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)

Abstract

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 (Td) 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 (α1)2α2. 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.

Physicochemical and Functional Properties of Type I Collagens in Red Stingray (Dasyatis akajei) Skin

“…The thermal denaturation temperatures of ASC and PSC from red stingray skin were 23.82 °C and 24.46 °C, respectively (Figure 5A). These values were similar to collagens from the swim bladders of miiuy croaker (T d = 24.7 °C, ASC; 26.7 °C, PSC) [35], the skins of tiger puffer (T d = 28.0 °C, ASC; 25.5 °C, PSC) [36], and of Axenillidae (T d = 24.3 °C) [4], but lower than the skins of giant croaker (T d ≈ 34.5 °C, ASC; 34.5 °C, PSC) [37] and of river puffer (T d = 29.5 °C, ASC; 27.5 °C, PSC) [36]. Furthermore, these values were higher than those for the skins of pacific cod (T d = 14.5 °C, ASC; 16.8 °C, PSC) [8] and Spanish mackerel (T d = 15.12 °C, ASC; 14.66 °C, PSC) [38].…”

Enhanced Wound Healing Activity of Undenatured Type I Collagen Isolated from Discarded Skin of Black Sea Gilthead Bream (Sparus aurata) Conditioned as 3D Porous Dressing

“…The FT‐IR spectra of BSC and BC exhibited an absorption ratio around 1 between the amide III vibration and the band corresponding to C−N stretching vibrations of pyrrolidine rings from 1449 cm −1 , [29] which indicated the triple helix conformation presence. All these results indicated that the secondary and tertiary structure of BSC analyzed by FT‐IR spectroscopy were similar to those of other marine collagens extracted from salmon, codfish, river puffer and tiger puffer [28–30] . As compared to BC, BSC preparation presented a shift of amide A and amide B bands towards lower frequencies, showing lower structural order of the latter.…”

“…It was previously showed that the thermal stability of collagen isolated from fish skin was clearly influenced by water temperature [9] . Thus, the Td of collagen isolated from most fish species displayed values below 37 °C [28] . It was documented that, at temperatures higher than Td, the triple helix of collagen molecule was dissociated into a random coil structure, affecting its physicochemical, mechanical and biological properties [12] .…”

Characteristics and Functional Properties of collagen extracted from Nile tilapia (Oreochromis niloticus) skin

“…The Td of miiuy croaker swim bladders for ASC= 24.7 ºC and PSC =26.7 ºC) [44]. The Td of tiger puffer skin for ASC =28 ºC and PSC =25.5 ºC [45] respectively. But lower than the Td of Nile tilapia skin (35.2 ºC, ASC) [31].The Td of river puffer skin for ASC = 29.5 ºC, PSC= 27.5 ºC [45].Also, according to Li et al 2013 [46], the collagen of land animal had a higher denaturation temperature than that fish collagen due to its higher amino acid content.…”

“…The Td of tiger puffer skin for ASC =28 ºC and PSC =25.5 ºC [45] respectively. But lower than the Td of Nile tilapia skin (35.2 ºC, ASC) [31].The Td of river puffer skin for ASC = 29.5 ºC, PSC= 27.5 ºC [45].Also, according to Li et al 2013 [46], the collagen of land animal had a higher denaturation temperature than that fish collagen due to its higher amino acid content. Chen et al, 2019 [43] showed that the hydrogen bond in the collagen molecule was destroyed when the temperature rises therefore the triple helix structure dissociates then converts into random coil.…”