Effect of Sarcoplasmic Protein Solutions Dried at Different Times and Rates on Water Migration in Lamb Myofibril In Vitro.

To determine whether sarcoplasmic proteins affected water migration in myofibrils during air-drying, with protein denaturation as an indicator of sarcoplasmic protein changes, the extent of sarcoplasmic protein changes in lamb during air-drying was first studied. The results showed that sarcoplasmic protein's thermal stability decreased and secondary structure changed, indicating sarcoplasmic protein denatured in lamb during air-drying (35 °C, 60% RH, 3 m/s wind speed). Subsequently, the effect of sarcoplasmic protein solutions, dried at different times and rates, on myofibril protein-water interaction was studied in vitro. Two sets of sarcoplasmic protein solutions were dried for 0, 3, 6, and 9 h in a drying oven, resulting in different degrees of change. These two sets with higher or lower drying rates were achieved by controlling the contact area between sarcoplasmic protein solution and air. These dried sarcoplasmic protein solutions were then mixed with extracted myofibril and incubated for 2 h. The results showed a significant increase in T21 relaxation time of the incubation system when sarcoplasmic protein solution was dried at 35 °C for 3 h. This indicated that myofibrillar protein-water interaction was weakened, facilitating water migration from the inside to the outside of myofibrils. The denaturation degree of sarcoplasmic proteins was slowed by a higher drying rate, thereby alleviating the increase in the amount of immobile water within myofibrils when dried for 6 h. In conclusion, the properties of sarcoplasmic proteins were influenced by both drying rate and time, thereby influencing the water migration within myofibrils during air-drying.

Development of Plastic/Gelatin Bilayer Active Packaging Film with Antibacterial and Water-Absorbing Functions for Lamb Preservation.

In order to extend the shelf life of refrigerating raw lamb by inhibiting the growth of microorganisms, preventing the oxidation of fat and protein, and absorbing the juice outflow of lamb during storage, an active packaging system based on plastic/gelatin bilayer film with essential oil was developed in this study. Three kinds of petroleum-derived plastic films, oriented polypropylene (OPP), polyethylene terephthalate, and polyethylene, were coated with gelatin to make bilayer films for lamb preservation. The results showed significant improvement in the mechanical properties, oxygen, moisture, and light barriers of the bilayer films compared to the gelatin film. The OPP/gelatin bilayer film was selected for further experiments because of its highest acceptance by panelists. If the amount of juice outflow was less than 350% of the mass of the gelatin layer, it was difficult for the gelatin film to separate from lamb. With the increase in essential oil concentration, the water absorption capacity decreased. The OPP/gelatin bilayer films with 20% mustard or 10% oregano essential oils inhibited the growth of bacteria in lamb and displayed better mechanical properties. Essential oil decreased the brightness and light transmittance of the bilayer films and made the film yellow. In conclusion, our results suggested that the active packaging system based on OPP/gelatin bilayer film was more suitable for raw lamb preservation than single-layer gelatin film or petroleum-derived plastic film, but need further study, including minimizing the amount of essential oil, enhancing the mechanical strength of the gelatin film after water absorption.

Shrinkage Properties and Their Relationship with Degradation of Proteins Linking the Endomysium and Myofibril in Lamb Meat Submitted to Heating or Air Drying.

The shrinkage of the connective tissue and myofiber of lamb meat submitted to heat treatment or air drying at different storage stages (1, 5 and 7 days) was evaluated herein. The longitudinal and transverse shrinkage of heated lamb meat was significantly influenced by storage time and water bath heating temperature (50 °C, 70 °C and 90 °C) (p < 0.001). In contrast, the shrinkage of air-dried lamb meat was not influenced by storage time (p > 0.05). The microstructure of heated lamb meat, namely, the distance between muscle fascicles, the distance between myofibril networks, the area of myofibril networks, and the endomysium circumference, was significantly influenced by storage time (p < 0.05). During storage, the proportion of muscle fibers completely detached from endomysium increased, which could be due to the progressive degradation of proteins linking the endomysium and myofibril, including ß-dystroglycan, α-dystroglycan, integrin-ß1, and dystrophin. However, degradation of such proteins did not influence the shrinkage of lamb meat stored for five days or longer, since the decreased distance between myofibril networks indicated a higher shrinkage ratio of the endomysium compared to myofibers in samples air-dried at 35 °C or heated at 90 °C. The effect of these proteins on the shrinkage of heated lamb meat (raw meat stored for 1 day or less time) requires further elucidation.

Microstructure and physiochemical properties of meat sausages based on nanocellulose-stabilized emulsions.

Here we prepared some meat sausages using soybean oil in pure liquid form or pre-emulsified form stabilized with nanocelluloses (NCs) to partially replace pork back-fat and investigated the effects of NC types (sisal cellulose nanofiber, cotton cellulose nanofiber, and cotton cellulose nanocrystal) on the physicochemical properties and microstructure of the sausages. The physicochemical properties, including cooking loss, water holding capacity (WHC), textural properties, and rheological behavior, were evaluated. The results show that the sausages with pre-emulsified oil exhibited much-improved water and fat binding capacities, with significantly increased hardness, springiness, and chewiness. Additionally, pre-emulsifying soybean oil provided a more compact structure with smaller cavities. The sausages with different NCs had no significant difference in textural and microstructural properties, whereas they presented different water and fat binding capacities. From the results, it is concluded that NC-based emulsions are a viable fat replacer for meat sausages by providing similar stability and textural attributes.

Meat Color Stability of Ovine Muscles Is Related to Glycolytic Dehydrogenase Activities.

The relationship between glycolytic dehydrogenase, including glyceraldehyde-3-phosphate dehydrogenase (GAPDH), lactic dehydrogenase (LDH), and meat color stability was studied in this study using ovine muscle. Three different ovine muscles, including M. longissimus lumborum (LL), M. semimembranosus (SM), and M. psoas major (PM), were obtained (n = 10, respectively), and then displayed for 7 days at 4 °C. The LL and SM muscle had higher surface redness, higher (P < 0.05) GAPDH activity, nicotinamide adenine dinucleotide (NADH) content, and lower (P < 0.05) LDH-B activity than PM muscles during display. The PM muscle had the worst color stability and lowest NADH content. These results suggest that variation in color stability of physiologically different muscles may be affected by glycolysis dehydrogenases. Comparatively, our data showed that GAPDH may play a more important role than LDH-B to maintain meat color stability.

Proteomic analysis of goat Longissimus dorsi muscles with different drip loss values related to meat quality traits.

Longissimus dorsi muscles from 3 goat species were assigned to high and low drip loss groups. Physio-chemical properties, sarcomere length, and proteome profiles were investigated. The high drip loss group had lower pH, higher brightness, and higher shear force values, and shorter sarcomere lengths than the low drip loss group. 22 differential proteins were identified between high and low loss groups. α-Enolase, NADH dehydrogenase, pyruvate dehydrogenase E1, HSP27, superoxide dismutase, peroxiredoxin-2, myosin, and the myosin light chain were among these proteins, which were metabolic enzymes, stress response factors, and structural proteins that affected glycolysis, oxidation, and muscle contraction. Drip loss was probably produced via proteins involved in glycolysis, oxidation, and muscle contraction.