Hydroxyapatite nanoparticles modified with metal ions for xylanase immobilization

Area of Science:

• Biotechnology
• Materials Science
• Enzyme Engineering

Background:

• Hydroxyapatite (HA) nanoparticles offer high surface area for enzyme immobilization.
• Metal ion modification (HA-Me²⁺) enhances protein interaction, with potential for enzyme support.
• Xylanase immobilization is crucial for cost-effective industrial applications in biofuel, pharmaceutical, and food sectors.

Purpose of the Study:

• To investigate the immobilization of xylanase on HA nanoparticles modified with Cu²⁺ and Ni²⁺.
• To develop a simple, fast, and efficient immobilization protocol using statistical experimental design.
• To evaluate the stability and reusability of the immobilized xylanase.

Main Methods:

• Systematic study of xylanase immobilization on HA-Cu²⁺ and HA-Ni²⁺ supports.
• Utilized statistical experimental design for protocol optimization.
• Assessed enzyme activity, pH/temperature profiles, and reusability of immobilized xylanase.

Main Results:

• Developed an efficient immobilization protocol via metal-ligand complexation.
• HA-Cu²⁺ demonstrated higher affinity for xylanase compared to HA and HA-Ni²⁺.
• Immobilized xylanase retained native pH/temperature activity profiles and up to 80% activity after the second reuse cycle on HA-Cu²⁺.

Conclusions:

• Xylanase can be successfully immobilized on HA nanoparticles modified with Cu²⁺ and Ni²⁺ using a straightforward method.
• The HA-Cu²⁺ system shows significant promise for repeated use in industrial biocatalysis.
• This immobilization strategy offers a viable route for enhancing enzyme recovery and reducing costs in various industrial processes.