Preparation And Physicochemical Properties Of The Jellyfish Collagen Preparation And Physicochemical Properties Of The Jellyfish Collagen
Keywords
Jellyfish Collagen Medium And Low Temperature Physicochemical Propertiesjellyfish Collagen Medium And Low Temperature Physicochemical Properties
Abstract
Using jellyfish processing scraps as raw materials, a collagen preparation process was established under medium and low temperature conditions using citric acid as the extractant, and the physical and chemical properties of jellyfish collagen were analyzed. The results showed that the best enzymatic extraction of jellyfish collagen was The process conditions are: extraction temperature 15¡ãC, citric acid concentration 0.05mol¡¤L-1, pepsin addition amount 1.5%, solid-liquid ratio 1:2.0 (w:V) and extraction time 8h. Under these conditions, the collagen extraction rate is 97.41%. SDS-PAGE analysis results show that its possible structure is [¦Á1]3; in collagen, glycine, proline and hydroxyproline account for 25.16%, 7.62% and 9.32% of the total amino acids respectively; Fourie Infrared spectrum analysis of leaves shows that it retains a complete triple helix structure; viscosity and solubility characteristics show that its isoelectric point pI value is between 6 and 9; in the range of pH values ¡Ü1 and ¡Ý10, the structure tends to be unstable , the thermal denaturation temperature is 22.7¡ãC, and it basically precipitates in NaCl solutions greater than 1.0 mg¡¤mL-1. To analyze the physicochemical properties of jellyfish collagen, the leftover jellyfish was used as raw material, and treated with preparation technology. The preparation technology for collagen was based on the low-temperature condition and citric acid which worked as an extraction agent. The optimum enzymatic extraction condition was: temperature 15¡æ, 0.05mol¡¤L-1 citric acid concentration, 1.5% (mass fraction, the following are the same as) pepsin addition, 1:2.0 (w:V) solid-liquid ratio and 8h extraction time. The jellyfish collagen extraction yield of 97.41% under this condition. By performing purified collagen on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS- PAGE), the result demonstrated that collagen as Type I marine collagen in which three ¦Á1 chains each other. In collagen, glycine (Gly), proline (Pro) and hydroxyproline (Hyp) account for 25.16%, 7.62% and 9.32% of the total amino acids, respectively. Fourier transform infrared spectroscopy(FTIR) data of the collagen revealed that stable triple-helical structure was existence. Meanwhile, the viscosity and solubility of purified collagen were measured to evaluate the pI value of collagen about 6 to 9. When the pH value is less than or equal to 1 and above 10 range, structure tended to be unstable, thermal denaturation temperature 22.7¡æ. According to the experimental results, collagen would precipitate completely in NaCl solution when its mass concentration was above 1.0mg¡¤ mL-1
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Original research was done by Li Yufen, Zheng Mingxing, Zhu Fan, Lin Juan
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