Collagen isolation with acid soluble method from the skin of Red Snapper (lutjanus sp.)

Abstract

Collagen is an extracellular matrix connective tissue that account for about 30% of the total protein. Red snapper skin has the potential as an alternative source of collagen that can increase the added value of food and fishery industrial waste. This research aimed to isolate collagen by acid-soluble method and collagen characterization. Isolation of red snapper skin collagen consists of two stages, which are pretreatment with 0.1 M NaOH over 12 hours and hydrolysis with 0.5 M acetic acid over 48 hours. The pretreatment process resulted a non-collagen protein content at 0.2576% mg/mL. Hydrolisis with acetic acid yielded 9.71% (wet) and 41.19% (dry). Chemical analysis by amino acid analysis showed the dominant amino acid glycine, proline, arginine and alanine. Physical characterization of collagen was done by FTIR analysis and showed the presence of amide group A, B, I, II and III which belong to typical group of collagen.