| 초록 |
This study reports the catalytic hydrolysis of p-nitrophenyl alkyl esters (alkanoates) with the Candida antarctica lipase B (CalB) immobilized silica-coated magnetic nanoparticles (Si-MNPs). CalB enzymes were immobilized with different functional groups on Si-MNPs such as -NH2, -Cl, and COOH, and the -Cl functional group among other functional groups showed the highest immobilization efficiency. With this material, we achieved the catalytic hydrolysis of p-nitrophenyl alkyl esters as a function of alkyl chain length such as C4 (PNPB), C8 (PNPO), C12 (PNPD), and C16 (PNPP), respectively. From the Michaelis-Menten kinetics and Lineweaver-Burk plots, various parameters were calculated such as Km, Vmax, and Kcat, and the catalytic hydrolysis of p-nitrophenyl alkyl esters with CalB enzymes immobilized Si-MNPs showed the order of C4 (PNPB) ＞＞ C8 (PNPO) ＞ C12 (PNPD) ＞ C16 (PNPP). This is attributed that the CalB immobilized Si-MNPs showed faster catalytic hydrolysis in short alkyl esters than in long alkyl esters. |
