Biochemical and Microstructural Properties of Lizardfish (Saurida tumbil) Scale Collagen Extracted with Various Organic Acids

The purpose of this research was to extract collagen from the scales of lizardfish (Saurida tumbil) using various acids. Acetic acid-extracted collagen (AScC) produced a higher yield (1.8 mg/g) than lactic acid-extracted collagen (LScC) and citric acid-extracted collagen (CScC) although not significantly different (p > 0.05). All extracted collagens were categorized as type I collagens with the presence of alpha chains (alpha(1) and alpha(2)) based on the SDS-PAGE profiles. The triple-helical structure of the collagen was maintained in the AScC, LScC, and CScC as confirmed by the FTIR spectra. The UV-vis and X-ray diffraction spectra observed in all collagens were in agreement with previous work on fish scale and calfskin (commercial) collagens. The thermal stability of AScC (T-max = 31.61 degrees C) was greater than LScC (T-max = 30.86 degrees C) and CScC (T-max = 30.88 degrees C). The microstructure of acid-extracted collagens was characterized as complex, fibrous, and multilayered, with irregular sheet-like structures. All samples were highly soluble in acidic pH (1.0-4.0) and in low concentrations of NaCl (0-20 g/L). In conclusion, the lizardfish scale collagen, particularly AScC, may be used as an alternative to terrestrial animal collagen.

Automated summary

The research extracted collagen from lizardfish scales using various acids and found that acetic acid-extracted collagen had a higher yield and thermal stability. All extracted collagens were categorized as type I collagens with a triple-helical structure.