Myofibrillars and Sarcoplasmic Proteins Separated The Effect of Different Preservation and Cooking Methods on Functional Characteristics of From Common Carp and Silver Carp Prof.
Authors: Sadiq Khadeeja , Al-Hussainy Jaffer , Al-Robeay Hala Yhya Essa 
Published: November 2021

Abstract
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.