Covalent Immobilization of Candida antarctica Lipase B on Functionalized Hollow Mesoporous Silica Nanoparticles

摘要

Candida antarctica lipase B (CALB) produced by recombinant Pichia pastoris was covalently immobilized to a carboxyl- functionalized hollow mesoporous silica sphere (HMS) synthe- sized by sol-gel precipitation. The HMS was characterized by scanning electron microscopy (SEM), transmission electron microscopy (TEM), X-ray diffractometer (XRD), and Brunauer- Emmett-Teller (BET). The immobilized CALB was characterized through Fourier transform infrared spectra (FT-IR) and elemen- tal analysis to verify the binding of enzyme. The free and immobilized CALB were tested in tributyrin hydrolysis.