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Efficient enzymatic degradation of hyaluronic acid by hyaluronidase-conjugated polyamidoamine dendrimer: A robust and stable nanobiocatalyst
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  • Asieh Soozanipour,
  • Asghar Taheri-Kafrani,
  • Amir Razmjou,
  • Mohsen Asadnia
Asieh Soozanipour
University of Isfahan
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Asghar Taheri-Kafrani
University of Isfahan

Corresponding Author:[email protected]

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Amir Razmjou
University of Isfahan
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Mohsen Asadnia
Macquarie University
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Abstract

In this work hyper-branched poly (amide amine) (PAMAM) nanoparticles were conjugated with Hyaluronidase to produce a robust nano-biocatalyst for hyaluronic acid (HA) degradation. The success enzyme attachment process was confirmed by FTIR, UV-Vis, transmission electron microscopy (TEM), and dynamic light scattering (DLS). The influence of pH, temperature, and inhibitor on enzymatic activity of hyaluronidase (Hyal) were 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 grater 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.