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

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-nitr...

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Bibliographic Details
Published in:Particle & Particle Systems Characterization
Main Authors: Barros, HR, Tanaka, LY, da Silva, RTP, Santiago‐Arcos, J, Torresi, SIC, López‐Gallego, F.
Format: Article in Journal/Newspaper
Language:unknown
Published: Zenodo 2021
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Online Access:https://doi.org/10.1002/ppsc.202100136
Description
Summary: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.