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  • Title: Immobilization of collagenase in inorganic hybrid nanoflowers with enhanced stability, proteolytic activity, and their anti-amyloid potential.
    Author: Jamal HS, Raja R, Ahmed S, Yesiloz G, Ali SA.
    Journal: Int J Biol Macromol; 2024 Aug; 274(Pt 1):133114. PubMed ID: 38871102.
    Abstract:
    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 (IC50 = 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.
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