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

• Published in: Particle & particle systems characterization 2021-10, Vol.38 (10), p.n/a
• Main Authors: Barros, Heloise Ribeiro, Tanaka, Lívia Yukari, da Silva, Rafael Trivella Pacheco, Santiago‐Arcos, Javier, Torresi, Susana I. Córdoba, López‐Gallego, Fernando
• Format: Article
• Language: English
• Subjects: Assembly; biocatalysis; Biomedical materials; Cascade chemical reactions; Catalysts; chemo‐enzymatic cascade reactions; colloidal chemistry; Esters; Gold; Immobilization; interfacial interactions; nanocatalysis; Nanoparticles; nanostructures; Nitrophenol; Silicon dioxide
• ISSN: 0934-0866; 1521-4117
• DOI: 10.1002/ppsc.202100136

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. The assembly of biocatalysts and nanocatalysts matters to the more efficient chemo‐enzymatic cascade reactions. The comparison of co‐immobilized and physically segregated assemblies reveals that interfacial interactions play a key role in both concurrent and sequential nano‐biocatalysis reaction modes. The overall performance is regulated by exploiting the localization of enzymes and Au nanoparticles on the surface of magnetic nanoparticles.