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Thermal Stabilisation of Lysozyme through Ensilication
Reveng A Abdulkareem1,2, Aswin Doekhie3, Nikoletta Fotaki1
1Department of Life Sciences, University of Bath, Claverton Down, Bath BA2 7AY, UK.
Molecules (Basel, Switzerland)
|September 14, 2024
Summary
Ensilication, a method of encapsulating proteins in silica, effectively stabilizes enzymes like lysozyme at room temperature for 18 months. The choice of biological buffer during ensilication did not impact the enzyme's activity post-release.
Area of Science:
- Biochemistry
- Materials Science
- Protein Stabilization
Background:
- Protein therapeutics and vaccines require stable storage conditions, often relying on refrigeration or freezing.
- Ensiling offers a promising alternative for room-temperature protein stabilization via encapsulation in a silica matrix.
Purpose of the Study:
- To evaluate the impact of three common biological buffers on the ensilication process.
- To assess the stability of ensilicated lysozyme under heat and long-term storage.
- To determine the effect of ensilication buffers on lysozyme activity after desilication.
Main Methods:
- Lysozyme was encapsulated within a silica matrix using three different biological buffers.
- Ensiled lysozyme was subjected to heat treatment (100 °C for 1 hour).
- Long-term storage stability was assessed over 18 months at room temperature.
Main Results:
- Ensiling effectively protected lysozyme from thermal degradation (100 °C for 1 hour).
- Lysozyme retained its activity after 18 months of room-temperature storage in the silica matrix.
- The selection of biological buffer during ensilication showed minimal impact on post-desilication lysozyme activity.
Conclusions:
- Ensiling is a robust method for achieving long-term protein stabilization at room temperature.
- The ensilication process is compatible with commonly used biological buffers.
- This methodology supports the development of stable protein-based products without the need for cold chain storage.

