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chondroitinase-abc-i-enzyme
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Experimental Study of Biological Synthesis, Stabilization and Delivery of the Recombinant Protein of Chondroitinase
, Ph.D. Dissertation Sharif University of Technology ; Vossoughi, Manouchehr (Supervisor) ; Alemzadeh, Iran (Supervisor) ; Khajeh, Khosro (Supervisor)
Abstract
In this research, immobilization method was employed to increase the thermal stability of Chondroitinase ABC I (cABC I) enzyme. In first step, magnetite nanoparticle (Fe3O4) was selected as a support and cABC I enzyme was attached via the adsorption method. The results showed that pH=6.5, temperature 15 ˚C, enzyme-to-support mass ratio 0.75, and incubation time 4.5 hr were the appropriate conditions for immobilizing cABC I enzyme on Fe3O4 nanoparticle. It was also found that the optimum pH for free and immobilized enzymes was 7.6 and 8.0, respectively. The maximum activity of free enzyme was obtained at 25 ˚C, whereas the activity of immobilized enzyme was almost constant in the temperature...
Examination of chondroitinase ABC I immobilization onto dextran-coated Fe3O4 nanoparticles and its in-vitro release
, Article Journal of Biotechnology ; Volume 309 , 2020 , Pages 131-141 ; Vossoughi, M ; Khajeh, K ; Alemzadeh, I ; Sharif University of Technology
Elsevier B.V
2020
Abstract
Chondroitinase ABC I (cABC I) has received notable attention in treatment of spinal cord injuries and its application as therapeutics has been limited due to low thermal stability at physiological temperature. In this study, cABC I enzyme was immobilized on the dextran-coated Fe3O4 nanoparticles through physical adsorption to improve the thermal stability. The nanoparticles were characterized using XRD, SEM, VSM, and FTIR analyses. Response surface methodology and central composite design were employed to assess factors affecting the activity of immobilized cABC I. Experimental results showed that pH 6.3, temperature 24 °C, enzyme/support mass ratio 1.27, and incubation time 5.7 h were the...