Study On Mechanism Of High Temperature Deterioration And Texture Protection Of Procambarus Clarkii

Procambarus clarkii is rich in nutrition and delicious taste.It is a high-quality aquatic product with high protein and low fat.At present,the procambarus processing industry is still restricted by many factors.Many studies have shown that the gel property of myofibrillar protein plays a decisive role in the quality of meat and aquatic products.Therefore,it is of great significance to explore the gelatinous deterioration of Procambarus clarkii myofibrillar protein under high temperature and the influence of gel strengthening on the gelatinous property of Procambarus clarkii under high temperature to improve the quality change of Procambarus clarkii meat caused by high temperature,and provide theoretical basis for guiding the production and sterilization process of readyto-eat Procambarus clarkii and Procambarus clarkii meat products.This paper mainly studied the effects of high temperature treatment on the quality of Procambarus clarkii meat and the composition and components of myofibrillar gel and protein,and explored the effects of different gel enhancer on the properties of myofibrillar protein gel under high temperature.The main research contents and results are as follows:(1)Using different high temperature processing Procambarus clarkii,the results showed that heat treatment caused crawfish salt soluble protein and soluble protein content decreased significantly,insoluble protein content increased significantly.When processing temperature rised to 115 ℃,protein began to appear different degree of degradation,and degradation degree increased with temperature increasing.When the process temperature reached 121℃,the heavy chain of protein myosin was completely degraded,the bands disappeared,and the actin content was significantly reduced.The changes of protein components resulted in the loose structure and elastic loss of the crawfish meat,and the Procambarus clarkii meat could not be completely separated from the shell.Meanwhile,the results showed that the optimum processing temperature of Procambarus clarkii was 105℃,and the texture and sensory quality of the processed Procambarus clarkii were the best.(2)Extract myofibrillar proteins from Procambarus clarkii and explore the influence of different temperatures(100℃～121℃)treatment on myofibrillar protein gel.The results showed that the main components of Procambarus clarkii myofibrillar protein gel were protein myosin heavy chain and actin.Proper heat treatment is conducive to the formation of a dense and elastic gel network of Procambarus clarkii myofibrillar protein.When the treatment temperature exceeded 110℃,Procambarus clarkii myofibrillar protein showed different degrees of degradation,especially the degradation of protein myosin heavy chain.With the degradation of protein,the average particle size of protein decreased,hydrophobic interaction in the gel was weakened,and water freedom was increased,and gel pores were enlarged,and network skeleton became brittle.(3)To explore the influence of the amount of curdlan on the gelatinability of myofibrillar proteinllar protein under high temperature(121℃).The results showed that high temperature would change the structure of myofibrillar protein,seriously degrade the heavy chain of protein myosin,significantly reduce the content of actin,and seriously damage the structure of protein gel network.After adding 1%curdlan,the water holding capacity of the whole system basically reached the level of conventional protein gel and increased the content of curdlan.The water holding capacity of the gel system increased by 3.82%,8.96%and 13.38%,respectively.The elasticity and hardness of the gel system can basically reach the level of the conventional gel when adding 2%of the curdlan,and continue to increase the amount of the curdlan added,the hardness of the gel system increased by 19.32%and 47.57%,respectively,while the elasticity increased by 7.7%and23.62%.(4)Different concentrations of transglutaminase were added to the myofibrillar protein-curdlan composite gels.The results showed that transglutaminase was beneficial to cross-linking of myosin heavy chain and actin,which protected the protein degradation caused by high temperature,enhanced the function of protein in the composite gels,and changed the composite gel into a network structure composed of polysaccharides and proteins.The gel surface becomes smoother and more delicate.When the amount of transglutaminase is too high,the protein and enzyme will react rapidly,forming a dense network structure on the surface,hindering the binding of internal protein molecules and protein,and having adverse effects on the composite gel.