Cold-Active Lipase-Based Biocatalysts for Silymarin Valorization through Biocatalytic Acylation of Silybin

Extremophilic biocatalysts represent an enhanced solution in various industrial applications. Integrating enzymes with high catalytic potential at low temperatures into production schemes such as cold-pressed silymarin processing not only brings value to the recovery from biomass residues, but also improves its solubility properties for biocatalytic modification. Therefore, a cold-active lipase-mediated system has been developed silybin acylation methyl fatty acid esters based on extracellular protein fractions produced by psychrophilic bacterial strain Psychrobacter SC65A.3 isolated Scarisoara Ice Cave (Romania). The of lipase fraction was 1% olive-oil-enriched culture media. Through multiple immobilization approaches putative lipases (using carbodiimide, aldehyde-hydrazine, or glutaraldehyde coupling), bio-composites (S1–5) similar even higher activity under conditions (25 °C) have synthesized covalent attachment nano-/micro-sized magnetic polymeric resin beads. Characterization methods (e.g., FTIR DRIFT, SEM, enzyme activity) strengthen biocatalysts’ settlement and potential. Thus, immobilized exhibited between 80 128% loading range 90–99% this led yield up 89%. performance reached maximum 67% conversion decanoate acylating agent nano-support biocatalyst.