Extraction and characterization of collagen from the skin of Amazonian freshwater fish pirarucu

Abstract

The need to fully exploit fishing resources due to increasing production and consequent waste generation requires research to promote the sustainability of the fishing industry. Fish waste from the industry is responsible for relevant environmental contamination. However, these raw materials contain high amounts of collagen and other biomolecules, being attractive due to their industrial and biotechnological applicability. Thus, to reduce the waste from pirarucu ( Arapaima gigas ) processing, this study aimed to obtain collagen from pirarucu skin tissue. The extraction process used 0.05 M sodium hydroxide, 10% butyl alcohol, and 0.5 M acetic acid, with extraction temperature of 20°C. The obtained yield was 27.8%, and through sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), it was determined that the collagen obtained was type I. This study showed that collagen solubility was highest at pH 3 and the lowest solubility was at concentrations of 3% sodium chloride. The denaturation temperature of collagen was 38.1°C, and its intact molecular structure was observed using the Fourier transform infrared spectrophotometry technique with an absorption radius of 1. The results showed that it was possible to obtain collagen from pirarucu skin at 20°C, which has the typical characteristics of commercial type I collagen. In conclusion, the procedures used may be considered to be an interesting alternative for collagen extraction, a new product obtained from the processing of fish waste.

Stem-Cell-Regenerative and Protective Effects of Squid (Symplectoteuthis oualaniensis) Skin Collagen Peptides against H2O2-Induced Fibroblast Injury

“…The amide A band of SCP (3411 cm −1 ) was a ributed The secondary structures of collagen (PSC and ASC) and peptide (SCP) were further evaluated using infrared spectroscopy, as depicted in Figure 4B. The characteristic peaks corresponding to amides A, B, I, II, and III exhibited similarities with PSC and ASC, consistent with previously reported collagens derived from diverse marine sources [40][41][42][43]. The positions of the amide bands and the arrangement of the dependent groups are presented in Table 2.…”