Fish gelatin (FG)-based wound dressings exhibit superior water absorption capacity, thermal stability, and gelation properties, which enhance the performance of these dressings. In this study, our objective was to investigate the conditions underlying the enzymatic hydrolysis of FG and subsequent cross-linking to prepare high-performance gels. A two-step enzymatic method of protease-catalyzed hydrolysis followed by glutamine transglutaminase (TGase)-catalyzed cross-linking was used to prepare novel high-performance fish gelatin derivatives with more stable dispersion characteristics than those of natural gelatin derivatives. Compared with conventional TGase cross-linked derivatives, the novel derivatives were characterized by an average pore size of 150 μm and increased water solubility (423.06% to 915.55%), water retention (by 3.6-fold to 43.89%), thermal stability (from 313 °C to 323 °C), and water vapor transmission rate, which reached 486.72 g·m⁻²·24 h⁻¹. In addition, loading glucose oxidase onto the fish gelatin derivatives increased their antibacterial efficacy to >99% against Escherichia coli and Staphylococcus aureus.

Aglycone-type soy isoflavones, recognized for their bioactive phytoestrogen properties, face industrial limitations due to their low natural abundance and inefficient conversion. This study optimized a multi-enzyme synergistic catalysis system using soybean sprout powder, achieving high conversion rates and purity through response surface methodology. The optimal enzyme system comprised β-glucosidase (25 U/mL), cellulase (200 U/mL), hemicellulase (400 U/mL), and β-galactosidase (900 U/mL) at pH 5.0, 50 °C, and 3.2 h. This system yielded an aglycone conversion rate of 92% and glycoside hydrolysis rate of 97%, outperforming single-enzyme approaches. Upon post-purification with AB-8 macroporous resin, the product reached a purity of 58.1 ± 0.54% and exhibited strong antioxidant activity, with DPPH and ABTS radical scavenging rates of 81.01 ± 0.78% and 71.37 ± 1.01%, respectively. In a zebrafish central nervous system injury model induced by mycophenolate mofetil, the 500 μg/mL sample group significantly reduced neural apoptosis fluorescence intensity compared to controls (p < 0.05), achieving a neuroprotective rate of 76.58%, which was similar to the effect of L-reducing glutathione. This study offers an efficient, cost-effective enzymatic strategy for producing aglycone soy isoflavones, highlighting their potential in functional foods and neuroprotective applications.