Polyaniline nanofiber as a novel immobilization matrix for the anti-leukemia enzyme l-asparaginase

In this study, polyaniline nanofibers are used as a novel immobilization support and evaluated using l-asparaginase as a model protein enzyme for precise investigation of the immobilized state of enzymes as well as its functional activity on polyaniline nanofiber surfaces at different concentrations. The supported enzyme has been characterized by XPS, XRD, TEM and FTIR, and the effect of polymer nanofiber conformations on the enzymatic activity is discussed in detail. Immobilized l-asparaginase showed greater stability towards decomposition/denaturation at different temperatures and pH conditions compared to the free enzyme. The calculated Km values are 1.809 and 3.705 mM L−1 for immobilized l-asparaginase, respectively, which are 2.05-fold lower in magnitude in comparison with the value obtained for free l-asparaginase; the Vmax values for immobilized and free l-asparaginase are 90.57 and 48.04 μM min−1 mg−1 respectively.

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► Polyaniline nanofiber was used as a novel immobilization support for l-asparaginase as a model protein enzyme for precise investigation of the immobilized state of enzymes as well as its functional activity on polyaniline nano sized fiber surfaces at different concentrations.
► Supporting process was confirmed by the characterization of the supported enzyme by XPS, XRD, TEM and FTIR.
► Effect of polymer nanofiber conformations on the enzymatic activity was discussed in detail.
► Influence of external temperature and pH of the medium on the karyotypic properties of the enzyme was studied in detail.