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: Jang, Woo Young, Sohn, Jung Hoon, Chang, Jeong Ho
• Format: Text
• Language: English
• Published: MDPI 2023
• Subjects: Article; Antarc*; Antarctica
• Online Access: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10298207/; http://www.ncbi.nlm.nih.gov/pubmed/37372985; https://doi.org/10.3390/ijms24129838

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.