Stabilizing enzymes within polymersomes by co-encapsulation of trehalose
Dinu, Maria Valentina and Dinu, Ionel Adrian and Saxer, Sina Simone and Meier, Wolfgang P. and Pieles, Uwe and Bruns, Nico (2021) Stabilizing enzymes within polymersomes by co-encapsulation of trehalose. Biomacromolecules, 22 (1). pp. 134-145. ISSN 1525-7797 (https://doi.org/10.1021/acs.biomac.0c00824)
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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.
ORCID iDs
Dinu, Maria Valentina, Dinu, Ionel Adrian, Saxer, Sina Simone, Meier, Wolfgang P., Pieles, Uwe and Bruns, Nico ORCID: https://orcid.org/0000-0001-6199-9995;-
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Item type: Article ID code: 74033 Dates: DateEvent11 January 2021Published9 July 2020Published Online22 June 2020AcceptedSubjects: Science > Chemistry Department: Faculty of Science > Pure and Applied Chemistry Depositing user: Pure Administrator Date deposited: 01 Oct 2020 14:51 Last modified: 21 Nov 2024 01:18 Related URLs: URI: https://strathprints.strath.ac.uk/id/eprint/74033