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<p>In this study, <i>Leiocassis longirostris</i> by-products were subjected to papain-assisted hydrolysis, with 4&#xa0;h identified as the optimal hydrolysis duration. The resulting hydrolysate was subsequently fractionated via ultrafiltration into three size ranges: &gt; 100&#xa0;kDa, 10–100&#xa0;kDa, and &lt; 10&#xa0;kDa. Each fraction was characterised for soluble protein content, peptide content, physicochemical properties, and functional characteristics. The &lt; 10&#xa0;kDa fraction had the highest soluble protein (59.77 ± 1.60%) and peptide content (48.67 ± 2.15%), along with superior solubility (30.23–82.64%) and emulsifying activity (18.31–82.12%) across the tested pH range. In contrast, the &gt; 100&#xa0;kDa fraction exhibited lower soluble protein (31.29 ± 2.52%) and peptide contents (19.13 ± 1.47%), but greater foaming capacity (19.10–91.52%), foaming stability (13.72–34.11%) and emulsifying stability (20.14–80.34%). All functional properties were markedly influenced by pH, with significant reductions observed at pH 4 (<i>p</i> &lt; 0.05), likely due to protein aggregation near the proteins’ isoelectric point. These findings demonstrate that papain hydrolysis combined with ultrafiltration enables the targeted production of peptide fractions with distinct functional properties, facilitating efficient valorisation of nutrient-rich aquatic by-products for food, pharmaceutical, and nutraceutical applications.</p>

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Characterisation of functional properties of papain-hydrolysed Leiocassis longirostris by-product fractions obtained via membrane ultrafiltration

  • 期刊论文

  • 发表日期：

    2026年7月31日

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  • Mingming Kan,
  • Zhi Yin Ter,
  • Yifei Sun

摘要

In this study, Leiocassis longirostris by-products were subjected to papain-assisted hydrolysis, with 4 h identified as the optimal hydrolysis duration. The resulting hydrolysate was subsequently fractionated via ultrafiltration into three size ranges: > 100 kDa, 10–100 kDa, and < 10 kDa. Each fraction was characterised for soluble protein content, peptide content, physicochemical properties, and functional characteristics. The < 10 kDa fraction had the highest soluble protein (59.77 ± 1.60%) and peptide content (48.67 ± 2.15%), along with superior solubility (30.23–82.64%) and emulsifying activity (18.31–82.12%) across the tested pH range. In contrast, the > 100 kDa fraction exhibited lower soluble protein (31.29 ± 2.52%) and peptide contents (19.13 ± 1.47%), but greater foaming capacity (19.10–91.52%), foaming stability (13.72–34.11%) and emulsifying stability (20.14–80.34%). All functional properties were markedly influenced by pH, with significant reductions observed at pH 4 (p < 0.05), likely due to protein aggregation near the proteins’ isoelectric point. These findings demonstrate that papain hydrolysis combined with ultrafiltration enables the targeted production of peptide fractions with distinct functional properties, facilitating efficient valorisation of nutrient-rich aquatic by-products for food, pharmaceutical, and nutraceutical applications.