Exploring the Effects of S-Nitrosylation on Caspase-3 Modification and Myofibril Degradation of Beef In Vitro.

This study aimed to explore the effects of S-nitrosylation on caspase-3 modification and its subsequent effects on beef myofibril degradation in vitro. Recombinant caspase-3 was reacted with different concentrations of S-nitrosoglutathione (GSNO, nitric oxide donor) at 37 °C for 30 min and subsequently incubated with purified myofibrillar protein from bovine semimembranosus muscle. Results indicated that the activity of caspase-3 was significantly reduced after GSNO treatments (P < 0.05) and showed a dose-dependent inhibitory effect, which was attributed to the increased S-nitrosylation extent of caspase-3. LC-MS/MS analysis revealed that caspase-3 was S-nitrosylated at cysteine sites 116, 170, 184, 220, and 264. Moreover, the degradation of desmin and troponin-T was notably suppressed by S-nitrosylated caspase-3 (P < 0.05). To conclude, protein S-nitrosylation could modify the cysteine residues of caspase-3, which accounts for the reduced caspase-3 activity and further represses its proteolytic ability on beef myofibrillar protein.

Effects of different hydrocolloids on the 3D printing and thermal stability of chicken paste.

This study investigated the effect of different hydrocolloids on the improvement of the printability and post-processing stability of minced chicken meat, each hydrocolloid was prepared with 1 % formulation and compared with the control. The effects of these hydrocolloids on the rheological properties of chicken mince and complex model printing capability were explored separately, while the cooking loss and microstructure changes of the samples before and after heating were analyzed. The results showed that the chicken mince gel containing carrageenan was more suitable for printing, increased the yield stress and apparent viscosity of the samples, and the printing process was easier to mold. In addition, carrageenan increased the hardness of the samples, and the microstructures were compact and changed little during the heating process, and the water was locked in the gel matrix, reducing shape changes during the heating process. The use of hydrocolloids improves the stability of post-processing of chicken 3D printing.

Applying Resistant Starch to Improve the Gel and Water Retention of Reduced-Fat Pork Batter.

Emulsified meat products contain high animal fat content, and excessive intake of animal fat is not good for health, so people are paying more and more attention to reduced-fat meat products. This study investigated the impact of varying proportions of pork back-fat and/or resistant starch on the proximate composition, water and fat retention, texture properties, color, and rheology characteristic of pork batter. The results found that replacing pork back-fat with resistant starch and ice water significantly decreased the total lipid and energy contents of cooked pork batter (p < 0.05) while improving emulsion stability, cooking yield, texture, and rheology properties. Additionally, when the pork back-fat replacement ratio was no more than 50%, there was a significant increase in emulsion stability, cooking yield, hardiness, springiness, cohesiveness, chewiness, and L* and G' values (p < 0.05). Furthermore, resistant starch and ice water enhanced myosin head and tail thermal stability and increased G' value at 80 °C. However, the initial relaxation times significantly decreased (p < 0.05) and the peak ratio of P21 significantly increased from 84.62% to 94.03%, suggesting reduced fluidity of water. In conclusion, it is feasible to use resistant starch and ice water as a substitute for pork back-fat in order to produce reduced-fat pork batter with favorable gel and rheology properties.

Effect of low-frequency alternating magnetic fields on the physicochemical, conformational and rheological properties of myofibrillar protein after iterative freeze-thaw cycles.

In this work, the effects of low-frequency alternating magnetic fields (LF-AMF) on the physicochemical, conformational, and functional characteristics of myofibrillar protein (MP) after iterative freeze-thaw (FT) cycles were explored. With the increasing LF-AMF treatment time, the solubility, active sulfhydryl groups, surface hydrophobicity, emulsifiability, and emulsion stability of MP after five FT cycles evidently elevated and then declined, and the peak value was obtained at 3 h. Conversely, the moderate LF-AMF treatment time can significantly reduce the average particle size, carbonyl content, and endogenous fluorescence intensity of MP. The rheology results showed that various LF-AMF treatment times would elevate the G' value of MP after iterative FT cycles. The FTIR spectroscopy results suggested that LF-AMF influenced the secondary structure of MP after multiple FT cycles, resulting in a depression in α-helix content and an increment in ß-folding proportion. Moreover, LF-AMF treatment induced the gradually lighter and wider myosin heavy chain bands of MP, implying that LF-AMF accelerated the degradation of macromolecular aggregates. Therefore, the LF-AMF treatment efficaciously ameliorates the structural and functional deterioration of MP after iterative FT cycles and could be used as a potential quality-improving technology in the frozen meat industry.

Low-frequency alternating magnetic field and CaCl2 influence the physicochemical, conformational and gel characteristics of low-salt myofibrillar protein.

In this study, the improvement mechanism of low-frequency alternating magnetic field (LF-AMF, 5 mT, 3 h) combined with calcium chloride (CaCl2, 0-100 mM) on the gel characteristics of low-salt myofibrillar protein (MP) was investigated. LF-AMF combined with 80 mM CaCl2 treatment increased solubility (32.71%), surface hydrophobicity (40.86 µg), active sulfhydryl content (22.57%), water-holding capacity (7.15%). Besides, the combined treatment decreased turbidity, particle size and intrinsic fluorescence strength of MP. Fourier transform infrared spectroscopy (FT-IR) results indicated that the combined treatment altered the secondary structure of MP by increasing ß-sheet and ß-turn, and reducing α-helix and random coil. The combined treatment also induced a high G' value and shortened T2 relaxation time for forming a homogeneous and compact gel structure. These results revealed that LF-AMF combined CaCl2 treatment could as a potential approach for modifying the gel characteristics of low-salt MP.

Using ultrasonic-assisted sodium bicarbonate treatment to improve the gel and rheological properties of reduced-salt pork myofibrillar protein.

To study the impact of ultrasonic duration (0, 30, and 60 min) and sodium bicarbonate concentration (0% and 0.2%) on the gel properties of reduced-salt pork myofibrillar protein, the changes in cooking yield, colour, water retention, texture properties, and dynamic rheology were investigated. The findings revealed that added sodium bicarbonate significantly increased (P < 0.05) cooking yield, hardness, springiness, and strength of myofibrillar protein while reducing centrifugal loss. Furthermore, the incorporation of sodium bicarbonate led to a significant decrease in L⁎, a⁎, b⁎, and white values of cooked myofibrillar protein; these effects were further amplified with increasing ultrasonic duration (P < 0.05). Additionally, storage modulus (G') significantly increased for myofibrillar protein treated with ultrasonic-assisted sodium bicarbonate treatment resulting in a more compact gel structure post-cooking. In summary, the results demonstrated that ultrasonic-assisted sodium bicarbonate treatment could enhance the tightness of reduced-salt myofibrillar protein gel structure while improving the water retention and texture properties.

Effects of low-frequency magnetic field on solubility, structural and functional properties of soy 11S globulin.

BACKGROUND: Soy 11S globulin has high thermal stability, limiting its application in the production of low-temperature gel foods. In this study, the low-frequency magnetic field (LF-MF, 5 mT) treatment (time, 30, 60, 90, and 120 min) was used to improve the solubility, conformation, physicochemical properties, surface characteristics, and gel properties of soy 11S globulin. RESULTS: Compared with the native soy 11S globulin, the sulfhydryl content, emulsifying capacity, gel strength, water-holding capacity, and absolute zeta potential values significantly increased (P < 0.05) after LF-MF treatment. The LF-MF treatment induced the unfolding of the protein structure and the fracture of disulfide bonds. The variations in solubility, foaming properties, viscosity, surface hydrophobicity, and rheological properties were closely related to the conformational changes of soy 11S globulin, with the optimum LF-MF modification time being 90 min. CONCLUSION: LF-MF treatment is an effective method to improve various functional properties of native soy 11S globulin, and this study provides a reference for the development of plant-based proteins in the food industry. © 2024 Society of Chemical Industry.

Oxidative Modification, Structural Conformation, and Gel Properties of Pork Paste Protein Mediated by Oxygen Concentration in Modified Atmosphere Packaging.

The objective of this study was to investigate the effect of pork oxidation through modified atmosphere packaging (MAP) on gel characteristics of myofibrillar proteins (MP) during the heat-induced gelation process. The pork longissimus thoracis (LT) was treated by MAP at varying oxygen concentrations (0, 20, 40, 60, and 80% O2) with a 5-day storage at 4 °C for the detection of MP oxidation and gel properties. The findings showed the rise of O2 concentration resulted in a significant increase of carbonyl content, disulfide bond, and particle size, and a decrease of sulfhydryl content and MP solubility (p < 0.05). The gel textural properties and water retention ability were significantly improved in MAP treatments of 0-60% O2 (p < 0.05), but deteriorated at 80% O2 level. As the concentration of O2 increased, there was a marked decrease in the α-helix content within the gel, accompanied by a simultaneous increase in ß-sheet content (p < 0.05). Additionally, a judicious oxidation treatment (60% O2 in MAP) proved beneficial for crafting dense and uniform gel networks. Our data suggest that the oxidation treatment of pork mediated by O2 concentration in MAP is capable of reinforcing protein hydrophobic interaction and disulfide bond formation, thus contributing to the construction of superior gel structures and properties.

Effects of Potassium Bicarbonate on Gel, Antioxidant and Water Distribution of Reduced-Phosphate Silver Carp Surimi Batter under Cold Storage.

The changes in storage loss, water distribution status, gel characteristics, thiobarbituric acid reactive substances (TBARSs), total volatile basic nitrogen, and total plate count of cooked reduced-phosphate silver carp surimi batter during cold storage at 4 °C were investigated. The storage loss, content of free water, pH, hardness, TBARSs, total volatile basic nitrogen value, and total plate count of all cooked silver carp surimi batters significantly increased (p < 0.05) with an increase in cold storage time. Meanwhile, the content of immobilized water, whiteness, springiness, and cohesiveness significantly decreased (p < 0.05). At the same cold storage time, the sample of cooked reduced-phosphate silver carp surimi batter had lower water mobility, darker color, and better texture characteristics than the cooked silver carp surimi batter without potassium bicarbonate; however, the values of TBARSs, total volatile basic nitrogen, and total plate count were not significantly different (p > 0.05). This meant that there was no difference between potassium bicarbonate and sodium tripolyphosphate in antioxidant and antibacterial activity during the cold storage of silver carp surimi batter. To summarize, the use of potassium bicarbonate instead of sodium tripolyphosphate could produce cooked reduced-phosphate silver carp surimi batter with better water-holding capacity and gel characteristics during cold storage.

Using Potassium Bicarbonate to Improve the Water-Holding Capacity, Gel and Rheology Characteristics of Reduced-Phosphate Silver Carp Batters.

To study the use of partial or total potassium bicarbonate (PBC) to replace sodium tripolyphosphate (STPP) on reduced-phosphate silver carp batters, all the batters were composed of silver carp surimi, pork back fat, ice water, spices, sugar, and sodium chloride. Therein, the sample of T1 contained 4 g/kg STPP; T2 contained 1 g/kg PBC, 3 g/kg STPP; T3 contained 2 g/kg PBC, 2 g/kg STPP; T4 contained 3 g/kg PBC, 1 g/kg STPP; T5 contained 4 g/kg PBC, and they were all produced using a bowl chopper. The changes in pH, whiteness, water- and oil-holding capacity, gel and rheological properties, as well as protein conformation were investigated. The pH, cooking yield, water- and oil-holding capacity, texture properties, and the G' values at 90 °C of the reduced-phosphate silver carp batters with PBC significantly increased (p < 0.05) compared to the sample without PBC. Due to the increasing pH and enhanced ion strength, more ß-sheet and ß-turns structures were formed. Furthermore, by increasing PBC, the pH significantly increased (p < 0.05) and the cooked silver carp batters became darkened. Meanwhile, more CO2 was generated, which destroyed the gel structure, leading the water- and oil-holding capacity, texture properties, and G' values at 90 °C to be increased and then decreased. Overall, using PBC partial as a substitute of STPP enables reduced-phosphate silver carp batter to have better gel characteristics and water-holding capacity by increasing its pH and changing its rheology characteristic and protein conformation.

Low-frequency alternating magnetic field thawing of frozen pork meat: Effects of intensity on quality properties and microstructure of meat and structure of myofibrillar proteins.

The purpose of the study was to evaluate the changes in quality properties and microstructure of pork meat as well as structural variation in myofibrillar proteins (MPs) after low-frequency alternating magnetic field thawing (LF-MFT) with different intensities (1-5 mT). LF-MFT at 3-5 mT shortened the thawing time. LF-MFT treatment significantly influenced the quality properties of meat and notably improved the structure of MPs (P < 0.05), compared to atmosphere thawing (AT). Especially, among the thawing treatments, LF-MFT-4 (LF-MFT at 4 mT) had the lowest values of thawing loss and drip loss, and the least changes in the color and myoglobin content. Regarding the results of rheological properties and micrographs, an optimal gel structure and a more compact muscle fiber arrangement formed during LF-MFT-4. Moreover, LF-MFT-4 was beneficial for improving the conformation of MPs. Therefore, LF-MFT-4 reduced the deterioration of porcine quality by protecting MPs structure, indicating a potential use in the meat thawing industry.

Effect of High Pressure Homogenization-Modified Soy 11S Globulin on the Gel and Rheological Properties of Pork Myofibrillar Protein.

The changes in texture and rheological characteristics, water holding capacity, and microstructure of pork myofibrillar protein with high-pressure homogenization-modified (0-150 MPa) soy 11S globulin were studied. The cooking yield, whiteness values, texture properties, shear stress, initial apparent viscosity, storage modulus (G'), and loss modulus (G″) of pork myofibrillar protein with high-pressure homogenization-modified soy 11S globulin were significantly increased (p < 0.05) compared with the sample of 0 MPa, and centrifugal yield was significantly decreased, except for the sample of 150 MPa. Therein, the sample of 100 MPa had the largest values. Meanwhile, the water and proteins bonded more tightly because the initial relaxation times of T2b, T21 and T22 from pork myofibrillar protein with high-pressure homogenization-modified soy 11S globulin were shorter (p < 0.05). Overall, the water-holding capacity, gel texture and structure, and rheological properties of pork myofibrillar protein could improve when adding soy 11S globulin treated with 100 MPa.

Effect of Artemisia sphaerocephala krasch gum on the functional properties of pork batters.

The influence of the incorporation of Artemisia sphaerocephala krasch gum (ASK gum; 0-0.18%) on the water holding capability (WHC), texture, color, rheological property, water distribution, protein conformation and microstructure of pork batters was investigated. The results showed that the cooking yield, WHC and L* value of pork batter gels significantly increased (p < .05) with the increasing incorporation of ASK gum, and the highest value were observed at 0.15%; the a* value decreased significantly (p < .05) and no significance was obtained in b* value (p > .05); the hardness, elasticity, cohesiveness and chewiness increased first and then decreased, and reached the highest value at 0.15%. The rheological results showed that the higher G' value was obtained in pork batters by the incorporation of ASK gum; the low field NMR analysis indicated that ASK gum significantly increased the proportion of P2b and P21 (p < .05) and decreased the proportion of P22 ; Fourier transform infrared spectroscopy (FTIR) indicated that the ASK gum significantly reduced the α-helix content and increased the ß-sheet content (p < .05). Scanning electron microscopy results suggested that the incorporation of ASK gum could promote the formation of a more homogeneous and stable microstructure of pork batter gels. Therefore, appropriate incorporation (0.15%) of ASK gum may improve the gel properties of pork batters, and while excessive incorporation (0.18%) could weaken the gel properties.

Effects of pre-emulsified safflower oil with magnetic field modified soy 11S globulin on the gel, rheological, and sensory properties of reduced-animal fat pork batter.

In this work, the differences in macrostructure and microstructure, rheology, and storage stability of pre-emulsified safflower oil (PSO) prepared by natural and magnetic field modified soy 11S globulin were analysised. It was concluded that the PSO with magnetic field modified soy 11S globulin (MPSO) has better emulsifying activity and physical stability. The changes in gel quality, oxidational sensitivity, rheological, and sensory properties of pork batters with different substitute ratios (0%, 25%, 50%, 75%, and 100%) of pork back-fat by MPSO with magnetic field modified soy 11S globulin were studied. Compared to the sample without MPSO, pork batter with MPSO showed higher emulsion stability, apparent viscosity, L⁎ value, springiness, cohesiveness, and expressible moisture, while lower a⁎ value and cooking loss. Moreover, added MPSO could be more uniformly distributed into the meat matrix with smaller holes. With the increase in the replacement proportion of pork back-fat, the hardness, water- and fat-holding capacity, and P21 of pork batter significantly decreased (P < 0.05). As revealed by sensory evaluation and TBARS, using MPSO to substitute for pork back-fat decreased the lipid oxidational sensitivity of pork batter, and without negative effects on the appearance, juiciness and overall acceptability. Overall, it is feasible to apply MPSO as a pork-fat replacer to produce reduced-animal fat pork batter with excellent gel and sensory properties.

Effects of heating rates on the self-assembly behavior and gelling properties of beef myosin.

BACKGROUND: Myosin is the most important component of myofibrillar protein, with excellent gelling properties. To date, heating treatment remains the mainstream method for forming gel in meat products, and it has the most extensive application in the field of meat industry. However, at present, there are few reports on the effects of heating rates on myosin self-assembly and aggregation behavior during heating treatment. RESULTS: The present study aimed to investigate the effects of different heating rates (1, 2, 3 and 5 °C min-1 ) on the self-assembly behavior, physicochemical, structural and gelling properties of myosin. At the lowest heating rate of 1 °C min-1 , the myosin gel had a dense microstructure, the highest elastic modulus (G') and water holding capacity compared to higher heating rates (2, 3 and 5 °C min-1 ). At higher temperatures (40, 45 °C), the surface hydrophobicity, turbidity, particle size distribution and self-assembly behavior of myosin in pre-gelling solutions showed that myosin had sufficient time to denature, underwent full structure unfolding before aggregation at the heating rate of 1°C min-1 , and formed regular and homogeneous spherical aggregates. Therefore, the myosin gel also had a better three-dimensional network. CONCLUSION: The heating rates had an important effect on the quality of myosin gels, and had theoretical implications for improving the quality of meat gel products. © 2023 Society of Chemical Industry.

Understanding the influence of fluctuated low-temperature combined with high-humidity thawing on gelling properties of pork myofibrillar proteins.

The present study further investigated the effects of fluctuated low-temperature combined with high-humidity thawing (FLHT) on the gelling properties of pork myofibrillar proteins (MPs). Results showed that compared with refrigerator thawing (RT) and low-temperature combined with high-humidity thawing (LHT), FLHT effectively reduced the protein aggregation and maintained the relative stability by decreasing the variation in the turbidity and absolute ζ-potential value. The rheological results confirmed its improved elastic gel network. Meanwhile, FLHT samples exhibited markedly higher WHC with lower cooking loss (P < 0.05). The whiteness and strength of MPs gel were significantly higher in the FLHT group (P < 0.05). Moreover, there was no difference in textural properties between FLHT samples and fresh meat (FS) (P > 0.05), due to its homogeneous and compact microstructure. Therefore, FLHT plays an essential role in holding a superior gel quality and a compact structure, thereby evidencing its potential application in meat thawing.

A comparative study of vacuum tumbling and immersion marination on quality, microstructure, and protein changes of Xueshan chicken.

Marination is a common technology in meat processing with advantages of enhancing tenderness, water retention, and overall quality. This study was conducted to investigate the effect of vacuum tumbling and immersion marination on meat quality, microstructure, water mobility, protein changes, and denaturation of Xueshan chicken. Results showed that vacuum tumbling significantly increased the marinating rate of chicken, tenderness, meat texture, and water retention. Meanwhile, vacuum tumbling decreased total sulfhydryl content alongside an increased protein surface hydrophobicity and free sulfhydryl content, indicating that vacuum tumbling elevated the degree of protein denaturation. Further, the peak area corresponding to the relaxation time T22 after vacuum tumbling was significantly higher than that of immersion marination, suggesting that the stability of the immobilized water of chicken was reduced by vacuum tumbling. Compared to immersion marination, vacuum tumbling improved myofibril fragmentation index (MFI) presenting fewer myofibrillar protein bands in sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) gel and more damaged muscular cells. Overall, vacuum tumbling could improve the marination absorptivity, protein degradation, and denaturation, resulting in changes in myofibril structure and meat quality of Xueshan chicken.

Changes in Gel Characteristics, Rheological Properties, and Water Migration of PSE Meat Myofibrillar Proteins with Different Amounts of Sodium Bicarbonate.

The changes in the gel and rheological properties and water-holding capacity of PSE meat myofibrillar proteins with different amounts of sodium bicarbonate (SC, 0−0.6/100 g) were studied. Compared to the PSE meat myofibrillar proteins with 0/100 g SC, the texture properties and cooking yield significantly increased (p < 0.05) with increasing SC; meanwhile, adding SC caused the gel color to darken. All samples had similar curves with three phases, and the storage modulus (G') values significantly increased with the increasing SC. The thermal stability of the PSE meat myofibrillar proteins was enhanced, and the G' value at 80 °C increased with the increasing SC. Because water was bound more tightly to the protein matrix, the initial relaxation times of T21 and T22 shortened, the peak ratio of P21 significantly increased (p < 0.05), and the P22 significantly decreased (p < 0.05), which implied that the mobility of the water was reduced. Overall, SC could improve the thermal stability of the PSE meat myofibrillar proteins and increase the water-holding capacity and textural properties of the cooked PSE meat myofibrillar protein gels.

Effects of NaCl on the interactions between neomethyl hesperidin dihydrochalcone and pork myofibrillar protein: Their relevance to gelation properties.

Effects of sweetener neomethyl hesperidin dihydrochalcone (NHDC) on the gelation properties of myofibrillar protein (MP) at 0.2 M and 0.6 M NaCl were investigated. The results showed that addition of NHDC did not obviously change the cooking loss and strength of MP gels at 0.2 M NaCl. Whilst at 0.6 M NaCl, addition of high doses of NHDC (50-100 µM/g) remarkably increased cooking loss and decreased strength of MP gels. The expanded MP enhanced the interactions between NHDC and MP, leading to aggregation of MP as evidenced by the increasing particle size and the reducing solubility. The MP aggregates impeded hydrophobic interactions and disulfide bonds crosslinking in the gelation process, thereby damaged the gelation properties of MP at 0.6 M NaCl. This was supported by the poor network of MP gels observed by SEM. In the end, molecular docking elucidated the main types of interaction at molecular level, including hydrogen bonding and hydrophobicity. The results would provide guidance for NHDC as a potential sweetener in meat products.

Effect of Ultrasound-Assisted Sodium Bicarbonate Treatment on Aggregation and Conformation of Reduced-Salt Pork Myofibrillar Protein.

To study the effects of an ultrasound (0, 30, and 60 min) and sodium bicarbonate (0% and 0.2%) combination on the reduced-salt pork myofibrillar protein, the changes in pH, turbidity, aggregation, and conformation were investigated. After the ultrasound-assisted sodium bicarbonate treatment, the pH increased by 0.80 units, the absolute value of Zeta potential, hydrophobic force, and active sulfhydryl group significantly increased (p < 0.05), and the turbidity and particle size significantly decreased (p < 0.05). Meanwhile, the fluorescence intensity decreased from 894 to 623, and the fluorescence peak showed a significant redshift, which indicated that the ultrasound-assisted sodium bicarbonate treatment exposed the non-polarity of the microenvironment in which the fluorescence emission group was located, leading to the microenvironment and protein structure of myofibrillar tryptophan being changed. Overall, an ultrasound-assisted sodium bicarbonate treatment could significantly improve pork myofibrillar protein solubility and change the protein structure under a reduced-salt environment.