Physicochemical and Biocompatibility Properties of Type I Collagen from the Skin of Nile Tilapia (Oreochromis niloticus) for Biomedical Applications

Abstract

The aim of this study is to investigate the physicochemical properties, biosafety, and biocompatibility of the collagen extract from the skin of Nile tilapia, and evaluate its use as a potential material for biomedical applications. Two extraction methods were used to obtain acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from tilapia skin. Amino acid composition, FTIR, and SDS-PAGE results showed that ASC and PSC were type I collagen. The molecular form of ASC and PSC is (α1)2α2. The FTIR spectra of ASC and PSC were similar, and the characteristic peaks corresponding to amide A, amide B, amide I, amide II, and amide III were 3323 cm−1, 2931 cm−1, 1677 cm−1, 1546 cm−1, and 1242 cm−1, respectively. Denaturation temperatures (Td) were 36.1 °C and 34.4 °C, respectively. SEM images showed the loose and porous structure of collagen, indicting its physical foundation for use in applications of biomedical materials. Negative results were obtained in an endotoxin test. Proliferation rates of osteoblastic (MC3T3E1) cells and fibroblast (L929) cells from mouse and human umbilical vein endothelial cells (HUVEC) were increased in the collagen-treated group compared with the controls. Furthermore, the acute systemic toxicity test showed no acute systemic toxicity of the ASC and PSC collagen sponges. These findings indicated that the collagen from Nile tilapia skin is highly biocompatible in nature and could be used as a suitable biomedical material.

Comprehensive Assessment of Nile Tilapia Skin (Oreochromis niloticus) Collagen Hydrogels for Wound Dressings

“…But there are still many problems that limit the application of collagen hydrogels, especially low mechanical strength making it unsuitable as a block gel [36]. Hou et al [37,38] have proved that the tilapia collagen showed high biocompatibility and they prepared a composite material using tilapia collagen with konjac glucomannan, which significantly improved its mechanical properties. Although the addition of the second component can significantly improve the mechanical strength of the collagen material, it may decrease the function of collagen.…”

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)

“…However, previous reports have confirmed that collagens from different raw materials may have varying structures and characteristics, and exhibit very different fibril formation abilities, which have limited their wide-spread use. Fish collagen has a similar amino acid composition as conventional collagens with a decreased amount of imino acid and increased serine and threonine, and carries no disease risk [25]. To the best of our knowledge, there have been few reports comparing the characteristics of collagen from different puffer species.…”

Collagen Based Materials in Cosmetic Applications: A Review

“…Examination of collagen obtained from tilapia skin showed that as well as acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) have typical type I collagen features. The ASC denaturation temperature was 36.1 °C, but for PSC it was 34.4 °C [ 51 ]. Whereas isolated acid-soluble collagen from the skin of silver carp ( Hypophthalmichthys molitrix ) also comprised type I collagen as shown by SDS-PAGE patterns [ 52 , 53 ], with denaturation temperature established at around 29 °C for ASC.…”