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Halloysite Clay Nanotubes for Enzyme Immobilization
Joshua Tully1, Raghuvara Yendluri1, Yuri Lvov1,2
1Institute for Micromanufacturing and Biomedical Engineering Program, Louisiana Tech University , Ruston, Louisiana, United States.
Biomacromolecules
|December 25, 2015
Summary
Halloysite nanotubes effectively immobilize enzymes like laccase, glucose oxidase, and lipase. This nanoconfinement enhances enzyme stability and activity, offering improved biocatalysis for various applications.
Area of Science:
- Materials Science
- Biotechnology
- Nanotechnology
Background:
- Halloysite nanotubes are aluminosilicate nanostructures with unique nanoscale properties.
- Their hollow structure and surface chemistry enable loading and controlled release of active agents.
- Applications include anticorrosions, biocides, and drug delivery.
Purpose of the Study:
- To investigate the immobilization of enzymes (laccase, glucose oxidase, lipase) within halloysite nanotubes.
- To evaluate the loading efficiency, release kinetics, and biocatalytic performance of immobilized enzymes.
- To assess the impact of nanoconfinement on enzyme stability and activity.
Main Methods:
- Proteins were loaded into halloysite nanotubes based on charge interactions.
- Loading capacity and release profiles were quantified.
- Enzyme activity and stability were measured under various conditions (pH, temperature).
Main Results:
- Proteins with negative charge, when above their isoelectric point, were efficiently loaded into the positively charged nanotube lumen.
- Loading reached 6-7 wt %, with one-third released within 5-10 hours and two-thirds retained.
- Immobilized lipase showed enhanced stability at acidic pH, with an alkaline optimum pH shift.
- Immobilized laccase exhibited improved stability over time.
- Immobilized glucose oxidase retained activity up to 70 °C, unlike the native enzyme.
Conclusions:
- Halloysite nanotubes serve as effective carriers for enzyme immobilization.
- Nanoconfinement within halloysite enhances enzyme stability and modifies optimal conditions.
- Immobilized enzymes demonstrate improved performance, enabling enhanced biocatalysis.
