Stabilizing enzymes within polymersomes by coencapsulation of trehalose
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Publication date
22.06.2020
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01A - Journal article
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Parent work
Biomacromolecules
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Volume
22
Issue / Number
1
Pages / Duration
134-145
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American Chemical Society
Place of publication / Event location
Washington
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Abstract
Enzymes are essential biocatalysts and very attractive as therapeutics. However, their functionality is strictly related to their stability, which is significantly affected by the environmental changes occurring during their usage or long-term storage. Therefore, maintaining the activity of enzymes is essential when they are exposed to high temperature during usage or when they are stored for extended periods of time. Here, we stabilize and protect enzymes by coencapsulating them with trehalose into polymersomes. The anhydrobiotic disaccharide preserved up to about 81% of the enzyme’s original activity when laccase/trehalose-loaded nanoreactors were kept desiccated for 2 months at room temperature and 75% of its activity when heated at 50 °C for 3 weeks. Moreover, the applicability of laccase/trehalose-loaded nanoreactors as catalysts for bleaching of the textile dyes orange G, toluidine blue O, and indigo was proven. Our results demonstrate the advantages of coencapsulating trehalose within polymersomes to stabilize enzymes in dehydrated state for extended periods of time, preserving their activity even when heated to elevated temperature.
Keywords
enzymes, polymersomes, trehalose
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1525-7797
1526-4602
1526-4602
Language
English
Created during FHNW affiliation
Yes
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Published
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Peer review of the complete publication
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Citation
Saxer, S., Pieles, U., Dinu, M. V., Dinu, I. A., Meier, W., Bruns, N., & Bruns, N. (2020). Stabilizing enzymes within polymersomes by coencapsulation of trehalose. Biomacromolecules, 22(1), 134–145. https://doi.org/10.1021/acs.biomac.0c00824