| 초록 |
This study reports the preparation of the Candida antarctica lipase B (CalB) enzyme immobilization on silica-coated magnetic nanoparticles (Si-MNPs@CalB) using a various cross-linkers, and demonstration of rapid esterolysis of p-nitrophenyl alkanoates. CalB enzymes were coupled with different cross-linkers silanes (-NH2, -CO2H, and -Cl) on the Si-MNPs surface. Among these cross-linkers, Cl-functionalized silane was better at immobilization of CalB than the others were. Esterolysis of p-nitrophenyl alkanoates was demonstrated against Native CalB and Si-MNPs@CalB as a function of the length of alkyl chain (C4, C8, C12, and C16). From the Michaelis-Menten equation and Lineweaver-Burk plots, various enzyme kinetic parameters (i.e., Km, Vmax, Kcat and Kcat/Km ) were calculated. Esterolysis was faster on the shorter alkyl chains of p-nitrophenyl alkyl esters for both Native CalB and Si-MNPs @ CalB in the order C4 ＞ C8＞ C12 ＞＞ C16. Furthermore, optimum catalytic activity of Native CalB and Si-MNPs@CalB were evaluated different in pH and the reusability of Si-MNPs@CalB were evaluated as a function of the number of reuses. |
