| 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 |
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Received: August 23, 2023; Revised: November 23, 2023 Accepted: November 25, 2023. Published online: December 12, 2023. |
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| ABSTRACT |
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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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