Extraction Of Collagen From Barramundi Scales And Skin And Analysis Of Its Physical And Chemical Properties
Keywords
Barramundi, Fish Scales, Fish Skin, Collagen, Amino Acids
Abstract
Using barramundi scales and fish skin as raw materials, enzyme-soluble collagen was extracted, separated and purified, and its amino acid composition was analyzed through sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Analysis, differential scanning calorimetry (DSC), Fourier transform infrared spectroscopy, X-ray diffraction, Zeta potential and solubility studies were conducted to analyze and compare its main physical and chemical properties. After freeze-drying, the yields (dry mass) of fish scale and fish skin collagen were 2.3 g/100 g and 47.3 g/100 g respectively; SDS-PAGE results showed that the configuration of both collagens was [¦Á1(¢ñ)]2¦Á2( ¢ñ), it is initially judged to belong to type ¢ñ collagen; DSC results show that the thermal denaturation temperatures (Td) of fish scale and fish skin collagen are 37.54 ¡æ and 36.74 ¡æ respectively; Fourier transform infrared spectroscopy and X-ray diffraction results show that collagen passes through the stomach The complete triple helix structure can still be maintained after protease treatment; Zeta potential results show that the isoelectric points of fish scale and fish skin collagen are pH 6.40 and pH 6.64 respectively; solubility study results show that the two collagens perform well under acidic conditions and low NaCl mass concentrations. showed good solubility under
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Original research was done by Qiu Changxu, Xia Guanghua, Liao Wei, Li Chuan, Li Yongcheng, Shen Xuanri
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