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<p>Collagen was extracted from Nile tilapia (<i>Oreochromis niloticus</i>) by-products using enzyme-assisted extraction followed by ultrafiltration (UF) and compared to conventional pepsin-solubilized collagen (PSC). The yield of papain-soluble collagen (PaSC) was 8.19 ± 0.32%, lower than PSC (9.00 ± 0.39%). FT-IR spectra suggests the characteristic of collagen-like secondary structural features with the presence of amide A, B, I, II and III bands. UV-visible spectroscopy showed absorption peaks at 220&#xa0;nm (PaSC) and 230&#xa0;nm (PSC). Additionally, both collagens exhibited acidic pH values and a bright white appearance. Scanning electron microscopy (SEM) analysis revealed a flaky, closely packed and randomly coiled microstructure. SDS-PAGE showed α-chain band in the typical molecular-weight range of type I collagen-like material with a distinct α-chains (~ 100–150&#xa0;kDa) and β-dimers (~ 250&#xa0;kDa) and lower-molecular-weight features, indicating some enzymatic fragmentation. PaSC and PSC showed similarly high WHC (43.40 ± 0.20 and 44.30 ± 0.01&#xa0;g/g, respectively) and OHC (35.70 ± 0.30 and 37.35 ± 0.08&#xa0;g/g, respectively), indicating strong water and oil retention capacities. PaSC showed a higher FC (22.22 ± 1.92% vs. 10.00 ± 0.10%), FS (69.84 ± 2.75% vs. 66.67 ± 0.00%), and EAI (71.24 ± 0.01 vs. 6.76 ± 1.17&#xa0;m²/g), while both samples showed similarly low emulsion stability, with ESI values of 12.34 ± 1.46 and 12.22 ± 0.12&#xa0;min for PaSC and PSC, respectively. These results demonstrate that papain-assisted extraction combined with UF, offers a viable alternative enzyme-assisted process for collagen production.</p>

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Structural, physicochemical and functional properties of type I collagen from Nile tilapia by-products via enzymatic extraction and ultrafiltration isolation

  • 期刊论文

  • 发表日期：

    2026年8月5日

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  • Ivy Bazar Divina,
  • Arman Idlan Haidis,
  • Jumardi Roslan,
  • Suryani Saallah,
  • Wolyna Pindi,
  • Nor Qhairul Izzreen Mohd Noor,
  • Yanty Noorzianna Abdul Manaf,
  • Ahmad Riduan Bahauddin,
  • Amiza Mat Amin,
  • Abdul Aziz Jaziri,
  • Rahmi Nurdiani

摘要

Collagen was extracted from Nile tilapia (Oreochromis niloticus) by-products using enzyme-assisted extraction followed by ultrafiltration (UF) and compared to conventional pepsin-solubilized collagen (PSC). The yield of papain-soluble collagen (PaSC) was 8.19 ± 0.32%, lower than PSC (9.00 ± 0.39%). FT-IR spectra suggests the characteristic of collagen-like secondary structural features with the presence of amide A, B, I, II and III bands. UV-visible spectroscopy showed absorption peaks at 220 nm (PaSC) and 230 nm (PSC). Additionally, both collagens exhibited acidic pH values and a bright white appearance. Scanning electron microscopy (SEM) analysis revealed a flaky, closely packed and randomly coiled microstructure. SDS-PAGE showed α-chain band in the typical molecular-weight range of type I collagen-like material with a distinct α-chains (~ 100–150 kDa) and β-dimers (~ 250 kDa) and lower-molecular-weight features, indicating some enzymatic fragmentation. PaSC and PSC showed similarly high WHC (43.40 ± 0.20 and 44.30 ± 0.01 g/g, respectively) and OHC (35.70 ± 0.30 and 37.35 ± 0.08 g/g, respectively), indicating strong water and oil retention capacities. PaSC showed a higher FC (22.22 ± 1.92% vs. 10.00 ± 0.10%), FS (69.84 ± 2.75% vs. 66.67 ± 0.00%), and EAI (71.24 ± 0.01 vs. 6.76 ± 1.17 m²/g), while both samples showed similarly low emulsion stability, with ESI values of 12.34 ± 1.46 and 12.22 ± 0.12 min for PaSC and PSC, respectively. These results demonstrate that papain-assisted extraction combined with UF, offers a viable alternative enzyme-assisted process for collagen production.