Influence Of Regulating Superchilling On The Quality And Physicochemical Properties Of Common Carp Muscle During Storage

Superchilling preservation technology in preservation and circulation of aquatic products can not only play the role of long-preservation during storage, but also a certain role in improving product quality. The objective of the present study was to investigate quality and myofibrillar protein structure and functional and gel changes in common carp muscle during superchilling and frozen storage, to clarify the quality of superchilling during storage of fish changes and the extent of protein denaturation. By regulating the freezing point to observe the extent of changes of fish quality and the mitigation of the extent of protein denaturation, thus further understand the mechanism of regulating the fish freezing point and thus protection of protein.At-1℃superchilling storage of common carp muscle,with increasing the time of storage, the L*values and whiteness decreased significantly (P<0.05), thiobarbituric acid number (TBARS values), volatile base nitrogen (TVB-N) and total colonies number increased(P<0.05), and at the same time myofibrillar protein Ca2+-ATPase activity, the active sulfhydryl and total sulfhydryl content decreased, while the carbonyl content increases (P<0.05); from-1℃to reduce the freezing point temperature of carp muscle by regulating freezing point to-3℃,stored at that temperature, the total number of colonies, TRBAS value and TVB-N content was significantly lower than-1℃superchilling storage of surimi (P<0.05), and myofibrillar protein Ca2+-ATPase activity, the active sulfhydryl and total sulfhydryl content decreased extent and carbonyl content increased by extent were less than-1℃superchilling storage of crap muscle (P<0.05), by SDS-PAGE electrophoresis showed that the superchilling storage of protein to varying degrees of degradation, and the longer the storage time, the degree of protein degradation is more significant (P<0.05).Superchilling storage has changed the structure of the carp protein, thus affecting the myofibrillar protein functional. With the extension of storage time, the emulsifying activity and emulsion stability of the carp protein was significantly decreased at-1℃superchilling conditions during storage(P<0.05), the surface hydrophobicity increased significantly (P<0.05); add freezing point regulator storage of crap muscle with higher vitality of the emulsification and emulsion stability and a lower surface hydrophobicity (P<0.05) relative to the myofibrillar protein in the fresh sample of common storage.Storage of superchilling weakening of the carp muscle and myofibrillar protein gel-forming ability, causing the decline of the gel hardness and elastic, gel micro-structure is a more direct description of this result. Fresh fish protein to form a dense, uniform, smooth surface and three-dimensional network structure, the gel formed to loose structure, the aperture increases, micelles rough, broken, dough structure, even the collapse of the phenomenon, gel whiteness decreased after the protein extracted. However, regulating freezing point to improve the deterioration of the quality of the gel.