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@SiO 2 ) to stepwise hydrolyze and re...

Full description

Bibliographic Details
Published in:Particle & Particle Systems Characterization
Main Authors: de Barros, Heloise Ribeiro, Tanaka, Lívia Yukari, da Silva, Rafael Trivella Pacheco, Santiago‐Arcos, Javier, de Torresi, Susana I. Córdoba, López‐Gallego, Fernando
Other Authors: Fundação de Amparo à Pesquisa do Estado de São Paulo, Coordenação de Aperfeiçoamento de Pessoal de Nível Superior, Agencia Estatal de Investigación
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 2021
Subjects:
Online Access:http://dx.doi.org/10.1002/ppsc.202100136
https://onlinelibrary.wiley.com/doi/pdf/10.1002/ppsc.202100136
https://onlinelibrary.wiley.com/doi/full-xml/10.1002/ppsc.202100136
Description
Summary: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@SiO 2 ) to stepwise hydrolyze and reduce p‐nitrophenyl esters in tandem reaction. The assembly of the two catalysts at the interface of the MNP@SiO 2 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@SiO 2 particle, the tandem reactions take place significantly faster than when both catalysts are physically segregated by their immobilization on different MNP@SiO 2 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.