Kelah Collagen: A Comparative Characterization With Barramundi and Tilapia Collagens

Kelah ( Tor tambroides ) is a high‐value and conservation‐sensitive species, and its collagen may offer unique advantages as an alternative source compared to more conventional fish such as tilapia or barramundi, which have been extensively studied. Collagen from freshwater fish is increasingly favored due to its benefits, including lower disease transmission risk, cost‐effective production, freedom from religious restrictions, high biocompatibility, low molecular weight, and excellent absorption by the human body. In this study, acid‐soluble collagen (ASC) was extracted from the skin of three freshwater species: kelah ( T. tambroides ), tilapia ( Oreochromis niloticus ), and barramundi ( Lates calcarifer ), by using ultrasonic‐assisted extraction. The collagen was characterized for total protein and hydroxyproline content using high‐performance liquid chromatography with a diode array detector (HPLC‐DAD). Molecular composition was assessed using sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE), and functional groups were identified through Fourier Transform Infrared‐Attenuated Total Reflectance (FTIR‐ATR) spectroscopy. Among the species, tilapia collagen had the highest total protein content (60.66% w/w), followed by barramundi (47.08% w/w) and kelah (22.44% w/w). Conversely, hydroxyproline content was the highest in barramundi (1372.96 mg/kg), followed by kelah (999.06 mg/kg) and tilapia (485.71 mg/kg). FTIR spectra showed characteristic collagen bands, including Amide A (∼3300 cm −1 ), Amide B (∼3100 cm −1 ), Amide I (∼1655 cm −1 ), Amide II (∼1560 cm −1 ), and Amide III (∼1245 cm −1 ). SDS‐PAGE confirmed all samples as type I collagen with molecular weights of ∼95–130 kDa. These results suggest that kelah collagen is a promising alternative source, comparable to barramundi and tilapia.