Halloysite Clay Nanotubes for Enzyme Immobilization
| Autor: | Joshua Tully, Raghuvara Yendluri, Yuri Lvov |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
Polymers and Plastics
Immobilized enzyme Bioengineering 02 engineering and technology engineering.material 010402 general chemistry 01 natural sciences Halloysite Biomaterials Glucose Oxidase Aluminosilicate Materials Chemistry Organic chemistry Glucose oxidase Lipase Laccase Nanotubes biology Chemistry Temperature Hydrogen-Ion Concentration Enzymes Immobilized 021001 nanoscience & nanotechnology Controlled release 0104 chemical sciences Kinetics Isoelectric point Chemical engineering engineering biology.protein Clay Aluminum Silicates Adsorption 0210 nano-technology Protein Binding |
| Zdroj: | Biomacromolecules. 17:615-621 |
| ISSN: | 1526-4602 1525-7797 |
| DOI: | 10.1021/acs.biomac.5b01542 |
| Popis: | Halloysite clay is an aluminosilicate nanotube formed by rolling flat sheets of kaolinite clay. They have a 15 nm lumen, 50-70 nm external diameter, length of 0.5-1 μm, and different inside/outside chemistry. Due to these nanoscale properties, they are used for loading, storage, and controlled release of active chemical agents, including anticorrosions, biocides, and drugs. We studied the immobilization in halloysite of laccase, glucose oxidase, and lipase. Overall, negatively charged proteins taken above their isoelectric points were mostly loaded into the positively charged tube's lumen. Typical tube loading with proteins was 6-7 wt % from which one-third was released in 5-10 h and the other two-thirds remained, providing enhanced biocatalysis in nanoconfined conditions. Immobilized lipase showed enhanced stability at acidic pH, and the optimum pH shifted to more alkaline pH. Immobilized laccase was more stable with respect to time, and immobilized glucose oxidase showed retention of enzymatic activity up to 70 °C, whereas the native sample was inactive. |
| Databáze: | OpenAIRE |
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