Characterization of Collagen from Skipjack Tuna (Katsuwonus pelamis) Bone Using Sodium Hydroxide-Assisted Hydrolysis
DOI:
https://doi.org/10.34310/jbsh.v2.i2.231Keywords:
Fish Bone Collagen; Skipjack Tuna (Katsuwonus pelamis); FTIR Spectroscopy; Lowry Method; Extraction YieldAbstract
Background. Collagen is the main structural protein in vertebrate connective tissue, comprising 25–30% of total animal protein. Skipjack tuna (Katsuwonus pelamis) bone is a promising alternative collagen source, available in large quantities as a fishery by-product in Indonesia. Objective. This study determined the extraction yield and characterized the collagen extract obtained from skipjack tuna bone via maceration with 5% sodium hydroxide (NaOH). Methods. Bone was macerated in 5% NaOH for three days, neutralized with 10% HCl to pH 7, and concentrated using a rotary evaporator. Characterization included yield, organoleptic properties, moisture, ash content, functional groups by FTIR, and protein content by the Lowry method with a BSA calibration curve. Results. Extraction yield was 29.85%, considerably higher than acid-based extraction of related tuna species (1.42–21.05%), indicating co-extraction of non-collagenous compounds by NaOH. Moisture (4.03%) and ash (0.18%) met the SNI 8076:2014 threshold. FTIR showed absorption peaks at 3450.65 cm⁻¹ (amide A), 2926.01 cm⁻¹ (amide B), and 1637.56 cm⁻¹ (amide I); the peak at 1408.04 cm⁻¹ fell outside the standard amide II range (1517–1560 cm⁻¹) and is more appropriately identified as a carboxylate vibration. The Lowry calibration curve yielded a protein concentration of 228.8 ppm and a protein content of 91.4%, meeting the SNI minimum standard (>75%). Conclusion. Skipjack tuna bone is a promising collagen source with proximate characteristics meeting national standards, though confirming collagen identity requires further analysis, including hydroxyproline content and SDS-PAGE profiling.
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Copyright (c) 2025 Nur Aini Abdul Rahman, Wahdaniar, Nur Insani Amir (Author)
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