Researches On The Properties Of Common Carp(Cyprinus Carpio) Myofibrillar Proteins

As an important part of Common Carp meat, Common Carp Myofibrillar Protein (CCMP)is closely related to many processing properties. For now, few papers investigated properties ofCCMP, the futher processing of Common Carp is limited. Therefore, this paper studied on theproperties of the myofibrillar proteins extracted from Common Carp in different experimentalconditions, such as solubility, emulsifying, foaming and gel properties. In order to improve gelproperties, the research on the optimal process of transglutaminase (TG) and CCMP wasdiscussed. Hydrolysates with strong antioxidant activity were prepared by means of enzymatichydrolysis technology on CCMP. The main work in this paper was concluded as follows:1. Common Carp protein content is17.72%, and myofibrillar protein content is9.86g (100gmuscle) accounting for55.64%of total protein. The results of myofibrillar protein bySDS-polyacrylamide showed that myosin, actin, tropomyosin and other small molecular proteinconstituted myofibrillar protein. Myosin was the major protein of myofibrillar protein.2. Studying on the functional properties of CCMP, the results showed that solubility ofCCMP had higher capability with deviation isoelectric. And CCMP is easy to be dissolved in0.6~1.0mol/L NaCl solution. Emulsifying and foaming properties of CCMP was changedsignificantly by changes of pH, NaCl concentration, protein concentration and temperature.Different factors conditions had different effect on emulsifying and foaming properties ofCCMP.3. Studying on Gel properties of CCMP, the results showed that the optimal process ofCCMP gel strength was at80℃, pH6,0.6mol/L NaCl concentration. Gel strength of CCMP wasimproved significantly by addition of TG. By single factor experiment and response surfaceexperiment, results showed that the optimal process of CCMP gel strength as follows: pH6,reaction temperature at42.5℃, reaction time for2.25h, and TG content with0.66%. Gel strengthwas better under the optimum condition, up to179.461g.4. Studying on enzymatic hydrolysis process of CCMP, the results showed that higherantioxidant activity of hydrolysates obtained by papain. By single factor experiment andresponse surface experiment, the best condition of the enzyme hydrolysis process was:hydrolysis temperature was55.6℃, enzyme addition was1118U/g and hydrolysis time is2.1h. Then, the biggest reduction power is0.861, in the condition of pH7and4%substrate. The studyon functional properties of hydrolysates showed that hydrolysates of CCMP had better solubilityat different conditions of pH and NaCl concentration. And emulsifying and foaming properties ofhydrolysates was changed significantly by changes of pH, NaCl concentration, hydrolysatesconcentration and temperature. Comprehensive comparison with the emulsifying and foaming ofCCMP and hydrolysates, it demonstrated that emulsifying properties and foam stability ofCCMP was higher than hydrolysates. But foaming capacity was inferior to hydrolysates.