Effects Of Fish Skin Collagen Based On Different Extraction Methods On The Quality Of Recombinant Fish Meat
Keywords
Fish Skin Collagen Extraction Method Restructured Fish Gel Characteristics Mechanism Of Action
Abstract
In order to improve the quality of freshwater surimi products, this study used grass carp as raw material to extract collagen from catfish skin using salt method, acid method and alkali method to explore its effect and mechanism on the quality of recombinant fish meat. By analyzing the changes in gel strength, TPA texture characteristics (hardness and chewiness), water separation rate and whiteness value of the recombinant fish meat, the impact of collagen on the quality of the recombinant fish meat was comprehensively evaluated, and through the chemical force and protein solubility rate and TCA soluble peptide content, as well as paraffin tissue sections and SDS-PAGE to explore the mechanism of fish skin collagen in restructured fish meat. The results showed that collagen significantly improved the quality characteristics of recombinant fish meat, and the improvement effect was alkaline method>acid method>salt method; and its mechanism of action was also different: during the process of alkali-soluble collagen and surimi gel, not only disulfide bonds were formed , and activates endogenous transglutaminase (TG) to generate more non-disulfide covalent bonds, enhancing the gel network structure; acid-soluble collagen forms disulfide bonds during gelation, enhancing the gel force. ; The polymer material formed by salt-soluble collagen and fish protein strengthens the gel network structure. To improve the quality of minced freshwater fish products, restructured fish products were prepared using grass carp as a raw material, and the effects of extraction method, and particularly of salt, acid, and alkaline solutions, were examined. Gel strength, textural characteristics ( hardness and chewiness), syneresis rate, and change in whiteness of the restructured fish were examined to comprehensively evaluate the effects of extraction method on collagen properties and the quality of restructured fish. Furthermore, the chemical bonding force, trichloroacetic acid (TCA) soluble peptide content, paraffin tissue sections, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) were used to study the collagen properties of restructured fish. The quality of restructured meat with respect to collagen quality was optimal for extraction with the alkaline solution, intermediate for acid, and lowest for the salt solution. Furthermore, alkali-soluble collagen not only formed disulfide bonds during the gelation of minced fish, but also formed non-disulfide bonds via the activation of endogenous transglutaminase (TG), strengthening the gel network structure . Acid-soluble collagen formed disulfide bonds during the gelation of minced fish and had increased gelation force. Salt-soluble collagen formed more macromolecules, thus enhancing the gel network.
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Original research was done by Zhao Li
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