Study On The Physical And Chemical Properties Of Sturgeon Skin Collagen
Keywords
Acipenser Gueldenstaedtii Skin Acid Soluble Collagen Pepsin Soluble Collagen Physicochemical Properties
Abstract
This article uses Russian sturgeon skin as raw material, uses acid method and enzymatic method to extract collagen, and studies the protein type, structure, thermal denaturation temperature and solubility of acid-soluble collagen (ASC) and enzymatic-soluble collagen (PSC). properties and compared with bovine Achilles tendon type I collagen (BATC). SDS-PAGE electrophoresis shows that both ASC and PSC contain two ¦Á chains (¦Á1 chain and ¦Á2 chain), which are type I collagens; Fourier transform infrared spectroscopy shows that the extracted two types of collagen retain a complete triple helix structure. However, the degree of order of ASC is relatively high; the thermal denaturation temperatures of ASC and PSC are 32.48 ¡æ and 32.68 ¡æ respectively, which are lower than BATC; under acidic pH conditions (pH 1~4), ASC and PSC have higher solubility. When NaCl When the concentration is greater than 2%, the solubility of PSC is higher; scanning electron microscopy shows that both collagens have a network structure, and the pore size of ASC is more uniform and smaller. The above results show that different extraction methods lead to certain differences in the physical and chemical properties of the two types of collagen, but they both have better thermal stability and solubility, can form a better network structure, and have the potential to be used as a substitute for collagen. source. The skin of Acipenser gueldenstaedtii was used as the raw material in this study, and collagens were extracted using acid and pepsin extraction methods. The protein type, structure, thermal denaturation temperature, solubility, and other physicochemical properties of acid soluble collagen (ASC) and pepsin soluble collagen (PSC) were studied and compared with those of bovine achilles tendon type I collagen (BATC). SDS-PAGE patterns revealed that both ASC and PSC contained two typical ¦Á chains (¦Á1 chain and ¦Á2 chain) and were type I collagens . The Fourier transform infrared spectroscopy (FT-IR) results indicated that both extracted collagens had a triple helical structure, but ASC had a higher degree of molecular order. The denaturation temperatures of ASC and PSC were 32.48 ¡æ and 32.68 ¡æ, respectively, which were lower than that of BATC. Both ASC and PSC had a relatively high solubility at acidic pH (pH 1~4). PSC had a higher solubility when the NaCl concentration was higher than 2%. Scanning electron microscopy (SEM) showed that the two collagen sponges had a network structure, and the pore size of ASC was relatively uniform and small. These results indicate that different extraction methods may lead to certain differences in the physicochemical properties of ASC and PSC; however, both collagens have good thermal stability and solubility, as well as the ability to form a better network structure than BATC. Therefore, the skin from Acipenser gueldenstaedtii can serve as an alternative source of collagens.
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Original research was done by Chen Minghui
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