Enzymatic behavior of laccase following interaction with γ-CD and immobilization into PCL nanofibers

• Successful immobilization of pure laccase and laccase-γ-CD complex into nanofibers.
• Improved enzyme activity and increased enzyme stability by CD use.
• Better enzyme activity by encapsulation methods than layering methods.
• Non inclusion complex formation instead of inclusion complex formation.

This study examines the effects of CD use on enzymatic activity, following enzyme immobilization into nanofibers. There is almost no research available on the change in enzyme activity following interaction with cyclodextrin and electrospun nanofiber mats together. Laccase enzyme was immobilized into nanofibrous structures by various techniques, with and without γ-CD addition, and the enzymatic activity of the laccase was analyzed. SEM, XRD, and FTIR analyses were used for the characterization of the resulting structures. Our results showed that cyclodextrin use has a positive effect on the enzyme's activity, and increases its stability. The enzymes treated by cyclodextrin showed activation after complex formation trials, and no activation loss or enzyme denaturation was detected. Our conclusions were supported by the enzyme activity test results, which also showed that immobilization by encapsulation methods gave better activity results than layering methods. Another important finding concerned the laccase's stable characteristics that helped to maintain its enzyme activation after the freeze drying process. Among all test groups, the best activity result was recorded by laccase-γ-CD complex encapsulated PCL nanofibers with 96.48 U/mg.

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