Collagen production from Tilapia skin (Oreochromis niloticus) using acid extraction and Deep Eutectic Solvents
Tilapia skin, collagen, extraction and purification, Deep Eutectic Solvents.
Brazil is one of the main powers when it comes to the fishing industry, generating a high level of waste. It is noteworthy that the average fillet yield is approximately 30%, and the 70% of waste includes: head, carcass, viscera, skin and scales. Several products can be obtained from waste from fish filleting, such as, for example, gelatin extraction and food supplements based on protein and collagen. Collagen is the most abundant structural protein in the extracellular matrix of various tissues. Collagen extraction can be carried out using acids, such as acetic acid, or with Deep Eutectic Solvents. Deep eutectic solvents or Deep Eutethic Solvents (DESs) are obtained by mixing two or more compounds that act as hydrogen bond donors (HBD) or hydrogen bond acceptors (HBA). acceptor). In the protein recovery and purification process (Downstream processing), differences in properties are explored, such as solubility, as there are hydrophobic and hydrophilic amino acid residues along the peptide chain. On the other hand, the ease of preparation and elimination of recovery and purification steps can significantly reduce production costs and the impact on the environment. Thus, the use of DESs in protein recovery and purification protocols is advantageous, since these are promising green solvents, within the context of green chemistry. In this context, in the present study collagen will be extracted from the skin of Tilapia fish (Oreochromis nilloticus) through acid extraction, using acetic acid, and through a green solvent using different DESs. The DESs produced will be based on choline chloride as HBA and, as HBD, oxalic acid and acetic acid will be used in different molar proportions. Thus, the influence of acids and different DESs on the mass yield of the collagen recovery and purification process will be investigated. The resulting samples will be analyzed using Fourier Transform Infrared Spectroscopy (FTIR), Differential Scanning Calorimetry (DSC) to determine the collagen denaturation temperature and morphological analyzes using Scanning Electron Microscopy (SEM), in addition to evaluating the molar mass by electrophoresis (SDS-PAGE).