The Characterization of Fish (Tilapia) Collagen Sponge as a Biomaterial

Abstract

For scaffold manufacturing, the utility of bioactive natural organic materials derived from marine products is useful and indispensable as an alternative to bovine collagen. The weakest feature of fish collagen for scaffold application is its low degeneration temperature (Td), indicating poor stability of fish collagen in mammalsin vivo. We have focused on the tropical fish tilapia as a candidate for generating a clinical scaffold. The aim of this study was to confirm theTdof tilapia type I atelocollagen (TAC) for biomedical application. Furthermore, the physical and structural properties were investigated and evaluated as a scaffold on a sponge form. Different concentrations {0.5%, 1.0%, and 2.0% (v/v)} of TAC solution were analyzed. Differential scanning calorimetry showed that theTdof TAC was 35-36°C. The scanning electron microscopy results indicated that the pore size (90–160 μm) of TAC sponges is acceptable for cell proliferation. The tensile strength of porous sponges was in the range of 0.01–0.07 MPa. These findings indicate that the TAC sponge prepared from tilapia is one of candidates as a scaffold. The 1.0% (v/v) concentration of TAC solution is especially recommended to be advantageous for preparing and handling the solution and for sponge formation.

Fish Collagen Promotes the Expression of Genes Related to Osteoblastic Activity

“…From our previous data [4,5] and the present results, TAC may represent not only a promising alternative to mammalian and avian collagen products but also a novel biomaterial with cell differentiation ability. The final goal with TAC is its clinical application as a scaffold in regenerative medicine.…”

“…The weakest point of fish collagen is its relatively low denaturation temperature ( ), which indicates a poor stability in clinical applications. However, our recent experiment using calorimetry revealed that of collagen solution derived from the tropical fish, tilapia (tilapia type I atelocollagen [TAC]), was 35-36 ∘ C [4], indicating that the abovementioned weak point has been completely overcome. In addition, the biological safety of TAC has been confirmed using various test methods recommended with ISO standards [5].…”

Rapid treatment of full‐thickness skin loss using ovine tendon collagen typeIscaffold with skin cells

“…Besides, the lack of biomaterials with the desired physicochemical (biodegradability, swelling ratio, etc. ), mechanical (tensile strength and Young's modulus), structural (porosity), biological (biocompatibility), and immunogenic properties limit the production of highly efficient TESS (Busra, Chowdhury, Saim, & Idrus, ; Yamamoto et al, ). Moreover, due to the tailor‐made approach and regulatory requirement to culture the cells in a state of art facility, the production cost is extremely high and typically unaffordable for general patients.…”

Extractability and physicochemical properties of cobia ( Rachycentron canadum ) skin collagen as influenced by lactic acid concentration

“…The study on thermal properties of extracted cobia skin ASC showed no detection on T d of cobia skin ASC extracted from 0.5 M lactic acid when analyzed using differential scanning calorimetry (DSC) while cobia skin ASC extracted by 1.0 M lactic acid showed a T d at 37.35°C. The high T d value of cobia skin ASC extracted by 1.0 M lactic acid was correlated with high content of hydroxylation of proline in collagen among warm water fish (Yamamoto et al., 2015), whereas cold water fish has lower hydroxyproline content that acted with the interchain hydrogen bonding to stabilize the triple helical structure of collagen but it has a higher content of hydroxy amino acids, serine, and threonine (Muyonga et al., 2004). However, comparing to the T d of cobia skin ASC extracted by 1.0 M lactic acid with study by Yamamoto et al.…”