| Autor: |
Abdulkareem RA; Department of Life Sciences, University of Bath, Claverton Down, Bath BA2 7AY, UK.; Department of Medical Education, College of Medicine, University of Duhok, 1006 AJ Duhok, Kurdistan Region, Iraq., Doekhie A; Department of Chemistry, University of Bath, Claverton Down, Bath BA2 7AY, UK., Fotaki N; Department of Life Sciences, University of Bath, Claverton Down, Bath BA2 7AY, UK., Koumanov F; Department for Health, Centre for Nutrition, Exercise and Metabolism, University of Bath, Claverton Down, Bath BA2 7AY, UK., Dodson CA; Department of Life Sciences, University of Bath, Claverton Down, Bath BA2 7AY, UK., Sartbaeva A; Department of Chemistry, University of Bath, Claverton Down, Bath BA2 7AY, UK.; Ensilicated Technologies Ltd., Science Creates St. Philips, Albert Road, St. Philips, Bristol BS2 0XJ, UK. |
| Abstrakt: |
Protein therapeutics, vaccines, and other commercial products are often sensitive to environmental factors, such as temperature and long-term storage. In many cases, long-term protein stability is achieved by refrigeration or freezing. One alternative is the encapsulation of the protein cargo within an inert silica matrix (ensilication) and storage or transport at room temperature as a dry powder. In this paper, we test the effect of three commonly used biological buffers on the ensilication, storage, and desilication of the enzyme lysozyme. We show that ensilication protects lysozyme from heat (100 °C for 1 h) and during storage (18 months at room temperature). The choice of ensilication buffer has little effect on the activity of lysozyme after desilication. Our results provide confidence in the continued pursuit of ensilication as a methodology for protein stabilisation and in its compatibility with biological buffers. |
