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J. Korean Ceram. Soc. > Volume 61(1); 2024 > Article
Journal of the Korean Ceramic Society 2024;61(1): 126-136.
doi: https://doi.org/10.1007/s43207-023-00355-9
Nanofructosome encapsulated CalB enzyme immobilized silica-coated magnetic nanoparticles for rapid enzymatic hydrolysis and acylation
Yu Jeong Kim1,2, Woo Young Jang1, Jeong Ho Chang1
1Korea Institute of Ceramic Engineering and Technology, Chungbuk, 28160, Korea
2Department of Chemical Engineering, Yonsei University, Seoul, 03722, Korea
Correspondence  Jeong Ho Chang ,Email: jhchang@kicet.re.kr
Received: August 23, 2023; Revised: November 23, 2023   Accepted: November 25, 2023.  Published online: December 12, 2023.
ABSTRACT
This study reports the preparation of Candida Antarctic lipase B (CalB) enzyme and nanofructosome encapsulated CalB enzyme (CalB@NF) immobilized silica coated magnetic nanoparticles (Si-MNPs) and demonstration of the enzymatic hydrolysis and acylation against p-nitrophenyl butyrate (p-NPB) and benzoic anhydride. Si-MNPs was prepared 60 nm of particle size with spherical shape, and the immobilization of CalB and CalB@NF was coupled by chlorosilane linker on the surface of Si-MNPs. The quantitative determination of CalB in Si-MNPs@CalB and Si-MNPs@CalB@NF was followed by Bradford assay. Various enzymatic kinetic parameters such as Km, Vmax, and Kcat were calculated using the Lineweaver-Burk equation and Michaelis-Menten kinetics. The hydrolysis of p-NPB with Si-MNPs@CalB@NF and Si-MNPS@CalB confirmed their utilization as effective catalysts. Furthermore, all four samples of native CalB, CalB@NF, Si-MNPs@CalB, and Si-MNPs@CalB@NF were successfully acylated to benzyl benzoate after column separation, and showed more than 99% conversion efficiency. The stability for pH and temperature of Si-MNPs@CalB and Si-MNPs@CalB@NF was optimized at 8 and 45 ℃, respectively.
Key words: CalB enzyme · Nanofructosome · Hydrolysis · Acylation · Magnetic nanoparticles · Cross-linkers
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