Related Experiment Video
Updated: Oct 11, 2025
12:48
PLGA Nanoparticles Formed by Single- or Double-emulsion with Vitamin E-TPGS
Published on: December 27, 2013
65.7K
Tween® Preserves Enzyme Activity and Stability in PLGA Nanoparticles
Jason Thomas Duskey1, Ilaria Ottonelli1,2, Arianna Rinaldi1,2
1Te.Far.T.I.-Nanotech Lab, Department of Life Sciences, University of Modena and Reggio Emilia, 41125 Modena, Italy.
Nanomaterials (Basel, Switzerland)
|November 27, 2021
Summary
Optimizing Tween® 20 stabilizer in poly(lactic-co-glycolic) acid nanoparticle formulations significantly enhances beta-glucosidase enzyme activity and stability, leading to more effective enzyme-loaded nanoparticles for potential therapeutic applications.
Area of Science:
- Biomaterials Science
- Enzyme Engineering
- Nanotechnology
Background:
- Enzymes are promising therapeutic molecules but suffer from instability during nanoparticle formulation.
- Stabilizers like Tween® polysorbates can protect enzyme activity, but their use is often unoptimized.
- Poly(lactic-co-glycolic) acid (PLGA) nanoparticles are widely used for drug delivery.
Purpose of the Study:
- To compare the effects of different Tween® polysorbates (20, 60, 80) on beta-glucosidase (β-Glu) loaded into PLGA nanoparticles.
- To optimize the molar ratio of Tween® 20 to β-Glu for improved enzyme stability and activity within nanoparticles.
- To investigate the binding affinity between Tween® 20 and β-Glu and its impact on nanoparticle characteristics and enzyme release.
Main Methods:
- Formulation of PLGA nanoparticles loaded with β-glucosidase and varying concentrations of Tween® 20, 60, or 80.
- Characterization of nanoparticle size, zeta potential, morphology, and enzyme loading efficiency.
- Assessment of enzyme activity and stability using isothermal titration calorimetry and activity assays.
- Evaluation of enzyme release profiles from the nanoparticles.
Main Results:
- Pre-formulation with Tween® 20, 60, or 80 increased enzyme loading but did not affect nanoparticle size or physical characteristics.
- Nanoparticles formulated with Tween® 20:β-Glu solutions exhibited significantly higher retained enzyme activity compared to other Tween® types.
- Optimization of Tween® 20:β-Glu molar ratios showed a trend towards higher activity with increased Tween® 20 concentration.
- While initial burst release was similar to free enzyme, the encapsulated enzyme remained active longer in solution.
Conclusions:
- Tween® 20 is a superior stabilizer for β-glucosidase loaded into PLGA nanoparticles compared to Tween® 60 and 80.
- Optimizing the concentration of Tween® 20 during nanoparticle formulation is crucial for maximizing enzyme activity and stability.
- These findings provide a foundation for developing more effective enzyme-loaded nanoparticle therapeutics.
