Matinja_2026_Prep.Biochem.Biotechnol__1

The application of cold-adapted enzymes in biocatalysis offers significant industrial advantages, particularly for processes that require high efficiency at low temperatures. However, their practical use is often hindered by their poor thermal stability and limited reusability. In this study, psychrophilic lipase Glalip03 from Glaciozyma antarctica PII2 was immobilized on Seplite LX120, a cost-effective macroporous resin, via physical adsorption. Comprehensive biophysical analyses, including Scanning Electron Microscopy (SEM), Fourier-transform infrared spectroscopy (FT-IR), and Brunauer-Emmett-Teller (BET) surface area analysis, confirmed successful immobilization. The immobilized Glalip03 displayed significantly improved thermal stability, maintaining over 50% activity at 55 degreesC, and retained more than 50% of its initial catalytic activity after five consecutive cycles. The adsorption equilibrium data best fit the Jossens isotherm model, indicating a heterogeneous multilayer adsorption process. Furthermore, the enzyme showed enhanced tolerance to selected organic solvents and maintained robust storage stability at both 4 degreesC and ambient temperatures. These findings demonstrate that Seplite LX120 is an effective carrier for cold-active lipase immobilization, offering a simple and scalable strategy for enhancing enzyme stability, reusability, and solvent compatibility. The improved biocatalyst holds strong potential for industrial applications in detergents, food processing, flavor synthesis, and cosmetics.