Heat-induced Gel Properties And Interaction Of Chicken Myosin And 11S Globulin

In recent years,chicken products occupy a larger market development space with its unique nutrition and flavor characteristics,so the research of chicken protein functional properties have attracted much attention.Gelation is the most important functional property of myosin,which is the most important of muscle protein and the functional properties of which determines the meat quality.Processing of meat products is the interaction between proteins and other materials,and also the aggregation or crosslinking of muscle proteins for gel formation.The interaction mechanism between muscle protein and soybean protein often used in meat processing is not clear.The research of which is very few in the world,and the interaction between 11S and myosin is rare.So,with the mixed gels of 11S and myosin for the study object,by the modern biotechnological means of SDS-PAGE?TPA?NMR?SEM and FTIR,this project aim to analysis the quality characteristics of the mixed gels,discuss the chemical and physical change law of protein,explore the interaction between the proteins during the formation of the myosin gels,in order to provide the theoretical foundation and scientific basis for the meat product development,process innovation and quality assessment.Conclusions below were obtained from the research:1.Study on the extraction,purification and identification methods for myosin and 11S were carried.Precipitation frequency of actomyosin was 3 times during the myosin extraction.,The initial saturation concentration of ammonium sulfate precipitation is 35%,and final is 48%.The end pH is 6.4 for 11S extraction and 2 times for purification.Purity of proteins was more than 90%.2.Control methods of mixed gel qualities were researched.2?4%11S was beneficial to form the mixed gel with high WHC and proper hardness;The mobile water and free water content increased and the mixed gel strength and water retention was more ideal,when pH was at 6-6.5 with ionic strength of 0.6-0.8mol/L.6-8mmol/L Ca²⁺ made the mixed gel microstructure dense,the mobility of gel and the content of water significantly increased.The addition of Mg²⁺decreased the content of free water and mobile water,and induced the microstructure of the mixed gel more compact.4-6 mmol/L PO₄^3-made the mobile water content higher,the gel strength decreased significantly,and the microstructure dense,the network structure not obvious.3.The interaction mechanism was established between 11S and myosin protein.Based on the above results,by analysising the relationship between mixed gel qualities and secondary structures,and discussing the physical and chemical characteristics of the mixed protein during heat-treatment,the interaction mechanism between 11S and myosin on different conditions was established.?1?With the addition of 2-4%11S,the interaction between 11S and myosin decreased the denaturation temperature of myosin,improved the gel WHC,and transfered beta angle structure to other structures.?2?Under acidic conditions,the interaction between 11S and myosin formed larger polymers,decreased the thermal stability of proteins,made more active groups exposed,increased protein cross-linking,and transferred the alpha helix and beta angle structures to other structures.?3?With the ionic strength of 0.4-0.6mol/L,the interaction increased the solubility,stability,and cross-linking of proteins,transfered alpha helix structure to other structures,decreased the ratio of alpha helix and beta folding structure,and improved the gel qualities.?4?With the addition of Ca²⁺,the interaction increased the solubility,stability of proteins,made more active groups exposed,transfered the alpha helix and beta folding structure to other structures,and increased the ratio of alpha helix and beta folding structure.?5?With the proper concentration of Mg²⁺ and PO₄^3-,the interaction changed the conformation of proteins,reduced the solution turbidity,improved the myosin denaturation temperature,made more active groups exposed,improved the cross-linking of protein,transfered the beta folding structure to other structures,increased the ratio of alpha helix and beta folding structure,improved the gel WHC.4.The application experiments of the interaction between 11S and the myosin protein to improve the qualities of smoked and cooked chicken sausage were carried.?1?2-4%soy protein isolate enhanced the water mobility of smoked and cooked chicken sausage,increased the free water content,and improved the yield,color,texture,flavor and other sensory qualities.?2?Improving the salt content had no significant effect on sensory qualities,but improved the yield,water retention,texture,water mobility and free water content of chicken sausage.0.5%KCL instead of salt had no significant effect on the texture,water retention,sensory qualities of smoked and cooked chicken sausage.So,KCL instead part of NaCL in the low-salt product development is feasible.?3?Addition of calcium chloride improved the texture and color of the smoked and cooked chicken sausage,but decreased the mobile water content and had a negative effect on water retention,yield,smell,taste and other qualities.?4?The appropriate concentration of Mg²⁺ increased the water retention and yield,improved the texture,color and taste,had no significant effect on sensory qualities,but had a negative impact on the smell of smoked and cooked chicken sausage.?5?1.0‰ pyrophosphate increased the bound mobile water content,and significantly improved the color,texture and taste of the smoked and cooked chicken sausage.In summary,the following conclusions were obtained:?1?The construction of method for protein extraction,purification and identification methods and method is feasible.?2?The control method of mixed gel qualities was formed.?3?The interaction mechanism was established between 11S and myosin protein.?4?The application experiments proved that interaction between 11S and myosin protein improved the meat products qualities.