This study examined the interaction between myofibrillar proteins (MPs) and the numbing substance hydroxy-α-sanshool (α-SOH) in a thermal environment, and provided an explanation of the numbness perception mechanism through muti-spectroscopic and molecular dynamics simulation methodology. Results showed that addition of α-SOH could reduce the particle size and molecular weight of MPs, accompanied by changes in the tertiary and secondary structure, causing the α-helix of MPs transitioned to β-sheet and β-turn due to the reorganization of hydrogen bonds. After a moderate heating (60 or 70 °C), MPs could form the stable complexes with α-SOH that were associated with attachment sites and protein wrapping. The thermal process might convert a portion of α-SOH\' into hydroxy-β-sanshool\' (β-SOH\'). When docking with the sensory receptor TRPV1, the RMSD, RMSF and binding free energy all showed that β-SOH\' demonstrated a low affinity, thereby reducing the numbing perception. These findings can provide a theoretical foundation for the advanced processing of numbing meat products.

In the current scientific literature, one can find >100 different methods to evaluate water-holding capacity in fresh and cooked meat. The main concepts are based on removing some of the water by either gravity, application of pressure (e.g., centrifugal force), and heating while measuring water exudate to predict the water holding capacity (WHC) during storage, processing, cooking, and/or distribution. More sophisticated methods include nuclear magnetic resonance (NMR) in which the relaxation of water molecules within a meat protein/gel system is measured to predict how the water (75% in lean meat) will behave during processing. Overall, the number of tests reported is also so high because there are quite big variations in test conditions (e.g., 750-30,000 g for centrifugal testing). The aim of this article (outcome of a symposium on methods for poultry meat characterization) is to help the reader navigate through the different setups and suggest standardized testing based on scientific principles. The recommended WHC test is the application of low centrifugal force (750 g so sample is not permanently deformed) to a protein gel, while the sample is placed on a screen platform to avoid reabsorbing the liquid separating during the slowing down of the centrifuge. It is also recognized that some meat samples (e.g., high in fat) might require a different g-force, so it is recommended to employ both the conditions mentioned above and the lab-specific conditions. Our overall goal should always be to increase uniformity in test procedures, which will enhance our capabilities to compare results among research groups.

This study aimed to assess the effect of an external protease secreted by Staphylococcus (S.) xylosus on the hydrolysis and flavor properties of meat protein. The results indicated that the protease significantly increased the solubility of myofibrillar proteins (MPs) and sarcoplasmic proteins (SPs) in water (P < 0.05), and altered their surface hydrophobicity and secondary structure. The results of micromorphological and free amino acids analyses suggested that the protease degraded the large and insoluble meat protein aggregates into small molecular proteins with uniform distribution and amino acids, especially glycine, glutamic acid, leucine, and cysteine. Moreover, the protease-catalyzed hydrolysis promoted the formation of some volatile compounds in the MPs and SPs. Additionally, molecular docking analysis suggested that hydrogen bond and hydrophobic interaction promoted the formation of a S. xylosus protease/meat protein complex. These results provided a basis for the future application of S. xylosus protease in meat products.

The kinetic properties and thermal characteristics of fresh pork meat proteins (Longissimus dorsi), as well as osmotically dehydrated meat proteins, were investigated using differential scanning calorimetry. Two isoconversional kinetical methods, namely the differential Friedman and integral Ortega methods, were employed to analyze the data. The obtained kinetic triplet, activation energy, pre-exponential factor, and extent of conversion, has been discussed. The resulting activation energy for proteins of fresh meat ranges between 751 kJ·mol-1 for myosin, 152 kJ·mol-1 for collagen and sarcoplasmic proteins, and 331 kJ·mol-1 for actin at a conversion degree of 0.1 to 0.9. For osmotically dried pork meat proteins, the values range from 307 kJ·mol-1 for myosin 272 kJ·mol-1 for collagen and sarcoplasmic proteins, and 334.83 kJ·mol-1 for actin at a conversion degree from 0.1 to 0.9. The proteins of the dry meat obtained by osmotic dehydration in molasses could be described as partly unfolded as they retain the characteristic protein denaturation transition. Concerning the decrease in enthalpies of proteins denaturation, thermodynamic destabilization of dried meat proteins occurred. On the contrary, dried meat proteins were thermally stabilized with respect to increase in the temperatures of denaturation. Knowledge of the nature of meat protein denaturation of each kind of meat product is one of the necessary tools for developing the technology of meat product processing and to achieve desired quality and nutritional value. The kinetic analysis of meat protein denaturation is appropriate because protein denaturation gives rise to changes in meat texture during processing and directly affects the quality of product.

Meat and meat products provide high levels of nutrition and many health benefits to consumers, yet a controversy exists regarding the use of non-meat additives, such as the inorganic phosphates that are commonly used in meat processing, and particularly their relationship to cardiovascular health and kidney complications. Inorganic phosphates are salts of phosphoric acid (e.g., sodium phosphate, potassium phosphate, or calcium phosphate), whereas organic phosphates are ester compounds (e.g., the phospholipids found in cell membranes). In this sense, the meat industry remains active in its efforts to improve formulations for processed meat products with the use of natural ingredients. Despite efforts to improve formulations, many processed meat products still contain inorganic phosphates, which are used for their technological contributions to meat chemistry including improvements in water-holding capacity and protein solubilization. This review provides a thorough evaluation of phosphate substitutes in meat formulations and other processing technologies that can help eliminate phosphates from the formulations of processed meat products. In general, several ingredients have been evaluated as replacements for inorganic phosphates with varying degrees of success such as plant-based ingredients (e.g., starches, fibers, or seeds), fungi ingredients (e.g., mushrooms and mushroom extracts), algae ingredients, animal-based ingredients (e.g., meat/seafood, dairy, or egg materials), and inorganic compounds (i.e., minerals). Although these ingredients have shown some favorable effects in certain meat products, none have exactly matched the many functions of inorganic phosphates, so the support of extrinsic technologies, such as tumbling, ultrasound, high-pressure processing (HPP), and pulsed electric field (PEF), may be necessary to achieve similar physiochemical properties as conventional products. The meat industry should continue to investigate ways to scientifically innovate the formulations of, and the technologies used in, processed meat products while also listening to (and acting upon) the feedback from consumers.

The goal of this study was to determine the qualities of pork myofibrillar protein (MP) gels added with pork gelatin and transglutaminase (TGase), as well as their application to restructured ham (RH). MP mixtures were prepared with various levels of gelatin (0.5, 1.0, and 1.5%. w/w) and TGase. In this study, cooking loss (CL), gel strength, shear stress, and the microstructure of MP with various levels of gelatin were evaluated. After RHs were manufactured with varying levels of gelatin and TGase, the physicochemical and textural properties were measured. The CL of the MP with 1% (w/w) of gelatin was decreased. Regardless of the presence of TGase, increased amounts of gelatin in the MP gels resulted in high shear stress. Shear values were higher in the RH with gelatin treatment than in the other treatments. In addition, the RHs with gelatin alone or combined with TGase had high water-holding capacity. The RH with the combination of gelatin and TGase had higher sensory attributes than the control. Gelatin improved the physical properties of the RHs and is recommended for application in various meat products.

Meat analogs based on plant protein extracts are rising in popularity as meat consumption declines. A dietary shift away from meat, which has a high iron bioavailability, may have a negative effect on the amount of iron absorbed from the diet. Iron absorption from legumes cultivated in regions not suitable for soy production, such as fava bean, has not yet been explored. The aim of this study was to evaluate non-heme iron absorption from a meal with texturized fava bean protein compared to beef and cod protein meals. The study included two single-blinded iron isotope trials in healthy Swedish women of the ages 18-45 years, each of whom served as their own control. The participants were served matched test meals containing beef and fava bean protein (Study 1) or cod and fava bean protein (Study 2) with radiolabeled non-heme iron 55Fe and 59Fe. The absorption of non-heme iron from test meals was measured by whole-body counting and erythrocyte incorporation. The absorption of non-heme iron, measured as erythrocyte incorporation ratio, from beef protein meal was 4.2 times higher compared to texturized fava bean meal, and absorption from cod protein meal was 2.7 times higher compared to the fava bean meal. The adjusted non-heme iron absorption, normalized to a 40% reference dose uptake, was 9.2% for cod protein meal, 21.7% for beef protein meal, and 4.2% for texturized fava bean meal. A fava bean protein meal has markedly lower iron bioavailability in healthy females compared with a meal of beef or cod protein. Therefore, a dietary shift from meat and fish protein to fava bean protein may increase the risk of iron deficiency.

Nowadays, there is increasing interest in developing strategies for the efficient and sustainable use of animal by-products, such as pork liver. In order to stabilize the product, a prior dehydration stage may be required due to its high perishability. The water removal process of pork liver is energy costly and time consuming, which justifies its intensification using novel technologies. In this sense, the aim of this study was to assess the effect of the airborne application of power ultrasound on the hot air-drying of pork liver. For that purpose, drying experiments were carried out at 30, 40, 50, 60 and 70 °C on pork liver cylinders at 2 m·s-1 with (US) and without ultrasonic application (AIR). The drying process was modeled from the diffusion theory and, in the dried pork liver, the protein solubility was analyzed in order to determine the effect of drying on the protein quality. The ultrasound application increased the drying rate, shortening the drying time by up to 40% at 30 °C. The effect of power ultrasound at high temperatures (60 and 70 °C) was of lesser magnitude. Drying at 70 °C involved a noticeable reduction in the protein solubility for dried liver, while the impact of ultrasound application on the solubility was not significant (p > 0.05).

The protease generated from Staphylococcus (S.) xylosus A2, which was isolated from Harbin dry sausages, was purified and characterized. The molecular weight of the purified protease was approximately 21.5 kDa, and its relative activity reached the highest at pH 6.0 and 50 °C. At pH 4.0−8.0 and temperatures of 20−50 °C, the protease was stable. Its activity was significantly improved by Ca2+ and Zn2+ ions (p < 0.05). The Michaelis constant and maximum velocity of the protease were 2.94 mg/mL and 19.45 U/mL·min, respectively. The thermodynamic parameters analysis suggested that the protease showed better catalytic properties at 40 °C. Moreover, the protease could hydrolyze meat proteins, and obtained hydrolysate is non-cytotoxic to the HEK-293 cells. These findings provide a theoretical basis for understanding the enzymatic characterization of S. xylosus A2 protease and its future application in fermented meat products.

We explored whether ultrasound treatment affected digestibility of myofibrillar protein (MP) isolated from modified atmosphere packed (MAP, 70% N2 and 30% CO2) pork. MP digestibility under pepsin and pancreatin treatments decreased significantly with storage time. Ultrasound treatment increased the digestibility and produced a greater number of smaller peptides. However, the total peptide count and unique peptide counts were significantly reduced. Moreover, active sulfhydryl, total sulfhydryl, particle size, turbidity and surface hydrophobicity of MP increased with time, while protein solubility and ATPase activity decreased. Compared with the untreated samples, ultrasound treatment increased protein solubility, surface hydrophobicity, and active sulfhydryl content, but decreased total sulfhydryl content (except 10 d), particle sizes, turbidity and ATPase activity. Ultrasound treatment resulted in a decline in β-turn and α-helix contents. Therefore, ultrasound is conducive to the digestion. Additionally, structural and functional properties of protein in MAP were less stable than those in vacuum-packed pork reported before.