Assembly of Nano‐Biocatalyst for the Tandem Hydrolysis and Reduction of p‐Nitrophenol Esters

Abstract

Hybrid nano‐biomaterials are exploited in the design and performance of chemo‐enzymatic cascades. In this study, lipase is immobilized from Candida antarctica fraction B (CALB) and gold nanoparticles (Au NPs) on magnetic particles coated with silica (MNP@SiO2) to stepwise hydrolyze and reduce p‐nitrophenyl esters in tandem reaction. The assembly of the two catalysts at the interface of the MNP@SiO2 particles and the temporal control of the reaction turns out to be the most determinant parameters for the cascade kinetics. When both CALB and Au NPs are co‐immobilized at the MNP@SiO2 particle, the tandem reactions take place significantly faster than when both catalysts are physically segregated by their immobilization on different MNP@SiO2 particles. Herein, it is demonstrated that the co‐immobilization of biocatalysts and nanocatalysts in solid materials creates hybrid interfaces that accelerated chemo‐enzymatic tandem reactions.

Design and Preparation of a Bifunctional Nanobiohybrid Catalyst by Combining Palladium and α‐Amylase Enzyme: Application in One‐pot Chemoenzymatic Catalysis

“…In contrast, in concurrent chemoenzymatic reactions, all reactants and catalysts are added simultaneously in a single pot at the beginning of the reaction [3] . Despite that, it is very challenging to conduct a successful concurrent chemoenzymatic reaction in a single‐pot due to the differences in chemical and enzymatic reaction conditions followed by mutual deactivation of both catalysts [3a,4] . Alternatively, the immobilization of both catalysts on solid surfaces avoids incompatibility between both catalysts and allows their recyclability, physical segregation, and separation [5] .…”

“…Likewise, Gallego and group members gave an idea to co‐immobilize the gold nanoparticles and CALB onto a magnetic silica shell (Scheme 1b). They tried to investigate the synergistic kinetic effects of both constituents towards the cascade chemoenzymatic hydrolysis and reduction of para‐nitrophenyl esters [3a] …”