Study On The Isolation, Purification And Physical And Chemical Properties Of Acid-Soluble And Enzyme-Soluble Collagen From The Head Of Navodon Septentrionalis
Keywords
Horse Puffer Fish, Fish Head, Acid-Soluble Collagen, Enzyme-Soluble Collagen
Abstract
Acid-soluble collagen (ASC) and enzyme-soluble collagen (PSC) of horse-faced puffer fish head were prepared by acid-soluble method and enzymatic method, and the amino acid composition, SDS-PAGE, infrared spectrum, and viscosity of the prepared ASC and PSC were analyzed. And thermal denaturation temperature, as well as solubility and other properties were analyzed. The results showed that the extraction rates of ASC and PSC from the pufferfish head were 0.94% ¡À 0.07% and 3.91% ¡À 0.14% respectively. The contents of Gly (265.0 and 251.8 residues/1000 residues), Ala (111.0 and 107.6 residues/1000 residues) and Pro (87.0 and 83.1 residues/1000 residues) are higher, while the contents of His and Tyr are lower , and Cys was not detected. The imino acid (Pro and Hyp) contents in ASC and PSC are 169.3 and 160.6 residues/1000 residues. Amino acid composition analysis, SDS-PAGE and infrared spectroscopy (FTIR) confirmed that ASC and PSC both belong to type I collagen, with thermal denaturation temperatures of 17.6 ¡æ and 16.5 ¡æ respectively. In the acidic pH range, the solubility of ASC and PSC is high; when the concentration of NaCl solution is higher than 2%, the solubility of ASC and PSC will be significantly reduced. In summary, compared with mammalian collagen, ASC and PSC from horsetail fish head have lower imino acid content and thermal denaturation temperature, poor structural stability, and are easy to degrade, and can be developed as raw materials for the preparation of collagen peptides.
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Original research was done by Zhao Yuqin, Wang Yumei, Wang Bin, Chi Changfeng, Ding Guofang
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