Functional Properties Of Myofibrillar Proteins Research Articles

Mechanism of tumbling-curing to improve beef quality: Insights from the structural and functional properties of myofibrillar protein

Beef is highly nutritious but lacks tenderness and emulsification properties. This study aimed to investigate the impact of static curing (SC), tumbling-curing (TC), pulsating vacuum tumbling-curing (PVTC), and vacuum tumbling-curing (VTC) on the structural and functional properties of myofibrillar proteins and the mechanisms involved in enhancing beef quality. VTC significantly enhanced beef tenderness, water-holding capacity (WHC) and cooking yield. Additionally, the shear force was reduced by 58% and the cooking yield and WHC were increased by 6% compared with SC. There was an increase in the myofibrillar protein (MP) α-helix content and sulfhydryl content, while there was a reduction in the surface hydrophobicity and dityrosine content. These changes led to the enhancement of the functional properties of beef, such as protein emulsification and solubility. VTC minimized the damage caused by the curing process to the secondary and tertiary structures of MP by reducing their aggregation and oxidation. When compared with other curing methods, VTC proved to be an effective technology for enhancing beef tenderness and emulsification properties, therefore, essential in promoting ultra-processed beef products.

Role of ultrasonic freezing­treated pork dumpling filling during frozen storage: Insights from protein oxidation, aggregation, and functional properties

The effects of air freezing (AF), immersion freezing (IF), and ultrasonic freezing (UF) on the oxidation, aggregation, and functional properties of myofibrillar protein (MP) in pork dumpling filling during frozen storage were investigated. The findings demonstrated that, compared to AF and IF treatments, UF treatment had higher total and reactive sulfhydryl content, solubility, and absolute zeta potential. Conversely, it exhibited lower values in carbonyl content, dityrosine content, turbidity, and particle size within the same storage time (p < 0.05). SDS-PAGE revealed that UF treatment delayed the oxidation and excessive aggregation of MP during frozen storage. Moreover, samples treated with UF at 180 days (d) displayed similar functional and qualitative characteristics to those treated with IF at 90 d or AF at 60 d, as per the hierarchical cluster analysis findings. In conclusion, UF effectively delayed the oxidation, aggregation, and loss of functional properties of MP in pork dumpling filling during frozen storage.

Modifying duck myofibrillar proteins using sodium bicarbonate under cold plasma treatment: Impact on the conformation, emulsification, and rheological properties

This study aimed to explore the potential advantages of incorporating sodium bicarbonate to enhance the processing characteristics of duck myofibrillar proteins (MPs) during cold plasma treatment. Various concentrations of sodium bicarbonate (0%, 0.2%, 0.4%, and 0.6%) were examined for their impact on the structural, physicochemical, and functional properties of MPs under cold plasma treatment conditions (50 V, 3 min). Results indicated that sodium bicarbonate increased the unfolding of MPs, resulting in elevated active sulfhydryl content, enhanced surface hydrophobicity, intensified intrinsic fluorescence intensity, and reduced average particle size. Additionally, sodium bicarbonate significantly augmented (P < 0.05) α-helix and β-sheet content, leading to modifications in the microenvironments of tyrosine and tryptophan. Scanning electron microscopy and atomic force microscopy revealed that sodium bicarbonate effectively mitigated the protein aggregation induced by cold plasma treatment. Sodium bicarbonate induced secondary and tertiary structural alterations, enhancing the solubility of duck MPs, consequently improving their emulsifying and rheological properties. These findings suggest that sodium bicarbonate can effectively enhance the processing performance of duck MPs during cold plasma treatment, offering novel insights into the application of sodium bicarbonate in the cold plasma processing of duck products.

Structural changes induced by ultrasound improve the ability of the myofibrillar protein to bind flavor compounds from spices

Effects of ultrasound (UT) treatments on the structural, physicochemical, and functional properties of myofibrillar proteins (MPs), as well as their ability to bind to flavor compounds from spices, were investigated. The results demonstrated that UT treatment enhanced surface hydrophobicity, SH content, and absolute ζ-potential value of the MPs. Atomic force microscopy analysis displayed formation of MPs aggregates with small particle size in the UT-treated MPs samples. Meanwhile, UT treatment could improve the emulsifying properties and physical stability of MPs’ emulsion. Additionally, the MPs gel network structure and stability significantly improved following UT treatment. Changes in the structural, physicochemical, and functional properties enhanced the ability of MPs to bind to flavor substances from spices depending on the duration of UT treatment. Furthermore, correlation analysis showed that the ability of myristicin, anethole, and estragole to bind to MPs was highly correlated with surface hydrophobicity, ζ-potential value, and α-helix content of MPs. The results of this study may help in understanding the relationship between the changes in MPs properties during the processing of meat products and their ability to bind to flavors from spices, thereby improving flavors retention and taste of processed meat products.

Chemical and Functional Properties of Myofibrillar Protein from Selected Species of Trash Fish

Chemical and Functional Properties of Myofibrillar Protein from Selected Species of Trash Fish

Modification of the structure and function of myofibrillar protein by structurally relevant natural phenolic compounds

Protein gelation is an important functional characteristic of shrimp surimi products. The effects of structurally relevant natural phenolic compounds on the structure and functional properties of myofibrillar protein (MP) of the Penaeus vannamei were investigated. In the present study, phenolics improved the oxidative stability of MP, while leading to a decrease in the emulsification properties of MP. The carbonyl and free radical contents and fluorescence quantification of protein oxidation products showed that the addition of phenolic compounds could effectively prevent MP oxidation due to their antioxidant capacity derived from hydroxyl groups. In addition, phenolics could improve the rheological properties and gelling behavior of MP. Finally, the interactions between the substituents of MP and phenolic compounds were explored by molecular docking to elucidate the modification mechanism. Gallic acid (GA), quercetin (QT), and (−)-epigallocatechin-3-gallate (EGCG) interacted with MP mainly through hydrogen bonding to unfold the secondary structure of MP and reduce the surface hydrophobicity. Unlike GA and EGCG, QT interacted electrostatically with MP, maintaining the α-helical structure and leading to a slight increase in surface hydrophobicity. This study demonstrated the great potential of phenolic compounds as natural additives for the functional modification of shrimp surimi products.

DANA ETİ MİYOFİBRİLER PROTEİNLERİNİN FONKSİYONEL ÖZELLİKLERİ ÜZERİNE TUZ, FOSFAT ve PH’NIN ETKİLERİNİN ARAŞTIRILMASI

This study aimed to investigate the effect of salt and phosphate on the functional properties of myofibrillar proteins (MPs) at pH 2, 4, 6, 8, and 10. The highest emulsion activity index (EAI) value (8.51 m²/g protein) was obtained with the use of NaCl, and phosphate at pH 10. The highest emulsion stability index (ESI) result was determined (230.8 minutes) with the use of salt at pH 8. The addition of salt and phosphate significantly (p&amp;lt;0.05) improved the emulsifying properties of proteins. Considering the water absorption capacity (WAC), the highest value was obtained as 1.9 mL water/g protein at pH 6 and pH 8. The highest fat absorption capacity (FAC) value of 8.3 mL fat/g protein was found with the addition of phosphate at pH 6. The highest foam capacity (FC) and foam stability (FS) were obtained at pH 10 and 4, respectively.

Physicochemical and functional properties of the muscle protein fraction of Hypomesus olidus.

The physicochemical and functional properties of myofibrillar protein (MP), sarcoplasmic protein (SP), and myostromin (MY) in Hypomesus olidus muscle were evaluated and reported in this study. These fractions are rich in Glu. Three proteins exhibited significantly different morphologies, colors, and particle sizes. The main protein bands of MP, SP, and MY are 15-220kDa, 26-60kDa, and 15-245kDa, respectively. In particular, MP is more hydrophobic. Three proteins exhibited a maximum UV absorption peak at 270nm, and all amide I secondary structures were shown to be composed of repetitive units (e.g., α-helices and β-sheets). The three proteins demonstrated a predominantly amorphous halo, with Td values of 52.22°C, 59.16°C, and 58.09°C. Regarding their properties in water/oil absorption, emulsification, and foaming, MP is the most preferred, followed by SP and MY. In conclusion, Hypomesus olidus muscle proteins are novel and potential functional nutrition ingredients for the food industry.

Ultrasound-assisted freezing retards the deterioration of functional properties of myofibrillar protein in chicken breast during long-term frozen storage

Ultrasound-assisted freezing (UF) is a novel and fast freezing technology that has attracted much attention in the food processing industry in recent years. The objective of this study was to investigate the influence of UF, immersion freezing (IF), and air freezing (AF) on the functional properties (solubility, emulsification, and gelation) of myofibrillar protein (MP) in chicken breast during frozen storage (0–180 days). Compared to AF and IF samples, UF samples showed higher solubility, absolute potential, and emulsifying activity index, and lower turbidity and particle size during frozen storage (P < 0.05). Furthermore, UF treatment could better delay the deterioration of gel structure during storage. The gel water holding capacity and gel strength of MP in UF samples were higher than those in IF and AF samples during frozen storage (P < 0.05). The results of a hierarchical cluster analysis revealed that MP in the UF, IF, and AF samples had similar functional properties at 180, 90, and 60 days, respectively. Overall, UF retarded the decrease in functional properties of MP usually seen during frozen storage.

Explore the mechanism of continuous cyclic glycation in affecting the stability of myofibrillar protein emulsion: The influence of pH

Emulsifying properties are one of the important functional properties of myofibrillar protein (MP), and improving the stability of the MP emulsions under a wide range of pH conditions can help resist the effects of unfavourable acid–base factors during processing. Previously, the continuous cyclic wet heating glycation was carried out to successfully prepare the MP–glucose conjugates, and the present study explored mechanism of the conjugates to stabilize emulsions under different pH conditions. The results showed that MP aggregated by intermolecular hydrophobic interactions under acidic conditions, while electrostatic repulsion induced the stretching of molecular conformation, and the emulsifying performance was significantly (P < 0.05) improved under neutral and alkaline conditions. Compared with the control MP, the more flexible structures and higher solubility of glycated molecules promoted the adsorption at the oil–water interface with increasing pH, resulting in a more uniform distribution of smaller oil droplets, which enhanced the internal structures and improved the rheological properties of the emulsions; meanwhile, due to the stronger intermolecular electrostatic repulsion and the steric hindrance, the emulsions prepared by glycated MP exhibited better dynamic stability and storage stability, especially at pH 11.

Effects of selenium yeast and jujube powder dietary supplements on conformational and functional properties of post-mortem chicken myofibrillar protein.

The aim of the study was to evaluate the effects of selenium yeast and jujube powder on the structure and functional properties of post-mortem myofibrillar protein (MP) in white feather broilers. Changes in the structure (surface hydrophobicity, secondary structure, and tertiary structure), functional properties (solubility, turbidity, emulsifying, and foaming characteristics), and gel properties (gel strength, springiness, and water-holding capacity) of the MPs of white feather broiler, which were fed with different concentrations of selenium yeast or/and jujube powder (selenium yeast: 0,0.3, and 0.6 mg/kg; jujube powder: 8% to replace corn) for 42 days, were determined at 0, 24, and 72 h post-mortem. The results showed that with increasing concentrations of selenium yeast and jujube powder in the diet, the α-helix content, solubility, emulsification, and foaming of post-mortem chicken MP increased significantly (P < 0.05). The gel strength, springiness, and water-holding capacity of MP also increased, but the differences between the treatment groups were not significant (P > 0.05). In addition, the β-folding content and turbidity of MP decreased significantly (P < 0.05). Both the increase in selenium yeast levels and the addition of jujube powder improved the structural integrity and functional properties of MP. The best improvement effect was found in the combination group of high-dose selenium yeast and jujube powder, and there were significant interactions between them in the indices of α-helix, β-folding, turbidity, emulsification, and foam stability of MP. In conclusion, supplementing diets with seleniumyeast and jujube powder could maintain the structural stability of MPs in post-mortem chicken breast, leading to good functional properties. The results of this study may provide new insights into the effects of pre-slaughter feeding on post-mortem muscle MP conformation control and quality improvement.

Structural and functional modifications of myofibrillar protein by natural phenolic compounds and their application in pork meatball

Effects of different phenolic compounds on the structural and functional properties of myofibrillar protein (MP) were investigated, and the phenolic compounds were applied as natural modifiers in pork meatball. Interactions between MP and phenolic compounds were determined via molecular docking to elucidate the modification mechanisms. Tannic acid, gallic acid, (-)-epigallocatechin gallate, and epigallocatechin interacted with MP primarily through hydrogen bonds, which unfolded the secondary structures of MP and lowered surface hydrophobicity. Accordingly, the solubility, gel properties, and oxidation stability of MP were improved, while the emulsifying properties significantly decreased. Quercetin and quercitrin showed electrostatic interactions with MP, which preserved α-helix structures and increased surface hydrophobicity. While, the modifications lent MP the enhanced emulsifying properties, thermal stability, and oxidation stability, but the gel properties and solubility were mitigated. In addition, the incorporation of phenolic compounds prevented MP oxidation based upon their antioxidant abilities deriving from hydroxyl groups. Once the phenolic compounds were used in pork meatball, a minced meat model, they significantly improved the quality of meatball by bettering the texture properties and controlling the oxidation level. The results suggest that phenolic compounds have great potential to be employed as natural additives in minced meat products for the modification of functional properties.

Functional Properties Changes of Common Carp Proteins Influenced by Frozen Storage with Different Additives

The objective of the present study was to examine the functional properties changes of common carp myofibrillar protein (MP) due to frozen storage with cryoprotectants and different antioxidants. Common carp surimi was stored in −25 ℃ for 0, 30, 60, 90, 120 d with different additives (control sample, sample with cryoprotectants, sample with cryoprotectants + propyl gallate (PG), sample with cryoprotectants + whey proteolytic peptide), then emulsification properties, gel properties and rheological characteristic of common carp MP were evaluated by texture analyzer, electron microscope and rheometer. The results showed that the functional properties of MP were reduced in the frozen storage, which could be proved by the decreasing in the emulsification properties, gel properties and rheological characteristic of common carp MP, but the functional properties of MP decreased less when the surimi frozen stored with cryoprotectants and two kinds of antioxidants. The results showed that the addition of cryoprotectants and antioxidants during the frozen storage of surimi could effectively inhibit the changes of MP structure and thus reduce the deterioration of the functional properties of MP.

Emulsion‐forming properties of heat‐induced pork myofibrillar protein affected by NaCl

SummaryThe emulsification characteristics of myofibrillar proteins (MPs) with different NaCl concentrations also affect the quality of meat products after cooking. We investigated the effects of heating (100 °C) on the solubility, emulsifying activity, and conformational and environmental changes of MPs prepared with different NaCl concentrations. Emulsifying activity increased with increasing NaCl prior to heating, but there was no significant effect after heating. The viscosity increased and particle size decreased with increasing NaCl before heating, but these properties did not change after heating. NaCl did not affect the amount of α‐helix and β‐sheet. We deduced that the different emulsifying activity of myofibrillar proteins with different NaCl concentrations after heating may have been due to changes in the local environment of MPs. An understanding of the physicochemical and functional properties of MPs would unlock an area for development of meat products at different NaCl and temperature in the food industry.

Kappa-carrageenan and its oligosaccharides maintain the physicochemical properties of myofibrillar proteins in shrimp mud (Xia-Hua) during frozen storage.

As a popular hot-pot ingredient, Chinese-style shrimp mud (Xia-Hua) is usually transported and stored frozen. However, frozen storage leads to decreased quality of Xia-Hua products caused by the variations in physicochemical and functional properties of myofibrillar proteins (MPs). Κ-carrageenan and its oligosaccharides are reported as antioxidants and antifreeze and can stabilize proteins in whole shrimp, but their effects on MPs in Xia-Hua remain poorly understood. Compared to the control and Na4 P2 O7 treatments, the physicochemical properties of MPs in κ-carrageenan and its oligosaccharides-incorporated Xia-Hua were evaluated during 120 days of frozen storage. The results showed that cold stress increased the susceptibility of MPs to denaturation and oxidation during frozen storage. Carrageenan oligosaccharides maintained the turbidity, emulsifying activity, stability, and foaming capacity of MPs. Oxidation analysis showed that the incorporation of carrageenan oligosaccharides significantly retarded the rapid decrease of Ca2+ -ATPase activity, total sulphydryl and active sulphydryl contents, and also effectively inhibited the increases of carbonyl content and surface hydrophobicity of MPs. Thermal stability results confirmed that the oligosaccharides improved the denaturation temperature and enthalpy of MPs compared to the control, Na4 P2 O7 , and carrageenan treatments. This study suggests that κ-carrageenan and its oligosaccharides maintain the properties of MPs in Xia-Hua during frozen storage. PRACTICAL APPLICATION: The cryoprotection and antioxidant effects of carrageenan oligosaccharides on the stability of MPs in frozen shrimp mud can be used to extend the shelf-life and maintain the quality of frozen Xia-Hua products. Furthermore, it can drive the development of aquatic product health industry, improve the quality and safety of aquatic products, reduce the occurrence of public food safety incidents, and maintain social stability.

The effect of egg white protein and β-cyclodextrin mixture on structural and functional properties of silver carp myofibrillar proteins during frozen storage

The aim of this study was to investigate the impact of egg white protein (EWP) and β-cyclodextrin (βCD) mixture (3:1) on the structural and functional properties of myofibrillar proteins (MP) from silver carp during 60 days of frozen storage. Different concentrations of EWP-βCD were prepared and incorporated with MP. It was analyzed that α-helix content significantly decreased (P < 0.05) during frozen storage. EWP-βCD substantially enhanced the stability of α-helix content with the minimum increase of β-turn and random coils. Furthermore, rheological studies revealed that MP with increased EWP-βCD concentrations (4 and 6%) improved the inter-molecular protein interactions and enhanced the viscoelastic properties during the gelation process. Moreover, this addition improved the textural properties compared to control. It was also observed from microstructural analysis that MP gelling properties were decreased, which showed coarser and porous structure in control MP (0%). Meanwhile, MP gel treated with EWP-βCD (6%) showed a more compact and well-established network of proteins. All experimental analysis confirmed that EWP-βCD (6%) showed better cryoprotective properties in the preservation of the functional and structural properties of silver carp MP during frozen storage, and could be effective in the industrial storage of fish and associated products.

Insight into the conformational and functional properties of myofibrillar protein modified by mulberry polyphenols

This paper investigated the conformational and functional properties of myofibrillar protein modified by five phenolic compounds, including cyanidin 3-O-glucoside, cyanidin 3-O-rutinoside, caffeic acid, quercetin and rutin, dominantly presented in mulberry polyphenols-enriched sausage. These phenolic compounds significantly affected the structure of myofibrillar protein as indicated by the remarkable losses of carbonyl and ε-NH2 and the obviously fluorescence quenching effect (P < 0.05). Modified myofibrillar protein increased antioxidative activity but decreased thermal stability. Myofibirllar protein modified with rutin had no change in thermal stability but improved emulsifying properties. Quercetin has little effect on secondary structure of myofibirlliar protein. Caffeic acid triggered the conversion of α-helix to β-sheet in myofibrillar protein, and the resulted protein exhibited the strongest fluorescence quenching, solubility and antioxidant activity among all samples. Overall, the results suggested that all phenolic compounds involved in the changes of meat product quality, with caffeic acid and rutin being the most critical ones.

Effect of cold atmospheric plasma on the physicochemical and functional properties of myofibrillar protein from Alaska pollock (Theragra chalcogramma)

SummaryThis study aimed to investigate the effect of cold atmospheric plasma (CAP) on the physicochemical and functional properties of myofibrillar protein isolated from Alaska pollock (Theragra chalcogramma) muscle. Free sulfhydryl content, surface hydrophobicity, turbidity, differential scanning calorimetry, SDS‐PAGE, heat‐induced myofibrillar protein gel properties and water holding capacity were determined to evaluate the effect of CAP treatment on protein properties. CAP treatment from 10 to 60 kV for 10 min significantly (P &lt; 0.05) increased the water holding capacity, textural properties and colour properties of heat‐induced myofibrillar protein gel. As treatment voltage increased, free sulfhydryl content decreased significantly, while the turbidity and surface hydrophobicity of myofibrillar protein were increased. DSC data showed enhancement of thermal stability of the treated samples; however, the electrophoretic profile displayed a significant reduction in the band's intensity of protein at a higher voltage. These results suggest that cold atmospheric plasma (CAP) treatment could be used as an alternative approach to enhance the gelling properties of myofibrillar protein from Alaska pollock.

Physicochemical changes of myofibrillar proteins of squid (Argentinus ilex) induced by hydroxyl radical generating system

The effect of a hydroxyl radical generating system (HRGS), which contained FeCl3, sodium ascorbate, and different concentrations of H2O2, on the physiochemical properties of myofibrillar protein (MP) from squid mantles, has been investigated. The effect of different exposure times to HRGS was also considered. Compared to non-oxidized MP, a significant (p < 0.05) increase in carbonyl content (more than 50% of its original content) and protein solubility, as well as in surface hydrophobicity, was observed in the oxidative MP. With different treatment times, a sharp decrease (p < 0.05) in sulfhydryl content was detected. In addition, hydroxyl radical treatment significantly reduced the MP gel’s texture properties, whiteness and water holding capacity, especially at higher concentrations of H2O2. This observation could be attributed to extensive disorderly and less compact structure of MP gels. The results demonstrate the negative effect of HRGS on the structural and functional properties of MP from squid mantles.

Effects of dielectric barrier discharge plasma on the physicochemical and functional properties of myofibrillar proteins

Abstract The present study was designed to investigate the effects of dielectric barrier discharge (DBD) plasma on myofibrillar proteins extracted from beef. For this purpose, myofibrillar proteins were extracted from Longissimus dorsi muscle and treated with DBD plasma for 0, 5, 10, 15, and 20 min to evaluate free sulfhydryl and carbonyl, FTIR, and DSC profiles as well as pH, color, foaming capacity and stability, emulsion capacity and stability, and water binding capacity of myofibrillar proteins. Evaluation of the chemical changes revealed that protein oxidation was the main event occurring during exposure to DBD plasma. Moreover, mild oxidation during the first 10 min of exposure was found to improve the functional properties of myofibrillar proteins such that significant (p