Myofibrillars and Sarcoplasmic Proteins Separated The Effect of Different Preservation and Cooking Methods on Functional Characteristics of From Common Carp and Silver Carp Prof.

The current study dealt with the use of methods of preserving (freezing and salting with drying), cooking methods (grilling and cooking in broth and frying) and studying their effect on functional characteristics (solubility, amount of water and oil absorbed, viscosity, emulsification, foaming, gel formation) of myofibrillars and sarcoplasmic proteins separated from carp meat, common and silver carp diagnosed with electrophoresis technique, the study was conducted during the period (10/2018-1/2020). The results were as follows: 1. Dried fibrous proteins and dried sarcoplasm proteins separated from fish meat have given a good functional properties compared to commercial cow's albumin. 2. It was found that the percentage of solubility and gelatinization of commercial cow's albumin protein was higher than in the myofibrillars and sarcoplasmic proteins separated from the two types of fish, whereas the amount of water absorbed by the commercial cow's albumin protein was less than of myofibrillars and sarcoplasmic proteins, while the amount of absorbed oil, viscosity, and emulsion composition. The commercial cow's albumin was comparable to the myofibrillars and sarcoplasmic proteins, and when comparing the foam properties of the myofibrillars and sarcoplasmic proteins of common carp and silver carp with the commercial cow's albumin at a concentration of 1% and at the normal pH=7, it was found that the foam size and persistence of sarcooplasmic proteins were close to the size and persistence of the foam for the commercial protein at the normal pH, while the volume and stability of the foam for myofibrillars proteins were slightly lower than in cow's albumin. 3. It was observed that the solubility values in the myofibrillars proteins and the sarcoplasmic proteins of the samples were close to each other when using preservation methods while the solubility of the myofibrillars proteins was lower than the solubility of the sarcoplasm proteins of the cooked samples. It was found that the amount of oil absorbed by the myofibrillars proteins was higher than the sarcoplasmic proteins, but that its viscosity and its ability to bind water and its ability to form gel were lower than it, and the capacity of emulsifiers of protein myofibrillars and their stability was higher than the capacity and the stability of emulsions of sarcoplasm proteins, as for the type of fish and the type of protein stability of emulsions, it was noted that there was a slight difference in the capacity of emulsions and the stability of emulsions for myofibrillars proteins as well as for sarcoplasm proteins. The emulsification values did not seem different between the two types of fish. 4. It was found that freezing contributed to reducing solubility and the amount of water absorbed while it had a role in increasing the amount of oil absorbed to fish proteins more than salting and drying. The freezing, as well as salting and drying were reduced the viscosity of proteins a little bit, also freezing reduced stability of emulsionsfor two type of fish proteins,but salting and drying was rised it, and the degree of influence of the measured foam property in myofibrillars and sarcoplasmic proteins of the fish species by means of preservation and cooking different methods was very small because the values were closely related, and we did not find a specific pattern that we could apply in terms of challenging degree of difference, freezing and salting with drying, grilling and frying and cooking in the broth sometimes susceptibility raises values formation of foam and other reduce it. 5. The solubility of proteins that measured on fish which cooked in broth was more than the solubility of grilled and fried samples. It was observed that the solubility values in myofibrillars proteins and sarcoplasm proteins for the cooked samples were close to each other, and the amount of water and absorbed oil, foam properties and viscosity of the measured proteins in cooked fish were not affected by the cooked methods whose used because the closely related of values. 6. Generally the results showed that the solubility and viscosity values in the samples of common carp were lower than in the silver carp which preserved and cooked by different ways, but the ability of common carp to bind the oil was higher than that of silver carp when using conservation methods while the values were close at the use of cooking methods, and we noted that there were no noticeable differences between myofibrillars proteins and sarcoplasmic proteins for the two fish species in their ability to bind water and their ability to form gel. It was also noted that there was a slight difference in the capacity of emulsions and their stability to myofibrillars proteins as well as to proteins sarcoplasm between the two types of fish. 7. The fish type, preservation methods, cooking methods, and di-interference had a significant effect at the probability level (P ≤ 0.05) on the percentage of solubility and the amount of water and oil absorbed by the myofibrillars and sarcoplasmic proteins separated from the meat of these fish, but did not significantly impact the viscosity of the protein.

Studying Chemical Composition of Myofibril and Sarcoplasmic Proteins Separated From Different Types of Meats

The present study was dealt with the estimation of the chemical composition (moisture, protein, fat, and ash) and physical properties (pH and water holding capacity) of camel, duck, and tuna meat purchased from local markets. Muscle proteins were separated, including myofibril and sarcoplasmic proteins from these meats, estimation of the yield and study of their content. have been studied. the results were as follows: 1. Statistical results disclosed that there was a significant difference at a probability level (P≤0.05) in the percentage of moisture, protein, fat, ash, pH, and values of water holding capability in each of camel, duck, and tuna's meat. 2. Statistical results made a clear reference that there were significant differences at a probability level (P≤0.05) in the percentage of yield, moisture, protein, fat, and ash of myofibril and sarcoplasmic proteins in each of camel, duck, and tuna's meat. Also, a dual interference between meat type and protein type was significant in its impact on percentages of yield and chemical composition. 3. It was observed the percentage of moisture and fat in tuna meat was higher than the percentage of moisture in duck meat. As to the lowest percentage of moisture, it was in the meat of tuna, while the tuna meat recorded the highest percentage in protein and ash, then followed by the percentage of protein and ash in duck meat, while camel's meat recorded the lowest percentage of protein and ash. Besides, results indicated that the values of pH and water holding capability of duck meat were higher than that in the meat of tuna meat and camel. 4. It was found that the percentage of the yield for proteins of a myofibril of duck meat was higher than that in the meat of tuna and camels, as the percentage of yield of sarcoplasmic proteins for tuna was higher than that in the meat of duck and camels. 5. It was found that the percentage of yield for myofibril of duck meat was higher than that in the meat of tuna and camels. As to the percentage of yield for sarcoplasmic proteins of tuna meat, it was higher than that in the meat of duck and camels. 6. The highest percentage of moisture for myofibril proteins was in the meat of camels, and the lowest percentage of it was registered in myofibril proteins in tuna meat, whilst the highest percentage of moisture for sarcoplasmic proteins was registered in the meat of duck, and the lowest of it registered in sarcoplasmic proteins in tuna meat. 7. It was observed that the highest percentage of protein and fat for myofibril and sarcoplasmic proteins was registered in tuna meat, as the lowest percentage of protein and fat for myofibril and sarcoplasmic proteins were observed in duck meat. 8. The study came up with a result revealing that the percentage of ash in proteins of myofibril proteins for duck meat was higher than that in myofibril proteins for camels and tuna meat, whilst, the percentage of ash in sarcoplasmic proteins for camel meat was higher than that in sarcoplasmic proteins for duck and tuna meat. 9. Results showed that the highest concentration of sarcoplasmic proteins was in tuna meat, followed by duck meat, and the lowest concentration for these proteins was in camel meat. The values of proteins (myosin, tropomyosin, reticulin, and collagen) in camel meat, then followed by duck meat, whilst the lowest values for these proteins were in tuna meat.

Antiglycating Effect of Phenolics from the Chilean Currant Ribes cucullatum under Thermal Treatment

Numerous dietary polyphenols possess antiglicating activity, but the effects of thermal treatment on this activity are mostly unknown. The effect of thermal treatment in the antiglycating activity of polyphenolic enriched extracts (PEEs) from Ribes cucullatum towards glyoxal-induced glycation of sarcoplasmic proteins was assessed. Sarcoplasmic proteins from chicken, beef, salmon, and turkey, were incubated 2 h at 60 °C with and without glyoxal and different concentrations of PEEs (0.25, 0.5, 1, and 5 mg/mL). The antiglycating activity was evaluated by: (1) Lys and Arg consumption, (2) Carboxymethyl lysine (CML) generation, and (3) lipid-derived electrophiles inhibition in a gastric digestion model. Protective effects were observed against CML generation in proteins and a decrease of electrophiles in the gastric digestion model. A dose-dependent consumption of Lys and Arg in proteins/PEEs samples, indicated the possible occurrence of quinoproteins generation from the phenolics. Protein/PEEs incubations were assessed by: (1) High pressure liquid chromatography analysis, (2) Gel electrophoresis (SDS-PAGE), and (3) Redox cycling staining of quinoproteins. Protein/PEEs incubations produced: (1) Decrease in phenolics, (2) increase of protein crosslinking, and (3) dose-dependent generation of quinoproteins. We demonstrate that phenolic compounds from R. cucullatum under thermal treatment act as antiglycating agents, but oxidative reactions occurs at high concentrations, generating protein crosslinking and quinoproteins.

The Effect of Point Mutations in the RYR-1 Gene on the Physicochemical Properties of Meat

The impact of gene mutations in the RYR-1 gene on the physicochemical qualities and nutritional value of homozygous and heterozygous stress-resistant NOR carcasses with RSE and DFD defects was studied using molecular genetics methods. NOR, which is meat of homozygous cross-breeding pigs, had a 0.44 higher pH level, 2.62% higher water-holding ability, 2.36 units×103 higher color and 0.37% higher content of organic matter; the tryptophan content and protein-quality index were lower by 0.3 mmol/g and 0.29, respectively. This low acidity caused the denaturation of some sarcoplasmic proteins, which contributed to the loss of the meat’s water-holding ability. A sharp decrease in pH led to partial denaturation of the sarcoplasmic proteins, which determined the pale color of the PSE meat. It was found that, compared to the heterozygous stress-sensitive animals with DFD defects, the NOR pH level was 0.55 lower, the water-holding ability was 4.05% lower, and the color intensity was 4.97 units×103 lower; the protein-quality indicator amounted to 8.24, which was 1.12 higher than that in the heterozygous stress-sensitive animals with DFD defects. The defects had a significant impact on other physicochemical properties of the meat. Defects of PSE meat worsened meat color. The intensity of staining of muscle tissue with PSE defects was lower than in normal pork by 11.5, 8.7 and 6.4 units×103 , respectively. DFD-pork exceeded normal meat in color by 13.7 (P> 0.99), 9.5 (P> 0.99) and 7.4 units×103 . Keywords: stress tolerance, stress sensitivity, genotype, meat defects PSE and DFD-, RYR-1 gene, pH, water-holding ability, meat coloring