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

• Published in: Particle & Particle Systems Characterization
• Main Authors: Heloise Ribeiro de Barros, Lívia Yukari Tanaka, Rafael Trivella Pacheco da Silva, Javier Santiago-Arcos, Susana I. Córdoba de Torresi, Fernando López-Gallego
• Other Authors: RIBEIRO DE BARROS, Heloise, Yukari Tanaka, Lívia, Trivella Pacheco da Silva, Rafael, Santiago-Arcos, Javier, Córdoba de Torresi, Susana I., López-Gallego, Fernando
• Format: Article in Journal/Newspaper
• Language: English
• Published: John Wiley and Sons Inc 2021
• Subjects: biocatalysi; chemo-enzymatic cascade reaction; colloidal chemistry; interfacial interaction; nanocatalysi; nanostructures; Antarc*; Antarctica
• Online Access: https://hdl.handle.net/11583/2995218; https://doi.org/10.1002/ppsc.202100136; https://onlinelibrary.wiley.com/doi/epdf/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.