Immobilization of collagenase in inorganic hybrid nanoflowers with enhanced stability, proteolytic activity, and their anti-amyloid potential.

Autor: Jamal HS; Third World Center for Science and Technology, H.E.J. Research Institute of Chemistry, University of Karachi, Karachi 75270, Pakistan., Raja R; Third World Center for Science and Technology, H.E.J. Research Institute of Chemistry, University of Karachi, Karachi 75270, Pakistan., Ahmed S; Third World Center for Science and Technology, H.E.J. Research Institute of Chemistry, University of Karachi, Karachi 75270, Pakistan., Yesiloz G; National Nanotechnology Research Center of Turkiye, Institute of Materials Science and Nanotechnology, Bilkent University-UNAM-Universiteler Mah, 06800 Cankaya, Ankara, Turkey., Ali SA; Third World Center for Science and Technology, H.E.J. Research Institute of Chemistry, University of Karachi, Karachi 75270, Pakistan. Electronic address: abid.ali@iccs.edu.
Jazyk: angličtina
Zdroj: International journal of biological macromolecules [Int J Biol Macromol] 2024 Aug; Vol. 274 (Pt 1), pp. 133114. Date of Electronic Publication: 2024 Jun 12.
DOI: 10.1016/j.ijbiomac.2024.133114
Abstrakt: Organic-inorganic hybrid nanomaterials are considered as promising immobilization matrix for enzymes owing to their markedly enhanced stability and reusability. Herein, collagenase was chosen as a model enzyme to synthesize collagenase hybrid nanoflowers (Col-hNFs). Maximum collagenase activity (155.58 μmol min -1  L -1 ) and encapsulation yield (90 %) were observed in presence of Zn(II) ions at 0.05 mg/mL collagenase, 120 mM zinc chloride and PBS (pH 7.5). Synthesized Col-Zn-hNFs were extensively characterized by scanning electron microscopy (SEM), energy dispersive X-ray (EDX), X-ray diffraction (XRD), Fourier transform infrared (FTIR), circular dichroism (CD), fluorescence spectroscopy, dynamic light scattering (DLS) and zeta potential measurements. SEM images showed flower-like morphology with average size of 5.1 μm and zeta potential of -14.3 mV. Col-Zn-hNFs demonstrated superior relative activity across wide pH and temperature ranges, presence of organic solvents and surfactants as compared to its free form. Moreover, Col-Zn-hNFs exhibited excellent shelf life stability and favorable reusability. Col-Zn-hNFs showed the ability to suppress and eradicate fully developed insulin fibrils in vitro (IC 50  = 2.8 and 6.2 μg/mL, respectively). This indicates a promising inhibitory potential of Col-Zn-hNFs against insulin amyloid fibrillation. The findings suggest that the utilization of Col-Zn-hNFs as a carrier matrix holds immense potential for immobilizing collagenase with improved catalytic properties and biomedical applications.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024. Published by Elsevier B.V.)
Databáze: MEDLINE
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