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Updated: Nov 20, 2025

Enrichment of Extracellular Matrix Proteins from Tissues and Digestion into Peptides for Mass Spectrometry Analysis
Published on: July 23, 2015
Characterization of pepsin-soluble collagen extracted from gourami (Osphronemus goramy) scales
H L Tangguh1, C Prahasanti1, N Ulfah1
1Department of Periodontology, Faculty of Dental Medicine, Universitas Airlangga, Surabaya, Indonesia.
Background:
Periodontal regeneration is the anticipated result of periodontal tissue therapy. Of the many scaffold materials utilized, collagen has been shown to possess characteristics that strongly promote the periodontal regeneration process. Gourami (Osphronemusgoramy) scales can be utilized as an alternative source of collagen due to their abundant availability, the absence of risk of zoonosis, and lack of religious strictures against their use.
Aims:
To analyze the characteristics of collagen extracted from gourami scales.
Methods And Materials:
A combination of scanning electron microscopy (SEM), Fourier Transform Infrared Spectroscopy (FTIR), and in vitro enzymatic biodegradation analysis were employed to determine pore sizes, constituent functional groups, and the degradation rate of collagen extractedfrom gourami scales.
Results:
Collagen extracted from gourami scales demonstrated an average porosity of 13.779 μm. The FTIR test results indicated Amide A, Amide B, Amide I, Amide II, and Amide III peaks. The degradation rate of extracted collagen from gourami scales was 92.00 ± 0.8165% on the first day, 95.75 ± 1.70783% on the third day and 100% on the seventh day.
Conclusion:
The pore sizes ofcollagen extracted from gouramy scalesare suitable for use as scaffold. FTIR analysis indicated that this collagen possessed a triple helix structure. Collagen extracted from gourami scales was completely degraded within seven days when treated with 0.6 g/mL collagenase solution.
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