Preparation of enzyme nanoparticles and studying the catalytic activity of the immobilized nanoparticles on polyethylene films

Using high-intensity ultrasound, in situ generated α-amylase nanoparticles (NPs) were immobilized on polyethylene (PE) films. The α-amylase NP-coated PE films have been characterized by E-SEM, FTIR, DLS, XPS and RBS. The PE was reacted with HNO3 and NPs of the α-amylase were also deposited on the activated PE. The PE impregnated with α-amylase (4 μg per 1 mg PE) was used for hydrolyzing soluble potato starch to maltose. The immobilization improved the catalytic activity of α-amylase at all the reaction conditions studied. The kinetic parameters, Km (5 and 4 g L−1 for the regular and activated PE, respectively) and Vmax (5 × 10−7 mol ml−1 min−1, almost the same numbers were obtained for the regular and activated PEs) for the immobilized amylase were found to slightly favor the respective values obtained for the free enzyme (Km = 6.6 g L−1, Vmax = 3.7 × 10−7 mol ml−1 min−1). The enzyme remained bound to PE even after soaking the PE in a starch solution for 72 h and was still found to be weakly active.

► Amylase nanoparticles (NPs) are formed in an aqueous solution of amylase.
► Avoided the dissolution of the amylase NPs they were embedded in Polyethylene film.
► Immobilization of the NPs on the polyethylene (PE) film was done sonochemically.
► The PE containing the amylase NPs was inserted in an aqueous starch solution.
► The hydrolysis of starch solution by the amylase NPs was monitored.