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<p>Fish skin-derived gelatin, hydrolysates, and peptide fractions have garnered attention for their potential applications in food, pharmaceuticals, packaging, and cosmetics. This study compares these three <i>Katsuwonus pelamis</i> skin-derived products, analyzing their structural and thermal properties using UV–Vis, FTIR, SEM, XRD, and thermal studies. UV–Vis spectra showed polypeptide chain cleavage in GH and 3PF, with bioactive chromophores above 320&#xa0;nm. FTIR revealed shifts in amide bands, indicating structural modifications due to hydrolysis and ultrafiltration. SEM images showed a transition from a fibrillar network in gelatin to fragmented structures in GH and 3PF, reflecting reduced stability. XRD indicated a loss of crystallinity, with hydrolysates and peptides being more amorphous. Thermal analyses showed higher degradation rates in GH and 3PF compared to gelatin. These structural transformations impact the physicochemical properties of gelatin and its derivatives. This study highlights the importance of understanding these properties for tailored applications in food fortification, nutraceuticals, wound healing, and biomaterials. The findings suggest promising prospects for the optimized use of fish skin-derived products across diverse industries.</p>

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A comparative analysis of gelatin, hydrolysates, and peptide fractions from Katsuwonus pelamis skin: Insights into characterization

  • 期刊论文

  • 发表日期：

    2025年4月28日

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  • Jean Mary Joy,
  • Amruth Padmaprakashan,
  • Rosemol Jacob Mannuthy,
  • Suseela Mathew

摘要

Fish skin-derived gelatin, hydrolysates, and peptide fractions have garnered attention for their potential applications in food, pharmaceuticals, packaging, and cosmetics. This study compares these three Katsuwonus pelamis skin-derived products, analyzing their structural and thermal properties using UV–Vis, FTIR, SEM, XRD, and thermal studies. UV–Vis spectra showed polypeptide chain cleavage in GH and 3PF, with bioactive chromophores above 320 nm. FTIR revealed shifts in amide bands, indicating structural modifications due to hydrolysis and ultrafiltration. SEM images showed a transition from a fibrillar network in gelatin to fragmented structures in GH and 3PF, reflecting reduced stability. XRD indicated a loss of crystallinity, with hydrolysates and peptides being more amorphous. Thermal analyses showed higher degradation rates in GH and 3PF compared to gelatin. These structural transformations impact the physicochemical properties of gelatin and its derivatives. This study highlights the importance of understanding these properties for tailored applications in food fortification, nutraceuticals, wound healing, and biomaterials. The findings suggest promising prospects for the optimized use of fish skin-derived products across diverse industries.