Physicochemical and Fibril Formation Properties of Pufferfish (Takifugu obscurus) Skin Collagen from Solvent Extraction in Different Conditions
文献类型： 外文期刊
作者： Wang, Shanshan 1 ; Zhou, Deqing 1 ; Liu, Nan 1 ; Sun, Yong 1 ; Sun, Guohui 1 ;
作者机构： 1.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Qingdao 266071, Peoples R China
2.Pilot Natl Lab Marine Sci & Technol Qingdao, Lab Marine Drugs & Bioprod, Qingdao 266237, Peoples R China
关键词： pufferfish skin; acid-solubilized collagen; pepsin-solubilized collagen; fibril formation; microstructural characteristic
期刊名称：GELS （ 影响因子：4.6； 五年影响因子：5.2 ）
ISSN：
年卷期： 2023 年 9 卷 1 期
页码：
收录情况： SCI
摘要： Acid-solubilized (ASC) and pepsin-solubilized collagen (PSC) extracted at 4 degrees C (ASC-4 and PSC-4), 12 degrees C (ASC-12 and PSC-12), and 20 degrees C (ASC-20 and PSC-20) from the skin of farmed pufferfish (Takifugu obscurus) was characterized by SDS-polyacrylamide gel electrophoresis (SDS-PAGE), Fourier-transform infrared spectroscopy (FTIR), and fibril-forming tests. The results indicate that extraction at 12 degrees C can effectively improve the extraction efficiency of natural collagen compared with extraction at 4 degrees C. However, extraction at 20 degrees C results in a decrease in molecular integrity, thus, inducing the resultant collagen to degrade or even lose fibril-forming ability. Transmission electron microscope (TEM) images revealed that ASC-4, PSC-4, ASC-12, and PSC-12 can assemble into fibrils with D-periodicities, and ASC-20 associated into molecular aggregates alongside partial D-banded fibrils, while no well-defined fibrils were observed in PSC-20. Scanning electron microscope (SEM) analysis confirmed the well-defined fibril morphologies of ASC-4, PSC-4, ASC-12, and PSC-12 with imino acid contents between 190.0 and 197.8 residues/1000 residues. The denaturation temperature of ASC-4, PSC-4, ASC-12 and PSC-12 was 30.0, 27.6, 25.9 and 22.7 degrees C, respectively. This study indicates that ASC and PSC extracted at 4 degrees C and 12 degrees C could be alternatives to terrestrial collagens for industrial applications.
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