Hoang V. Tran, Nghia D. Nguyen, Anh-Tuan Le, Luyen T. Tran, Thu D. Le and Chinh D. Huynh
{"title":"Fe3O4@C magnetite nanocomposite: an artificial peroxidase nanozyme for the development of a colorimetric glucose biosensor†","authors":"Hoang V. Tran, Nghia D. Nguyen, Anh-Tuan Le, Luyen T. Tran, Thu D. Le and Chinh D. Huynh","doi":"10.1039/D4NJ03808H","DOIUrl":null,"url":null,"abstract":"<p >Horseradish peroxidase (HRP), a natural enzyme, consists of a Fe<small><sup>III</sup></small> ion, which plays the role as an active center of the enzyme, wherein the binding of H<small><sub>2</sub></small>O<small><sub>2</sub></small> to the Fe<small><sup>III</sup></small> ion creates an octahedral configuration around Fe<small><sup>III</sup></small>, leading to the decomposition of the –O–O– bond of H<small><sub>2</sub></small>O<small><sub>2</sub></small>. Based on this considering, here, we propose amorphous-carbon-functionalized Fe<small><sub>3</sub></small>O<small><sub>4</sub></small> nanoparticles (Fe<small><sub>3</sub></small>O<small><sub>4</sub></small>@C) that serve as a peroxidase nanozyme with Fe<small><sup>III</sup></small> and exhibits peroxidase-like catalytic activity. In this work, Fe<small><sub>3</sub></small>O<small><sub>4</sub></small>@C was synthesized <em>via</em> a simple hydrothermal process from a suspension of Fe<small><sub>3</sub></small>O<small><sub>4</sub></small> nanoparticles and glucose solution. The peroxidase-mimicking activity of Fe<small><sub>3</sub></small>O<small><sub>4</sub></small>@C was demonstrated following the Michaelis–Menten and Lineweaver–Burk equations of the enzymatic model. At optimized conditions, Fe<small><sub>3</sub></small>O<small><sub>4</sub></small>@C showed stronger catalytic activity than HRP, with Michaelis–Menten constants (<em>K</em><small><sub>m</sub></small>) 0.052 mM and 0.004 mM for the H<small><sub>2</sub></small>O<small><sub>2</sub></small> substrate and TMB co-substrate, respectively. Using Fe<small><sub>3</sub></small>O<small><sub>4</sub></small>@C as a replacement for HRP, a colorimetric chemical sensor for H<small><sub>2</sub></small>O<small><sub>2</sub></small> sensing and a colorimetric biosensor for glucose detection were constructed, and they exhibited high selectivity and sensitivity with an LOD of 20 μM for H<small><sub>2</sub></small>O<small><sub>2</sub></small> and 40 μM for glucose. The applicability of the glucose biosensor was also tested in real samples, including a 5% intravenous glucose solution and human blood serum, revealing high recovery rates.</p>","PeriodicalId":95,"journal":{"name":"New Journal of Chemistry","volume":" 47","pages":" 20007-20017"},"PeriodicalIF":2.7000,"publicationDate":"2024-11-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"New Journal of Chemistry","FirstCategoryId":"92","ListUrlMain":"https://pubs.rsc.org/en/content/articlelanding/2024/nj/d4nj03808h","RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
引用次数: 0
Abstract
Horseradish peroxidase (HRP), a natural enzyme, consists of a FeIII ion, which plays the role as an active center of the enzyme, wherein the binding of H2O2 to the FeIII ion creates an octahedral configuration around FeIII, leading to the decomposition of the –O–O– bond of H2O2. Based on this considering, here, we propose amorphous-carbon-functionalized Fe3O4 nanoparticles (Fe3O4@C) that serve as a peroxidase nanozyme with FeIII and exhibits peroxidase-like catalytic activity. In this work, Fe3O4@C was synthesized via a simple hydrothermal process from a suspension of Fe3O4 nanoparticles and glucose solution. The peroxidase-mimicking activity of Fe3O4@C was demonstrated following the Michaelis–Menten and Lineweaver–Burk equations of the enzymatic model. At optimized conditions, Fe3O4@C showed stronger catalytic activity than HRP, with Michaelis–Menten constants (Km) 0.052 mM and 0.004 mM for the H2O2 substrate and TMB co-substrate, respectively. Using Fe3O4@C as a replacement for HRP, a colorimetric chemical sensor for H2O2 sensing and a colorimetric biosensor for glucose detection were constructed, and they exhibited high selectivity and sensitivity with an LOD of 20 μM for H2O2 and 40 μM for glucose. The applicability of the glucose biosensor was also tested in real samples, including a 5% intravenous glucose solution and human blood serum, revealing high recovery rates.
辣根过氧化物酶(HRP)是一种天然酶,由FeIII离子组成,作为酶的活性中心,H2O2与FeIII离子结合在FeIII周围形成八面体结构,导致H2O2的- o - o -键分解。在此基础上,我们提出了非晶碳功能化的Fe3O4纳米颗粒(Fe3O4@C),它可以作为含FeIII的过氧化物酶纳米酶,并具有类似过氧化物酶的催化活性。在这项工作中,通过简单的水热法,以Fe3O4纳米颗粒悬浮液和葡萄糖溶液为原料合成了Fe3O4@C。根据酶模型的Michaelis-Menten和Lineweaver-Burk方程证明了Fe3O4@C的过氧化物酶模拟活性。在优化条件下,Fe3O4@C的催化活性高于HRP, H2O2底物和TMB共底物的Michaelis-Menten常数分别为0.052 mM和0.004 mM。利用Fe3O4@C替代HRP,构建了H2O2比色化学传感器和葡萄糖比色生物传感器,对H2O2和葡萄糖的LOD分别为20 μM和40 μM,具有较高的选择性和灵敏度。葡萄糖生物传感器的适用性也在实际样品中进行了测试,包括5%静脉注射葡萄糖溶液和人血清,显示出很高的回收率。