enhanced activity and stability of lipase via immobilization in pectin-based hydrogels

Pectin-based hydrogels are hydrophilic polymeric networks created from the cross-linking of the plant-based polysaccharide pectin. in this study, the hydrogels were synthesized using chemical modification with glycidyl methacrylate and used for the immobilization of aspergillus niger lipase (anl). the immobilization efficiency and relative activity recovery achieved about 82% and 88.3%, respectively. scanning electron microscopy revealed the porous three-dimensional structure of the pristine hydrogels, and the surface became rougher and the pore structure changed during the immobilization of the lipase enzymes, indicating the successful immobilization of the enzymes within the hydrogels. fourier transform infrared spectroscopy confirmed the presence of the enzyme within the hydrogels, with the presence of the carbonyl and amide groups at 1650 and 1540 cm⁻¹, respectively. while, the functional groups of the pectin-based hydrogels remaining intact during the immobilization process. at 60°c, the immobilized lipase showed 15% of its original temperature stability compared to 5% for the free lipase. at ph 5, the immobilized enzyme was found to have 70% of its maximum ph activity, while the free enzyme was found to have 52% of its maximum ph activity. these results indicate pectin hydrogels are effective supports for lipase immobilization, improving enzyme stability for biocatalytic applications.