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

Soozanipour, A; Taheri-Kafrani, A; Razmjou, A; Asadnia, M

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

Soozanipour, A Taheri-Kafrani, A Razmjou, A Asadnia, M

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Publisher:: ELSEVIER
Publication Type:: Journal Article
Citation:: Journal of Molecular Liquids, 2022, 349
Issue Date:: 2022-03-01

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Field	Value	Language
dc.contributor.author	Soozanipour, A
dc.contributor.author	Taheri-Kafrani, A
dc.contributor.author	Razmjou, A
dc.contributor.author	Asadnia, M
dc.date.accessioned	2023-03-26T23:00:36Z
dc.date.available	2023-03-26T23:00:36Z
dc.date.issued	2022-03-01
dc.identifier.citation	Journal of Molecular Liquids, 2022, 349
dc.identifier.issn	0167-7322
dc.identifier.issn	1873-3166
dc.identifier.uri	http://hdl.handle.net/10453/168454
dc.description.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.
dc.language	English
dc.publisher	ELSEVIER
dc.relation.ispartof	Journal of Molecular Liquids
dc.relation.isbasedon	10.1016/j.molliq.2021.118111
dc.rights	info:eu-repo/semantics/closedAccess
dc.subject	0306 Physical Chemistry (incl. Structural)
dc.subject.classification	Chemical Physics
dc.title	Hyaluronidase enzyme conjugated polyamidoamine dendrimer: An efficient and stable nanobiocatalyst for enzymatic degradation of hyaluronic acid
dc.type	Journal Article
utslib.citation.volume	349
utslib.for	0306 Physical Chemistry (incl. Structural)
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Engineering and Information Technology
pubs.organisational-group	/University of Technology Sydney/Faculty of Engineering and Information Technology/School of Civil and Environmental Engineering
utslib.copyright.status	closed_access	*
dc.date.updated	2023-03-26T23:00:35Z
pubs.publication-status	Published
pubs.volume	349

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.

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http://hdl.handle.net/10453/168454