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 HNO(3) and NPs of the α-amylase were also deposited on the activated PE. The PE impregnated with α-amylase (4 μg per 1mg 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, K(m) (5 and 4 g L(-1) for the regular and activated PE, respectively) and V(max) (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 (K(m) = 6.6 g L(-1), V(max) = 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.
Department of Chemistry and Kanbar Laboratory for Nanomaterials, Center for Advanced Materials and Nanotechnology, Bar-Ilan University, Ramat-Gan 52900, Israel.
David
D
Meridor
Aharon
A
Gedanken
D055162:Biocatalysis / Q000187:drug effects; D004800:Enzymes, Immobilized / Q000737:chemistry* / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D053758:Nanoparticles / Q000737:chemistry*; D017942:Nitric Acid / Q000494:pharmacology; D020959:Polyethylene / Q000737:chemistry*; D013213:Starch / Q000378:metabolism; D014465:Ultrasonics; D000516:alpha-Amylases / Q000737:chemistry* / Q000378:metabolism*
D004800:Enzymes, Immobilized; D017942:Nitric Acid; D020959:Polyethylene; D013213:Starch; D000516:alpha-Amylases