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Freezing-directed construction of enzyme/nano interfaces:Reagentless conjugation,superior activity,and better stability
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作者 Ke Quan Jiajie Tong +4 位作者 Lifang Chen shuyao fang Mengjiao Li Linlin Wu Zhihe Qing 《Chinese Chemical Letters》 SCIE CAS CSCD 2024年第1期471-474,共4页
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)... 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,maintaining enzymatic activity while circumventing cumbersome modification remains a formidable challenge.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 conjugation process can be facilely completed at−20°C under aqueous solution.Moreover,with the loading of GOx on AuNP at freezing,the enzyme exhibited superior catalytic activity and stability upon thermal 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 peroxidase(HRP)and papain.This facile conjugation strategy accompanied by remarkable bioactivity expand the possibilities for enzymatic biosensing,microdevice and even drug delivery. 展开更多
关键词 Enzyme conjugation FREEZING AuNPs Catalytic activity
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