Hyaluronidase enzyme conjugated polyamidoamine dendrimer: an efficient and stable nanobiocatalyst for enzymatic degradation of hyaluronic acid

Asieh Soozanipour, Asghar Taheri-Kafrani*, Amir Razmjou, Mohsen Asadnia

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

In this work hyper-branched poly (amide amine) (PAMAM) nanoparticles were conjugated with hyaluronidase (Hyal) to produce a robust nano-biocatalyst for hyaluronic acid (HA) degradation. The success enzyme attachment process was confirmed by Fourier transform infrared (FTIR), transmission electron microscopy (TEM), dynamic light scattering (DLS), and UV–Vis. The influence of pH, temperature, and inhibitor on the enzymatic activity of hyaluronidase was also investigated. The optimum pH, temperature and storage time of Hyal-PAMAM nanocomplex were higher than free enzyme. Also, ascorbic acid showed more inhibitory effect on free enzyme, the IC50 values were determined to be around 55 ± 0.7 and 70 ± 0.3 mM for free Hyal and Hyal-PAMAM nanocomplex, respectively. Based on the greater υmax and lower Km, the Hyal-PAMAM showed a better catalytic efficiency for HA degradation. Moreover, the in silico screening of PAMAM/Hyal interactions further confirmed the experimental results. The novel strategy for combining Hyal and PAMAM dendrimer can hold great promise for applications in biomedical, sensing, and industrial catalysis.

Original languageEnglish
Article number118111
JournalJournal of Molecular Liquids
DOIs
Publication statusAccepted/In press - 15 Nov 2021

Keywords

  • Hyaluronidase
  • PAMAM dendrimer
  • Enzyme immobilization
  • Hyaluronic acid
  • Enzymatic degradation
  • Inhibitory activity

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