Thermally Stable and Reusable Silica and Nano-Fructosome Encapsulated CalB Enzyme Particles for Rapid Enzymatic Hydrolysis and Acylation

• Published in: International Journal of Molecular Sciences
• Main Authors: Woo Young Jang, Jung Hoon Sohn, Jeong Ho Chang
• Format: Article in Journal/Newspaper
• Language: English
• Published: MDPI AG 2023
• Subjects: thermal stability; reusability; silica; encapsulation; CalB enzyme; nano-fructosome; Biology (General); QH301-705.5; Chemistry; QD1-999; Antarc*; Antarctica
• Online Access: https://doi.org/10.3390/ijms24129838; https://doaj.org/article/3bfeecab7f924485b603d57eda6ef040

This study reports the preparation of silica-coated and nano-fructosome encapsulated Candida antarctica lipase B particles (CalB@NF@SiO 2 ) and a demonstration of their enzymatic hydrolysis and acylation. CalB@NF@SiO 2 particles were prepared as a function of TEOS concentration (3–100 mM). Their mean particle size was 185 nm by TEM. Enzymatic hydrolysis was performed to compare catalytic efficiencies of CalB@NF and CalB@NF@SiO 2 . The catalytic constants (K m , V max , and K cat ) of CalB@NF and CalB@NF@SiO 2 were calculated using the Michaelis–Menten equation and Lineweaver–Burk plot. Optimal stability of CalB@NF@SiO 2 was found at pH 8 and a temperature of 35 °C. Moreover, CalB@NF@SiO 2 particles were reused for seven cycles to evaluate their reusability. In addition, enzymatic synthesis of benzyl benzoate was demonstrated via an acylation reaction with benzoic anhydride. The efficiency of CalB@NF@SiO 2 for converting benzoic anhydride to benzyl benzoate by the acylation reaction was 97%, indicating that benzoic anhydride was almost completely converted to benzyl benzoate. Consequently, CalB@NF@SiO 2 particles are better than CalB@NF particles for enzymatic synthesis. In addition, they are reusable with high stability at optimal pH and temperature.