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J. Korean Ceram. Soc. > Volume 59(4); 2022 > Article
Journal of the Korean Ceramic Society 2022;59(4): 527-535.
doi: https://doi.org/10.1007/s43207-021-00181-x
Reusable and rapid esterolysis of nitrophenyl alkanoates with CalB enzyme‑immobilized magnetic nanoparticles
Ha Yull Lee, Woo Young Jang, Jeong Ho Chang
Center for Convergence Bioceramic Materials, Korea Institute of Ceramic Engineering and Technology (KICET), Chungbuk 28160, South Korea
Correspondence  Jeong Ho Chang ,Email: jhchang@kicet.re.kr
Received: October 18, 2021; Revised: December 8, 2021   Accepted: December 15, 2021.  Published online: July 31, 2022.
This study reports the preparation of the Candida antarctica lipase B (CalB) enzyme immobilization on silica-coated magnetic nanoparticles (Si-MNPs@CalB) using various cross-linkers and demonstration of rapid catalytic hydrolysis of p-nitrophenyl alkyl esters. CalB enzymes were coupled with diferent cross-linker silanes on the Si-MNPs surface. Among these cross-linkers, Cl-functionalized silane was better at immobilization of CalB than the others. Catalytic hydrolysis of p-nitrophenyl alkyl esters was demonstrated against 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, and Kcat) were calculated. Catalytic hydrolysis was faster in shorter alkyl chain of p-nitrophenyl alkyl esters with Si-MNPs@CalB in the order C4>> C8> C12>> C16. Furthermore, the reusability and optimum catalytic activity of Si-MNPs@ CalB were evaluated as a function of the number of reuses and with diferent pH values.
Key words: CalB enzyme · Catalytic hydrolysis · Magnetic nanoparticles · Cross-linkers · Nitrophenyl alkanoates
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