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Assembly of Nano-Biocatalyst for the Tandem Hydrolysis and Reduction of p-Nitrophenol Esters
Particle & Particle Systems Characterization ( IF 2.7 ) Pub Date : 2021-08-26 , DOI: 10.1002/ppsc.202100136
Heloise Ribeiro Barros 1, 2 , Lívia Yukari Tanaka 1 , Rafael Trivella Pacheco da Silva 1 , Javier Santiago‐Arcos 2 , Susana I. Córdoba Torresi 1 , Fernando López‐Gallego 2, 3
Affiliation  

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.

中文翻译:

用于串联水解和还原对硝基苯酚酯的纳米生物催化剂的组装

混合纳米生物材料用于化学酶级联的设计和性能。在这项研究中,脂肪酶从南极念珠菌组分 B (CALB) 和金纳米颗粒 (Au NPs) 固定在涂有二氧化硅 (MNP@SiO 2 ) 的磁性颗粒上,以串联反应逐步水解和还原对硝基苯酯。两种催化剂在 MNP@SiO 2颗粒界面处的组装和反应的时间控制是级联动力学的最决定性参数。当 CALB 和 Au NPs 共同固定在 MNP@SiO 2 上时颗粒,串联反应的发生速度明显快于两种催化剂通过固定在不同的 MNP@SiO 2颗粒上而物理分离的情况。在此,证明了生物催化剂和纳米催化剂在固体材料中的共固定产生了加速化学酶促串联反应的混合界面。
更新日期:2021-10-18
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