1Department of Marine Science, Faculty of Fisheries and Marine Sciences, Universitas Diponegoro, Indonesia
2Research Center for Oceanography, National Research and Innovation Agency, Indonesia
BibTex Citation Data :
@article{JKT29932, author = {Wilis Ari Setyati and Sri Sedjati and Rini Pramesti and Rinta Widya Pangestu and Dafit Ariyanto}, title = {Characterization of Collagen from Bone and Scales from White Sea Bass (Lates calcarifer)}, journal = {Jurnal Kelautan Tropis}, volume = {29}, number = {3}, year = {2026}, keywords = {acid extraction; collagen; FTIR; Lates calcarifer; sustainable biomaterial}, abstract = { Fishery by-products have become an increasingly valuable source of fish collagen as a substitute for mammalian collagen. This research aimed to analyze and compare bone and scale collagen isolated from white sea bass (Lates calcarifer) by acetic acid extraction. Bone and scale samples were deproteinized with sodium hydroxide, demineralized with EDTA, and extracted with 0.5 M acetic acid. The extraction solution was salted out with sodium chloride to precipitate collagen. The yield and various properties of the isolated collagen, including ninhydrin and Hopkins–Cole reactions, pH, moisture, UV–Vis absorption, and Fourier transform infrared (FTIR) spectra, were determined and compared with those of commercial collagen as a reference. The yields of collagen from both the scales and the bones were 0.15% and 0.18%, respectively. Both extracts tested positive for the ninhydrin reaction and negative for the Hopkins–Cole reaction. The pH values of both were 6.90 and 6.75, and the moisture content was 1.43% and 2.00% for bone and scale collagen, respectively. The UV–Vis spectra exhibited typical absorption in the region of 200–250 nm, and the characteristic Amide A, B, I, II, and III bands were recognized by FTIR analysis. These spectral features are indicative of peptides related to collagen in both extracts. Although the recovery was relatively low, the result showed that bones and scales of L. calcarifer could be used as an alternative source of marine collagen. Further modification of pretreatment and extraction parameters may be necessary for enhancing collagen extraction. }, issn = {2528-3111}, pages = {317--326} doi = {10.14710/jkt.v29i3.29932}, url = {https://ejournal2.undip.ac.id/index.php/jkt/article/view/29932} }
Refworks Citation Data :
Fishery by-products have become an increasingly valuable source of fish collagen as a substitute for mammalian collagen. This research aimed to analyze and compare bone and scale collagen isolated from white sea bass (Lates calcarifer) by acetic acid extraction. Bone and scale samples were deproteinized with sodium hydroxide, demineralized with EDTA, and extracted with 0.5 M acetic acid. The extraction solution was salted out with sodium chloride to precipitate collagen. The yield and various properties of the isolated collagen, including ninhydrin and Hopkins–Cole reactions, pH, moisture, UV–Vis absorption, and Fourier transform infrared (FTIR) spectra, were determined and compared with those of commercial collagen as a reference. The yields of collagen from both the scales and the bones were 0.15% and 0.18%, respectively. Both extracts tested positive for the ninhydrin reaction and negative for the Hopkins–Cole reaction. The pH values of both were 6.90 and 6.75, and the moisture content was 1.43% and 2.00% for bone and scale collagen, respectively. The UV–Vis spectra exhibited typical absorption in the region of 200–250 nm, and the characteristic Amide A, B, I, II, and III bands were recognized by FTIR analysis. These spectral features are indicative of peptides related to collagen in both extracts. Although the recovery was relatively low, the result showed that bones and scales of L. calcarifer could be used as an alternative source of marine collagen. Further modification of pretreatment and extraction parameters may be necessary for enhancing collagen extraction.
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