Stabilizing Enzymes within Polymersomes by Coencapsulation of Trehalose

Area of Science:

• Biochemistry
• Materials Science
• Nanotechnology

Background:

• Enzymes are crucial biocatalysts with therapeutic potential.
• Enzyme functionality heavily depends on stability, which is compromised by environmental changes during use or storage.
• Maintaining enzyme activity under stress conditions like high temperature or prolonged storage is essential.

Purpose of the Study:

• To stabilize and protect enzymes by coencapsulating them with trehalose into polymersomes.
• To evaluate the preservation of enzyme activity in desiccated and heated nanoreactors.
• To demonstrate the catalytic application of these stabilized enzyme nanoreactors.

Main Methods:

• Coencapsulation of enzymes (laccase) and trehalose into polymersomes to create nanoreactors.
• Assessment of enzyme activity after desiccation for 2 months at room temperature.
• Evaluation of enzyme activity after heating at 50 °C for 3 weeks.
• Testing the catalytic efficiency for bleaching textile dyes (orange G, toluidine blue O, indigo).

Main Results:

• Trehalose coencapsulation preserved up to 81% of the enzyme's original activity after 2 months of desiccation.
• Approximately 75% of enzyme activity was retained when nanoreactors were heated at 50 °C for 3 weeks.
• Laccase/trehalose-loaded nanoreactors effectively catalyzed the bleaching of textile dyes.

Conclusions:

• Coencapsulating trehalose within polymersomes is advantageous for stabilizing enzymes in a dehydrated state.
• This approach effectively preserves enzyme activity during extended storage and elevated temperatures.
• The developed nanoreactors show practical applicability as catalysts in industrial processes like textile dyeing.