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Sci Rep ; 13(1): 18220, 2023 10 25.
Article in English | MEDLINE | ID: mdl-37880390

ABSTRACT

Spinal cord injury healing has been shown to be aided by chondroitinase ABC I (cABCI) treatment. The transport of cABCI to target tissues is complicated by the enzyme's thermal instability; however, cABCI may be immobilized on nanosheets to boost stability and improve delivery efficiency. This investigation's goal was to assess the immobilization of cABC I on graphene oxide (GO). for this purpose, GO was produced from graphene using a modified version of Hummer's process. the immobilization of cABC I on GO was examined using SEM, XRD, and FTIR. The enzymatic activity of cABC I was evaluated in relation to substrate concentration. The enzyme was then surface-adsorption immobilized on GO, and its thermal stability was examined. As compared to the free enzyme, the results showed that the immobilized enzyme had a greater Km and a lower Vmax value. The stability of the enzyme was greatly improved by immobilization at 20, 4, 25, and 37 °C. For example, at 37 °C, the free enzyme retained 5% of its activity after 100 min, while the immobilized one retained 30% of its initial activity. The results showed, As a suitable surface for immobilizing cABC I, GO nano sheets boost the enzyme's stability, improving its capability to support axonal regeneration after CNC damage and guard against fast degradation.


Subject(s)
Chondroitinsulfatases , Graphite , Spinal Cord Injuries , Humans , Enzyme Stability , Chondroitinases and Chondroitin Lyases/metabolism , Enzymes, Immobilized/metabolism , Chondroitinsulfatases/metabolism , Hyaluronoglucosaminidase/metabolism , Spinal Cord Injuries/therapy , Hydrogen-Ion Concentration , Temperature , Kinetics
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