Comparison of Physicochemical Characteristics and Fibril Formation Ability of Collagens Extracted from the Skin of Farmed River Puffer (Takifugu obscurus) and Tiger Puffer (Takifugu rubripes)
文献类型： 外文期刊
作者： Wang, Shan-Shan 1 ; Yu, Ying 1 ; Sun, Yong 1 ; Liu, Nan 1 ; Zhou, De-Qing 1 ;
作者机构： 1.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Qingdao 266071, Shandong, Peoples R China
2.Pilot Natl Lab Marine Sci & Technol Qingdao, Lab Marine Drugs & Bioprod, Qingdao 266237, Shandong, Peoples R China
关键词： puffer fish; acid-soluble collagen (ASC); pepsin-soluble collagen (PSC); fibril formation; fibril morphologies
期刊名称：MARINE DRUGS （ 影响因子：5.118； 五年影响因子：5.951 ）
ISSN：
年卷期： 2019 年 17 卷 8 期
页码：
收录情况： SCI
摘要： Acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from the skin of river puffer (ASC-RP and PSC-RP) and tiger puffer (ASC-TP and PSC-TP) were extracted and physicochemically examined. Denaturation temperature (T-d) for all the collagens was found to be 25.5-29.5 degrees C, which was lower than that of calf skin collagen (35.9 degrees C). Electrophoretic patterns indicated all four samples were type I collagen with molecular form of (alpha(1))(2)alpha(2). FTIR spectra confirmed the extracted collagens had a triple-helical structure, and that the degree of hydrogen bonding in ASC was higher than PSC. All the extracted collagens could aggregate into fibrils with D-periodicity. The fibril formation rate of ASC-RP and PSC-RP was slightly higher than ASC-TP and PSC-TP. Turbidity analysis revealed an increase in fibril formation rate when adding a low concentration of NaCl (less than 300 mM). The fibril formation ability was suppressed with further increasing of NaCl concentration, as illustrated by a reduction in the turbidity and formation degree. SEM analysis confirmed the well-formed interwoven structure of collagen fibrils after 24 h of incubation. Summarizing the experimental results suggested that the extracted collagens from the skin of river puffer and tiger puffer could be considered a viable substitute to mammalian-derived collagens for further use in biomaterial applications.
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