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Peer-reviewedCC BY 4.0ACS Omega

Development of Supramolecular Calix[4]arene-MCM-Based Nanomaterials Doped with CuNPs: An Inorganic–Organic Hybrid Recyclable Nanoenzyme as a Potent Peroxidase and Oxidase Mimic

  1. 1J.C. Bose University of Science and Technology, YMCA , , , ,
  2. 2Indian Institute of Technology Bombay , , , ,
  3. 3University of Virginia , , , ,

Abstract

An inorganic–organic hybrid nanomaterial, Cu@MCMCal, was synthesized by immobilizing p-tert-butyl calix[4]arene on to mesoporous silica followed by incorporation of CuNPs. The synthesized nanomaterial was characterized extensively using various analytical techniques such as FT-IR, UV–Vis spectroscopy, TEM, PXRD, XPS, Cu LMM Auger, BET, and TGA analyses. The hybrid nanomaterial was evaluated for its catalytic performance toward peroxidase-like activity using 3,3′,5,5′-tetramethylbenzidine (TMB) and o-phenylenediamine (OPD) as a substrate at room temperature at pH 4.5 in acetate buffer and pH 7.4 in PBS buffer, respectively. Enzyme kinetics was performed for both the substrates using the Michaelis–Menten steady-state kinetics and the Lineweaver–Burk plot to determine the catalytic affinity. Based on the kinetic measurements, the values of the Km for TMB and OPD were found to be 0.661 ± 0.143 and 0.606 ± 0.061 mM, respectively. The hybrid nanoenzyme also exhibits the oxidase-like activity using dopamine as a substrate at pH 7.4 in PBS buffer. The Cu@MCMCal nanomaterial acted as a nanoenzyme, efficient for catalysis toward oxidation reactions with better cost effectiveness and improved stability and recyclability as compared to biological enzymes. Therefore, a promising, stable, efficient, and robust nanoenzyme has been development for oxidation reactions.

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BibTeX
@article{goyal2026development,
  title = {{Development of Supramolecular Calix[4]arene-MCM-Based Nanomaterials Doped with CuNPs: An Inorganic–Organic Hybrid Recyclable Nanoenzyme as a Potent Peroxidase and Oxidase Mimic}},
  author = {Meenakshi Goyal and Anuj Kumar and Pardeep Kumar and Bhawna Uttam},
  journal = {ACS Omega},
  year = {2026},
  month = oct,
  doi = {10.1021/acsomega.6c07489},
  url = {https://pubs.acs.org/acsodf/article/doi/10.1021/acsomega.6c07489/5453036/Development-of-Supramolecular-Calix-4-arene-MCM},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - Development of Supramolecular Calix[4]arene-MCM-Based Nanomaterials Doped with CuNPs: An Inorganic–Organic Hybrid Recyclable Nanoenzyme as a Potent Peroxidase and Oxidase Mimic
AU  - Meenakshi Goyal
AU  - Anuj Kumar
AU  - Pardeep Kumar
AU  - Bhawna Uttam
PY  - 2026
DA  - 2026/10/16
JO  - ACS Omega
DO  - 10.1021/acsomega.6c07489
UR  - https://pubs.acs.org/acsodf/article/doi/10.1021/acsomega.6c07489/5453036/Development-of-Supramolecular-Calix-4-arene-MCM
AB  - An inorganic–organic hybrid nanomaterial, Cu@MCMCal, was synthesized by immobilizing p-tert-butyl calix[4]arene on to mesoporous silica followed by incorporation of CuNPs. The synthesized nanomaterial was characterized extensively using various analytical techniques such as FT-IR, UV–Vis spectroscopy, TEM, PXRD, XPS, Cu LMM Auger, BET, and TGA analyses. The hybrid nanomaterial was evaluated for its catalytic performance toward peroxidase-like activity using 3,3′,5,5′-tetramethylbenzidine (TMB) and o-phenylenediamine (OPD) as a substrate at room temperature at pH 4.5 in acetate buffer and pH 7.4 in PBS buffer, respectively. Enzyme kinetics was performed for both the substrates using the Michaelis–Menten steady-state kinetics and the Lineweaver–Burk plot to determine the catalytic affinity. Based on the kinetic measurements, the values of the Km for TMB and OPD were found to be 0.661 ± 0.143 and 0.606 ± 0.061 mM, respectively. The hybrid nanoenzyme also exhibits the oxidase-like activity using dopamine as a substrate at pH 7.4 in PBS buffer. The Cu@MCMCal nanomaterial acted as a nanoenzyme, efficient for catalysis toward oxidation reactions with better cost effectiveness and improved stability and recyclability as compared to biological enzymes. Therefore, a promising, stable, efficient, and robust nanoenzyme has been development for oxidation reactions.
SN  - 2470-1343
ER  -