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 )

• Published in: Marine drugs Vol. 17; no. 8; p. 462
• Main Authors: Wang, Shan-Shan, Yu, Ying, Sun, Yong, Liu, Nan, Zhou, De-Qing
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 07.08.2019; MDPI
• Subjects: acid-soluble collagen (ASC); Acids - chemistry; Amino acids; Amino Acids - chemistry; Animals; Biomaterials; Biomedical materials; Biopolymers; Catfish; Collagen; Collagen (type I); Collagen Type I - chemistry; Consumption; Denaturation; fibril formation; fibril morphologies; Fibril-Associated Collagens - chemistry; Fibrils; Fish Proteins - chemistry; Foot & mouth disease; Fourier transforms; Hydrogen Bonding; Hydrogen bonds; Incubation period; Pepsin; Pepsin A - chemistry; pepsin-soluble collagen (PSC); Periodicity; Polypeptides; puffer fish; Rivers; Skin; Skin - chemistry; Sodium chloride; Solubility; Spectrum analysis; Takifugu - metabolism; Temperature; Tetraodontiformes - metabolism; Turbidity; China; fibril morphologies; acid-soluble collagen (ASC); fibril formation; pepsin-soluble collagen (PSC); puffer fish
• ISSN: 1660-3397; 1660-3397
• DOI: 10.3390/md17080462

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 ) for all the collagens was found to be 25.5-29.5 °C, which was lower than that of calf skin collagen (35.9 °C). Electrophoretic patterns indicated all four samples were type I collagen with molecular form of (α ) α . 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.