Jet cutter technique as a tool to achieve high lipase hydrolytic activity

Lipase immobilization has been widely studied because it allows for enzyme reuse and provides more assertive control over the catalytic process. This study aimed to evaluate the effect of bead size on the performance of entrapped lipase. Eversa® Transform 2.0 was immobilized on calcium alginate beads by jet cutting and dripping. Beads produced by jet cutting were small (D[3,4] = 803.36 ± 16.9 µm) and had a relatively narrow size distribution (span of 0.79). Beads obtained by extrusion dripping measured 2459.98 ± 15.6 µm and had a span of 0.45. Infrared spectroscopy and microscopic analysis confirmed the presence of lipase in both types of beads. Lipase showed high hydrolytic activity in its free form (15,000 U g−1). Immobilization in calcium alginate was effective but decreased recovered enzyme activity. The porosity of loaded beads varied with size. The high surface area (5.46 vs 3.13 m2 g−1) and porosity (76.33% vs 21.65%) of beads produced by jet cutting, as compared with those produced by dripping, favored enzyme activity (3000 vs 1500 U g−1 protein). The results indicate that facilitated mass transfer is an important factor in the development of immobilized enzymes.