Dopamine-modified hydrated silica immobilized Flavourzyme for efficient bioactive peptide release from β-lactoglobulin

This study addresses the challenges of low stability, high production costs, and inefficient peptide recovery in conventional liquid enzymatic hydrolysis of β-lactoglobulin (β-Lg) by developing a novel dopamine-modified hydrated silica-immobilized Flavourzyme (DHS-F). Our objectives were to enhance enzyme stability and reusability while improving the release of bioactive peptides. Structural characterization via FTIR and TGA confirmed the covalent binding of Flavourzyme to the carrier and revealed enhanced thermal stability. DHS-F demonstrated superior catalytic performance with 69.7 % activity at 70 °C (compared to 20.3 % for free enzyme) and broad pH adaptability (pH 6–10). It maintained over 50 % activity after 20 cycles. Hydrolysis of β-Lg by DHS-F achieved 72.6 % degree of hydrolysis, yielding over 80 % of peptides below 1 kDa. Peptidomics analysis identified 49 unique peptides with ACE inhibitory activity. This innovative method addresses the economic limitations of liquid enzymes and offers a promising avenue for efficiently producing bioactive peptides from food proteins.