Abstract
Immobilizing enzyme to nano interfaces has demonstrated to be a favorable strategy for prompting the industrialized application of enzyme.Despite tremendous endeavor has been devoted to using gold nanoparticles(AuNPs)as conjugation matrix due to its fascinating physico-chemical properties,main-taining enzymatic activity while circumventing cumbersome modification remains a formidable chal-lenge.Herein,the freezing-directed conjugation of enzyme/nano interfaces was constructed without extra reagent.As the proof of concept,glucose oxidase(GOx)was chosen as model enzyme.The one-pot con-jugation process can be facilely completed at-20 ℃ under aqueous solution.Moreover,with the loading of GOx on AuNP at freezing,the enzyme exhibited superior catalytic activity and stability upon ther-mal and pH perturbation.The mechanism of boosted activity was then discussed in detail.It was found that higher loading density under freezing condition and more enzyme tending to bind AuNPs via Au-S bond were the main factors for the superior activity.More importantly,this methodology was universal and can also be applied to other enzyme which contains natural cysteine,such as horseradish peroxi-dase(HRP)and papain.This facile conjugation strategy accompanied by remarkable bioactivity expand the possibilities for enzymatic biosensing,microdevice and even drug delivery.
基金项目
国家自然科学基金(32001782)
国家自然科学基金(22222402)
湖南省自然科学基金(2021JJ40564)
长沙市自然科学基金(kq2007021)
Opening Foundation of State Key Laboratory of Chemo/Biosensing and Chemometrics,Hunan University(2019013)
Open Project of State Key Laboratory of Supramolecular Structure and Materials(sklssm2023016)
NETL
NSTL
维普
万方数据