gel.

The improved gel properties of myofibrillar protein under low salt condition by ultrasound-assisted sodium tripolyphosphate

Excessive salt intake is associated with increased risks of cardiovascular disease, while directly reducing salt content significantly decreased the quality of meat. The objective of this study was to investigate the synergistic effects of sodium tripolyphosphate (STP) and ultrasound treatment on the gel properties of MP under low-salt conditions (0.3 M NaCl). The results of FTIR spectra showed that P3O105− group of STP bound to -NH2 or -OH group of MP form C-N-P or C-O-P bond, indicating the STP was successfully introduced to MP. The addition of STP significantly increased the absolute value of Zeta-potential, suggesting that the presence of STP increased the electrostatic interaction of MP-MP. Importantly, STP combined with ultrasound treatment under low salt condition (STP-U0.3) significantly increased solubility and decreased particle size of MP. Besides, STP-U0.3 treatment also promoted the exposure of hydrophobic groups and improved the rheological behavior of MP, resulting in the highest gel strength (37.78 ± 0.71 g) and the lowest cooking loss (26.73 ± 0.90 %) especially in 10 mM STP combined 100 W ultrasound treatment. These results corresponded by the gradually increases of α-helix content and the decrease of tryptophan fluorescence intensity. Furthermore, results of SEM illustrated that STP-U0.3 treatment contributed to formation of more homogeneous and dense gel network of MP gel. The above results displayed that the STP-U treatment under 0.3 M NaCl resulted in an equivalent effect to control group of 0.6 M NaCl, indicating that the combined application of STP and ultrasound has a promising potential in the low-salt meat processing industry.

Effect of chitosan oligosaccharides with different molecular weight in alleviating textural deterioration of chicken myofibrillar protein gel with high-temperature treatment

The molecular weight (MW) of oligosaccharides on gel properties of myofibrillar protein (MP) at high temperature remains unclear. In this study, it was found that chitosan oligosaccharides (CO) with different MW all significantly alleviated the textural deterioration of MP gel with high-temperature treatment. Moreover, MP-CO gel with the largest MW had the highest breaking force and the lowest cooking loss. Low-field NMR results further indicated that MP-CO gel with larger MW of CO had gradually increased relaxation rate, thus binding water more tightly. Rheological and microrheological tests suggested the addition of CO with larger MW resulted in much tighter gel network. These results indicated that CO with larger MW improved the quality of MP gel more effectively, which was because CO with larger MW inhibited aggregation of MP to a larger extent, resulting in smaller MP aggregates. Then MP-CO gel with much denser and more homogeneous structure was formed. Besides, MP-CO gel with larger MW of CO had higher content of β-sheet, resulting in MP gel with more ordered structure and better gel quality. Therefore, this study provided theoretical guidance for choosing the appropriate CO in improving texture of high temperature meat products.

Effect of chitosan on thermal gelling properties of pork myofibrillar protein and its mechanism.

Previous studies have demonstrated that the addition of chitosan can improve the quality and functional properties of meat products. However, the underlying mechanism remains unclear. In this study, the effect and mechanism of the addition of chitosan on the gel properties of myofibrillar protein (MP) were investigated. The results indicated that the gel strength and the water-holding capacity of MP-chitosan gel increased significantly when chitosan was added at 2.5-10 mg mL-1. Myofibrillar protein samples with 10 mg mL-1 added chitosan exhibited the highest elasticity and viscosity during gel formation and strengthening. The addition of chitosan also caused a modification in both the secondary and tertiary structure of MP, resulting in an enhanced exposure of hydrophobic and sulfhydryl groups in comparison with the control. Chitosan inhibited the conversion of immobilized water into free water and the formation of water channels during the thermal gelation process of MP. The denaturation enthalpy (ΔH) of myosin decreased as the concentration of chitosan exceeded 5 mg mL-1. The microstructure showed that the incorporation of chitosan (5-10 mg mL-1) facilitated the formation of compact and well organized MP gel networks. The addition of chitosan can enhance the functional properties of meat protein and facilitate heat-induced gelation, making it a promising ingredient for improving the quality of processed meat products. © 2024 Society of Chemical Industry.

Effect of lipoxygenase-catalyzed linoleic acid oxidation and 4-hydroxy-2-nonenal on digestibility and gel properties of myofibrillar protein

The oxidative modification of myofibrillar proteins (MPs) has been identified as a crucial factor affecting meat quality during processing. We compared the effects of 4-hydroxy-2-nonenal (HNE) and lipoxygenase (LOX)-catalyzed linoleic acid (LA) oxidation products on the digestibility and gel properties in MPs from bighead carp. Both treatments resulted in decreased free amino acid content, reduced digestibility, and loss of amino acids in MPs. The HNE treatment enhanced gel strength by increasing hydrophobic interactions within the gel matrix. Conversely, the LOX-catalyzed LA oxidation enhanced disulfide bonds, leading to an agglomerated microstructure. Reduced myofibrillar protein (MP) solubility, primarily due to protein aggregation, was observed in the LA group but not in the HNE group. This distinction suggests that the impact on MP functionality is predominantly influenced by the protein aggregation induced by LOX-catalyzed LA oxidation rather than by HNE alone.

Molecular mechanism of acetylated distarch phosphate with pea protein isolate to improve the gel quality of myofibrillar protein gel

AbstractIt is crucial to improve the gel properties of myofibrillar protein (MP) in the production of surimi products. This study investigated the effects of combining acetylated distarch phosphate (ADSP) with pea protein isolate (PPI) as exogenous additives on the physicochemical properties of Larimichthys crocea MP gel and elucidated the molecular mechanisms underlying the improvement of MP gel quality. The results showed that the mixture of 3% ADSP and 1% PPI increased the MP gel strength to 2.1 times and water holding capacity to 1.8 times. The rheological properties during thermal‐induced gelation were improved, and the surface roughness of gel microstructure was reduced. The protein conformation was stabilized by enhancing surface hydrophobicity and sulfhydryl content, and the gels showed trends of decreasing α‐helix and increasing random coils. Correlation and cluster analysis showed that physicochemical properties of MP gels were closely related to the changes of protein structure and the denaturation of active groups. The molecular interaction between ADSP, PPI, and MP and the mechanism of enhancing the properties and functions of MP gel were further clarified. These findings highlight the feasibility of ADSP–PPI as an effective strategy to improve the quality of fish MP gel.

Effect of γ-oryzanol/β-sitosterol-based oleogels on the physicochemical and gel properties of Nemipterus virgatus myofibrillar protein.

The effect of oleogels prepared with peanut oil and different concentrations of γ-oryzanol and β-sitosterol mixture (γ/β; 20, 40, 60, 80 and 100 g kg-1) on the physicochemical and gel properties of myofibrillar protein (MP) was investigated. The solubility and average particle size of MP first decreased and then increased with increasing γ/β concentration. Peanut oil or oleogels could induce the exposure of hydrophobic amino acids and the unfolding of MP, thus significantly increasing the surface hydrophobicity, sulfhydryl content and absolute value of zeta potential, which reached maximum values when the γ/β concentration was 60 g kg-1 (P < 0.05). The addition of peanut oil decreased the gel strength and water holding capacity of MP gel. However, oleogels prepared with 60 g kg-1 γ/β could significantly increase the hydrophobic interactions and disulfide bond content of MP gel (P < 0.05), which promoted the crosslinking and aggregation of MP, enhancing the gel properties. Peanut oil had no significant influence on the secondary structure of MP, while oleogels promoted the transition of MP conformation from α-helix to β-sheet structure. The results of light microscopy and confocal laser scanning microscopy indicated that oleogels prepared with 60 g kg-1 γ/β filled in the pores of MP gel network to form denser and more uniform structure. Oleogels prepared with 60 g kg-1 γ/β could effectively improve the quality of MP gel and have promising application prospects in surimi products. © 2024 Society of Chemical Industry.

Effects of high-intensity ultrasound on physicochemical and gel properties of myofibrillar proteins from the bay scallop (Argopecten irradians)

Myofibrillar proteins (MPs) have a notable impact on the firmness and flexibility of gel-based products. Therefore, enhancing the gelation and emulsification properties of scallop MPs is of paramount significance for producing high-quality scallop surimi products. In this study, we investigated the effects of high-intensity ultrasound on the physicochemical and gelation properties of MPs from bay scallops (Argopecten irradians). The carbonyl content of MPs significantly increased with an increase in ultrasound power (150, 350, and 550 W), indicating ultrasound-induced MP oxidation. Meanwhile, high-intensity ultrasound treatment (550 W) enhanced the emulsifying capacity and the short-term stability of MPs (up to 72.05 m2/g and 153.05 min, respectively). As the ultrasound power increased, the disulfide bond content and surface hydrophobicity of MPs exhibited a notable increase, indicating conformational changes in MPs. Moreover, in the secondary structure of MPs, the α-helix content significantly decreased, whereas the β-sheet content increased, thereby suggesting the ultrasound-induced stretching and flexibility of MP molecules. Sodium-dodecyl sulfate–polyacrylamide gel electrophoresis and scanning electron microscopy analysis further elucidated that high-intensity ultrasound induced MP oxidation, leading to modification of amino acid side chains, intra- and intermolecular cross-linking, and MP aggregation. Consequently, high-intensity ultrasound treatment was found to augment the viscoelasticity, gel strength, and water-holding capacity of MP gels, because ultrasound treatment facilitated the formation of a stable network structure in protein gels. Thus, this study offers theoretical insights into the functional modification of bay scallop MPs and the processing of its surimi products.

Effect of starch and peanut oil on physicochemical and gel properties of myofibrillar protein: Amylose content and addition form

Starch and peanut oil (PO) were widely used to improve the gel properties of surimi, however, the impact mechanism of addition forms on the denaturation and aggregation behavior of myofibrillar protein (MP) is not clear. Therefore, the effect of starch, PO, starch/PO mixture, and starch-based emulsion on the physicochemical and gel properties of MP was investigated. The results showed that amylose could accelerate the aggregation of MP, while amylopectin was conducive to the improvement of gel properties. The addition of PO, starch/PO mixture, or starch-based emulsion increased the turbidity, solubility, sulfhydryl content of MP, and improved the gel strength, whiteness, and texture of MP gel. However, compared with starch/PO mixture group, the gel strength of MP with waxy, normal and high amylose corn starch-based emulsion increased by 22.68 %, 10.27 %, and 32.89 %, respectively. The MP containing emulsion had higher storage modulus than MP with starch/PO mixture under the same amylose content. CLSM results indicated that the oil droplets aggregated in PO or starch/PO mixture group, while emulsified oil droplets filled the protein gel network more homogeneously. Therefore, the addition of starch and PO in the form of emulsion could effectively play the filling role to improve the gel properties of MP.

Impact of Flammulina velutipes polysaccharide on properties and structural changes of pork myofibrillar protein during the gel process in the absence or presence of oxidation

The present study aimed to investigate the impact of Flammulina velutipes polysaccharide (FVSP) on the rheological properties and structural alterations of myofibrillar protein (MP) and oxidized MP (OMP), utilizing techniques such as rhehometer, fourier transform infrared spectroscopy (FTIR), scanning electron microscopy (SEM), and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). In the unoxidized system, the addition of 5.00% FVSP significantly improved (p < 0.05) the storage and loss moduli of the composite gel and promoted the α-helix to β-sheet transformation. These effects enhanced the protein's gel strength and water-holding capacity (WHC). In the oxidation system, 5.00% FVSP had significant effects (p < 0.05) on repair and improvement of the oxidized MP. These effects inhibited the cross-linking aggregation and degradation of the protein. In addition, the addition of FVSP significantly improved the gel properties of MPs after oxidation (p < 0.05), hindered fracture of the protein gel network structure. In summary, polysaccharides have a substantial effect on the functional characteristics of MP, and FVSP could potentially be applied in meat products.

Inhibition of the interactions of myofibrillar proteins with gallic acid by β-cyclodextrin-metal-organic frameworks improves gel quality under oxidative stress

Generally, high levels of natural phenolic antioxidants, which are needed in meat products to exert equivalent antioxidant effects as synthetic antioxidants, can interact with myofibrillar proteins and cause aggregation of the proteins, giving rise to undesirable deterioration of gel quality. In this study, β-cyclodextrin-metal-organic frameworks (K-β-CD-MOFs) were synthesized based on β-CD and K+ ions using methanol vapor diffusion method, and used to inhibit excessive covalent and non-covalent interactions between gallic acid (GA) and myofibrillar proteins under oxidative stress without degrading the phenolic antioxidant activity. Results of zeta potential, scanning electron microscope (SEM), X-ray diffraction (XRD), Fourier transform infrared spectroscopy (FT-IR), and differential scanning calorimetry (DSC) provided evidence for the formation of GA/K-β-CD-MOFs inclusion complexes. From sulfydryl content, surface hydrophobicity, tryptophan fluorescence, turbidity and particle size analyses, the presence of K-β-CD-MOFs dose-dependently prevented the sulfydryl loss, unfolding of the proteins and formation of insoluble aggregates caused by GA (180 μM/g protein). Dynamic rheology, cooking loss, gel strength, water distribution, microstructure and Raman spectrum were further tested to evaluate effects of K-β-CD-MOFs on the qualities of GA-treated myofibrillar protein gel. Results indicated that more proteins were involved in the formation of a more ordered and homogeneous gel structure with higher gel elasticity and strength, more immobilized water and decreased cooking loss. The overall gel properties of myofibrillar proteins were improved. K-β-CD-MOFs ameliorated the instability of protein structure, manifested as increase in β-sheet content and inter-chain hydrogen bonding and decrease in hydrophobic forces (p < 0.05). This paper provides a novel method to increase the loading amount of phenolic antioxidants without jeopardizing the gel quality of meat products.

A novel EGCG-Histidine complex improves gelling and physicochemical properties of porcine myofibrillar proteins: Insight into underlying mechanisms

Herein, an EGCG-Histidine complex is prepared, characterized, and further used to improve gel properties of myofibrillar proteins (MP). Results of FTIR, XRD, UV–Vis spectroscopy showed that histidine is covalently bound to EGCG by Michael addition or Schiff base reaction to form EGCG-Histidine complex, and antioxidant activity of EGCG-Histidine complex is significantly increased compared to EGCG or histidine alone (P < 0.05). The addition of EGCG-Histidine complex results in cooking loss of gel decreasing from 66.7 ± 0.23 % to 40.3 ± 2.02 %, and improves rheological properties of MP, and enhances gel strength from 0.10 ± 0.01 N to 0.22 ± 0.03 N, indicating positive effect of EGCG-Histidine complex on MP gel formation, above results is supported by results of SEM, CD spectroscopy, SDS-PAGE, and tryptophan fluorescence. These results indicated that EGCG-Histidine complex can be used as a functional ingredient to improve gel quality of meat products.

Insight into the Effects of Hydrodynamic Cavitation at Different Ionic Strengths on Physicochemical and Gel Properties of Myofibrillar Protein from Tilapia (Oreochromis niloticus).

Effects of different ionic strengths (0.2, 0.4, and 0.6 mol/L) and different hydrodynamic cavitation (HC) treatment times (0, 1, 2, 3, and 4 min) on the conformation and gel properties of tilapia myofibrillar proteins (TMP) were investigated. The results showed that the solubility of TMP was significantly enhanced (p < 0.05) with the increase in NaCl concentration, and the gel characteristics were significantly improved. After HC treatment of TMP, the average particle size was significantly reduced (p < 0.05) and solubility was significantly enhanced (p < 0.05) with the increase in treatment time, the internal hydrophobic groups and reactive sulfhydryl groups were exposed. The intrinsic fluorescence spectra showed the unfolding of the spatial tertiary structure of proteins, and the circular dichroism spectroscopy showed the significant reduction in the content of α-helix in the secondary structure of the proteins (p < 0.05). In addition, the WHC and gel strength of the TMP heat-induced gels were enhanced, which improved the microstructure of the gels, and scanning electron microscopy showed that the gel network of the TMP gels became denser and more homogeneous. Dynamic rheology results showed that HC treatment resulted in a significant increase in the final G' and G" values of TMP. In conclusion, HC treatment was able to improve the physicochemical structure and gel properties of TMP at different ionic strengths. This study presents a novel processing technique for the quality maintenance aspect of salt-reduced surimi gel products.

Perilla seed oil high internal phase emulsion improve the gel properties of myofibrillar protein

The effects of perilla seed oil high internal phase emulsions stabilized by pea protein (PP-PSO HIPEs) on the gel properties and conformation of myofibrillar protein (MP) gels were investigated. The results showed that the PP-PSO HIPEs with 4.0 % (w/v) PP formed stable HIPEs with low droplet size and good viscoelasticity. The addition of PP-PSO HIPEs (5.0 % − 15.0 %) could significantly improve the MP gel properties (P < 0.05), while the addition of 10.0 % PP-PSO HIPEs showed the highest gel strength and water holding capacity. Otherwise, the MP gels with 10.0 % PP-PSO HIPEs showed higher proportions of immobile water (PT22) and lower proportion of free water (PT23), and the Raman spectra suggested that the content of α-helix decreased, while the content of β-sheet increased (P < 0.05), thus facilitating the formation of better gel properties. Therefore, the addition of PP-PSO HIPEs is a potential alternative for developing fat-reduced meat products.

Paramyosin from field snail (Bellamya quadrata): Structural characteristics and its contribution to enhanced the gel properties of myofibrillar protein

To assess the blending effect of field snails with grass carp muscle, the effects of paramyosin (PM) and actomyosin (AM) with different mixture ratios on the gel properties of the binary blend system were investigated in our work. The purified PM from field snail muscle was about 95 kDa on SDS-PAGE. Its main secondary structure was α-helix, which reached to 97.97 %. When the amount of PM increased in the binary blend system, their rheological indices and gel strength were improved. The water holding capacity (WHC) increased to 86.30 % at a mixture ratio of 2:8. However, the WHC and the area of immobile water (P22) dramatically decreased, and the area of free water (P23) increased when the mixture ratio exceeded 4:6. The low level of PM in binary blend system promoted the formation of a homogenous and dense gel network through non-covalent interactions as observed results of SEM and FTIR. When there were redundant PM molecules, the development of heterostructure via hydrophobic interaction of tail-tail contributed to the reduced gel properties of the binary blend system. These findings provided new insight into the binary blend system of PM and AM with different ratios to change the gel properties of myofibrillar protein.

Effects of calcium chloride on the gelling and digestive characteristics of myofibrillar protein in Litopenaeus vannamei

In this study, the effects of CaCl2 (0, 25, 50, 75, and 100 mM) on the gelling and digestive properties of the myofibrillar protein (MP) in Litopenaeus vannamei were investigated. The results showed that increasing CaCl2 concentration led to changes in the tertiary structure of MP. Specifically, compared with the control group, a 64.31 % increase in surface hydrophobicity and a 45.90 % decrease in the sulfhydryl group were observed after 100 mM CaCl2 treatment. Correspondingly, the water holding capacity and strength of the MP gel increased by 24.46 % and 55.99 %, respectively. These changes were positively correlated with the rheological properties, microstructure pore size, and content of non-flowable water. The mechanical properties of MP gel were improved, and the microstructure became more compact with the increase in CaCl2 concentration. Furthermore, the particle size of the digested MP gels decreased in the presence of CaCl2, which improved the digestion characteristics of MP gels.

Effects and mechanisms of different κ-carrageenan incorporation forms and ionic strength on the physicochemical and gelling properties of myofibrillar protein

The present work was aimed to investigate the effects of incorporating κ-carrageenan into myofibrillar protein (MP) as a dry powder (CP) or water suspension (CW) and the ionic strength (0.3 or 0.6 M sodium chloride (NaCl)) on MP physicochemical and gelling properties. The results indicated that incorporation of either CP or CW significantly increased turbidity, surface hydrophobicity, particle size and rheological behaviour of MP. In contrast, the protein solubility and fluorescence intensity of MP decreased when added with each form of κ-carrageenan (P < 0.05). These observed effects improved MP's gelling properties and produced a more compact and homogenous gel network after heating treatment. Moreover, the addition of CW rendered higher gel strength, water holding capacity and intermolecular interactions, such as ionic, hydrogen and disulphide bonds and hydrophobic interactions in MP gel compared with those added with CP, especially for 0.3 M NaCl (P < 0.05). Furthermore, addition of CW significantly decreased the α-helix content of MP gels (P < 0.05), which mainly contributing to the transformation from a random structure to an organised configuration. In addition, a higher NaCl concentration (0.6 M) enhanced the gelling properties of MP gels compared with 0.3 M NaCl concentration in the presence of each form of κ-carrageenan. Therefore, our present study indicated that incorporation form of κ-carrageenan and ionic strength have distinctive effects on regulating physicochemical characteristics and improves gelling properties of MP.

Study of four polyphenol-Coregonus peled (C. peled) myofibrillar protein interactions on protein structure and gel properties

The effects of four polyphenols—chlorogenic acid (CA), gallic acid (GA), epicatechin gallate (ECG), and epigallocatechin gallate (EGCG) on the structure, gel properties, and interaction mechanisms of myofibrillar protein (MP) were studied. The changes in MP structure with polyphenols were analyzed using circular dichroism. The ultraviolet and fluorescence spectra and thermodynamic analysis indicated that the type of binding between the four polyphenols with the MP was static quenching of complex formation. GA had a more pronounced effect on improving MP gel properties. Finally, molecular docking determined that the affinity of the protein with the four polyphenols was in the order EGCG > ECG > CA > GA, with the main interaction force being hydrophobic interactions and hydrogen bonding, but hydrogen bonding dominates the interaction between GA and the protein. The findings illuminate the mechanism of MP binding to different polyphenols and facilitate the study of polyphenol–protein properties.

Effects of exopolysaccharide by Pediococcus acidilactici S1 on the gelation properties and microstructure of porcine myofibrillar protein

The utilization of extracellular polysaccharides (EPS) derived from lactobacilli is widely observed in the dairy and cereal sectors, whereas their implementation in meat products has received limited research attention. This study was to enhance the utilization of EPS from Pediococcus acidilactici S1 (S1-EPS) in the meat industry and optimize the gel properties of myofibrillar protein (MP)-based food systems. In the study, the impact of incorporating S1-EPS on the properties of MP gels was investigated, revealing significant improvements in water retention, strength, textural characteristics, and rheological behavior. Furthermore, it was observed that S1-EPS facilitated myosin aggregation through hydrophobic interactions and induced a transition in the secondary structure and microstructure of MP from disorder to order. In molecular docking experiments, S1-EPS demonstrated stable binding to myosin through hydrogen bonding and robust electrostatic interactions, indicating its potential as a valuable gelling agent for meat products and contribution to the development of MP gel structure following heat treatment.

Effects of eugenol on the structure and gelling properties of myofibrillar proteins under hydroxyl radical-induced oxidative stress

The effects of eugenol (EG; 0, 5, 20, and 50 mg/g protein) on the structure and gel properties of pork myofibrillar protein (MPs) under a hydroxyl radical-generating system were explored in this study. The results revealed that the addition of a high concentration of EG (50 mg/g protein) markedly reduced the carbonyl content and enhanced the fluorescence intensity, surface hydrophobicity, and protected the secondary structure of MPs, compared to oxidized MPs. In addition, the high concentration group noticeably increased the storage modulus (G′), gel strength, and water-holding capacity (WHC), and significantly hindered the oxidation-induced transformation of immobilized water of the MPs gel to free water and basically favored the formation of a finer and more homogeneous three-dimensional network structure, This work verified that the adding of EG could effectively improve the gel quality of oxidized MPs and more successfully delay oxidation-induced damage to muscle protein structure.