Valorization of emperor fish (Lethrinus lentjan) skin for collagen isolation: effect of acetic acid ratio and extraction time

• Published in: IOP conference series. Earth and environmental science Vol. 1137; no. 1; pp. 12047 - 12060
• Main Authors: Firdayanti, W, Trilaksani, W, Purwaningsih, S
• Format: Journal Article
• Language: English
• Published: Bristol IOP Publishing 01.01.2023
• Subjects: Acetic acid; acid soluble collagen; Alanine; Amino acids; Collagen; emperor fish; Extracellular matrix; extraction; Fish; Fish skins; Glycine; Lethrinus lentjan; Lipids; Molecular chains; Proteins; Skin; Sodium hydroxide; valorization
• ISSN: 1755-1307; 1755-1315
• DOI: 10.1088/1755-1315/1137/1/012047

Abstract About 30% of all the proteins in an animal’s body are found in the extracellular matrix, the major consisting of collagen. Industries that process emperor fish ( Lethrinus lentjan ) produce fish skin that can be utilized to produce collagen sustainably. The objective of this research is to determine the effect of various ratios acetic acid to fish skin and extraction times on the characteristics of collagen. Collagen from the skin of emperor fish was extracted and treated first. For the pretreatment, the skin was immersed in 0.1 M NaOH tenfold (w/v) and replaced after 2 hours for 24 hours at 4 °C. The soaking solution’s proteins, amino acids, and lipid content were all examined. A pre-treated sample was extracted in 0.5 M acetic acid for 24, 36, and 48 hours at 4°C in ratios of 1:10, 1:20, and 1:30. (w:v). The optimum treatment involved extracting for 48 hours at 1:30 (w/v) in acetic acid. The extracted collagen has a yield of 7.70±35% and a whiteness value of 66.76±0.2. The primary amino acids were glycine, proline, and alanine, according to the peptide patterns of the collagen from the skin of emperor fish, which showed α1 and α2 chains with molecular weights of 150-177 kDa. Additionally, this collagen was type 1, and its FTIR spectra and protein pattern were comparable.