Immobilization of enzymes for synergy in polymers to produce lactose free milk

Stabilization of the enzyme lactase is of interest in obtaining lactose-free foods. Optimization of the lactase enzyme activity was investigated using various immobilization methods, including encapsulation, and electrospinning. The physical properties of the immobilized lactase, such as thermal stability, mechanical strength, and resistance to denaturation have been enhanced and evaluated. The activity of the immobilized lactase was compared to that of the free enzyme. Additionally, lactase was examined in combination with glucose oxidase and catalase to reduce feedback inhibition of glucose and the toxicity of H₂O₂. The core-shell electrospinning technique was employed, wherein lactase was encapsulated within an aqueous core and shielded by a non-biodegradable shell. Electrospinning enhanced the enzyme's stability, reduced diffusion limitations, and improved reusability. The enzyme activity remained stable for four weeks and retained its activity after three months of storage at 4 °C in phosphate-buffered saline (PBS). This approach represents a preliminary investigation into the potential benefits of enzyme synergy.