Temperature window for encapsulation of an enzyme into thermally shrunk, CaCO 3 templated polyelectrolyte multilayer capsules

Van der Meeren, L, Li, J, Konrad, M, Skirtach, AG, Volodkin, D ORCID: https://orcid.org/0000-0001-7474-5329 and Parakhonskiy, BV, 2020. Temperature window for encapsulation of an enzyme into thermally shrunk, CaCO 3 templated polyelectrolyte multilayer capsules. Macromolecular Bioscience, 20 (7): 2000081. ISSN 1616-5187

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Abstract

Encapsulation of enzymes allows to preserve their biological activities in various environmental conditions, such as exposure to elevated temperature or to proteases. This is particularly relevant for in vivo applications, where proteases represent a severe obstacle to maintaining the activity of enzymes. Polyelectrolyte multilayer capsules are suitable for enzyme encapsulation, where CaCO3 particles and temperature‐dependent capsule formation are the best templates and the most adequate method, respectively. In this work, these two areas are combined and, ALP (alkaline phosphatase), which is a robust and therapeutically relevant enzyme, is encapsulated into thermally shrunk polyelectrolyte multilayer (PDADMAC/PSS)4 capsules templated on calcium carbonate particles (original average diameter: ≈3.5 µm). The activity of the encapsulated enzyme and the optimal temperature range for encapsulation are investigated. The enzymatic activity is almost four times higher upon encapsulation when the temperature range for encapsulation is situated just above the glass transition temperature (40 °C), while its optimal conditions are dictated, on the one hand, by the enzyme activity (better at lower temperatures) and, on the other hand, by the size and mechanical properties of capsules (better at higher temperatures).

Item Type:	Journal article
Publication Title:	Macromolecular Bioscience
Creators:	Van der Meeren, L., Li, J., Konrad, M., Skirtach, A.G., Volodkin, D. and Parakhonskiy, B.V.
Publisher:	Wiley
Date:	20 July 2020
Volume:	20
Number:	7
ISSN:	1616-5187
Identifiers:	Number Type 10.1002/mabi.202000081 DOI 1347120 Other
Divisions:	Schools > School of Science and Technology
Record created by:	Jill Tomkinson
Date Added:	03 Aug 2020 09:51
Last Modified:	02 Jun 2021 03:00
URI:	https://irep.ntu.ac.uk/id/eprint/40300

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