| With the rapid development of China’s poultry products, the demand for the type of meatproduction is increasingly diverse in recent years. Especially because of the broad space fordevelopment of chicken deep processing products, the exploitation of basic research of chickenis imminent. This test is studied on the properties of the myofibrillar proteins extracted from thethigh meat, in order to provide a theory for the further development of the chicken deepprocessing products.First, the study taked the antioxidants which obtained from the Papain hydrolysis ofmyofibrillar proteins as the object of study and DPPH radical scavenging rate as index tooptimize the conditions of hydrolysis by orthogonal experiment method. The results showed thatthe best condition of the enzyme hydrolysis process was: the enzyme amount of0.6%, thesolid-liquid ratio of1:5, the reaction temperature was50℃, reaction time was3h. And at thistime, DPPH radical scavenging rate of hydrolyzate is84.7%. The enzyme hydrolyzate had astrong antioxidant activity. Under optimized conditions, the protein structural of chickenmyofibrillar protein after papain hydrolyzed had changes which can observed by SDS-PAGE gelelectrophoresis. And experiments on the oxidation resistance studies of the hydrolysis productsshow that the hydrolysates of myofibrillar proteins in the concentrated evaporation, dry,sunlightin and long-term storage had good stability.In order to improve the quality of meat products processing, this article on myofibrillarprotein gel properties were studied. At first, transgluninase doses, GDL doses as well as pH valueand sodium concentrations were optimized by single factor test, based on which Box-Benhnkencenter-united experiment was designed for optimization of ratio scheme for gelation to improvethe quality by response surface method using gel strength as an indicator. Results: The optimumconditions for best gel strength were found to be: the myofibrillar proteins with0.37%transgluninase doses,1.19%GDL doses were homogenized in0.88mol/L sodium concentrationat pH5.96to form40mg/ml protein concentration solution. Under these optimum conditions,thegel strength was316.953g. The study showed that optimization transgluninase doses and GDLdoses could improve gel strength significantly and had interaction.The texture analysis on the thermally induced gel adding different ratio of TG and GDL showed that the addition of TG and GDL could significantly increase in gel hardness, gumminessrespectively. The right amount of TG could improve the elasticity of the gel, and excess TG dosecaused the gel elasticity decreased. Besides the increasing amount of GDL will cause theformation of gel cohesiveness decreased. In the comparation of various ratio of TG and GDL inthe thermally induced gel, the best group of the amount of TG: GDL,1:1(0.36%TG,1.2%GDL),was obtained. This is consistent with the results of response surface.Results from the rheological testing of the MP suspensions with or without TG and GDL atvarious salt concentration levels upon heating showed that the combination of TG and GDLproduced the strongest gels across all the salt levels than respective treatments, with a greatereffect observed at increasing salt concentrations. In other words, the storage modulus G’ of theMP suspensions treated by TG and GDL dramatic increased.That’s because of good crosslinkingin the formation of gel network. In addition, myofibrillar proteins are salt-soluble proteins, withthe increase of the ion levels, and its solubility is also increased. Combined with the effect of theTG and GDL, myofibrillar protein suspension in the high salt concentration relative to the lowsalt concentration had larger storage modulus G’. In each level of salt concentration, the effect ofTG was larger than GDL. |
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