Siti Dharmawati, Aam Gunawan, Antoni Pardede, Osfar Sjofjan
Freshwater snails (Pomacea paludosa) are aquatic biota abundantly available as a source of collagen. Collagen isolation can be done chemically and enzymatically with bromelain. This study aims to study the isolation of collagen enzymatically using bromelain enzymes and hydroextraction acid using acetic acid and to determine the physicochemical characteristics of freshwater snail flesh collagen. Collagen isolation is carried out in two stages: pretreatment and hydrolysis enzymatically and chemically using an acid solution. The stages include pretreatment (a) chemically using 0.1 M and 0.15 M NaOH at ratios of 1:8 and 1:10 and biologically using 10% rice husk charcoal with a soaking time of 24 hours. (b) Freshwater snail flesh collagen is extracted with 0.1 and 0.3 M acetic acid for 2 and 3 hours and hydrolysed with distilled water for 12 hours. (c) Enzymatic extraction with 3% and 4% bromelain for 3 and 4 hours. The best non-collagen protein results in chemical pretreatment came from using 0.1 M NaOH (1:8) at 105.88 ppm and 10% rice husk charcoal at 110.48 ppm. The research found that using 3-4% bromelain enzyme for extraction gave better collagen yield, protein content, and viscosity results than the acid hydro-extraction method. The FTIR test results indicate that swamp snail meat has collagen with a strong hydrogen triple helix structure in its bonds, which include amides A, B, I, II, and III. In the hydroextraction acid, the detected functional groups were amides A, B, and III. © 2025 Dharmawati et al.
Department of Animal Science, Faculty of Agricultural, University of Islam Kalimantan, South Kalimantan, Banjarmasin, 70712, Indonesia; Departement of Chemistry Education, University of Islam Kalimantan, South Kalimantan, Banjarmasin, 70712, Indonesia; Departement of Animal Nutrition and Feed Science, Faculty of Animal Science, University of Brawijaya, East Java, Malang, 65145, Indonesia
