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Substrate-permeable encapsulation of enzymes maintains effective activity, stabilizes against denaturation, and protects against proteolytic degradation

Nasseau, Mathieu and Boublik, Yvan and Meier, Wolfgang and Winterhalter, Mathias and Fournier, Didier. (2001) Substrate-permeable encapsulation of enzymes maintains effective activity, stabilizes against denaturation, and protects against proteolytic degradation. Biotechnology and Bioengineering, 75 (5). pp. 615-618.

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Official URL: https://edoc.unibas.ch/72392/

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Abstract

How can enzymes be protected against denaturation and proteolysis while keeping them in a fully functional state? One solution is to encapsulate the enzymes into liposomes, which enhances their stability against denaturation and proteases. However, the permeability barrier of the lipid membrane drastically reduces the activity of enzyme entrapped in the liposome by reducing the internal concentration of the substrate. To overcome this problem, we permeabilized the wall of the liposome by reconstitution of a porin from Escherichia coli. In this way, we recovered the full functionality of the enzyme while retaining the protection against denaturation and proteolytic enzymes. © 2001 John Wiley & Sons, Inc. Biotechnol Bioeng 75: 615âEuro"618, 2001.
Faculties and Departments:05 Faculty of Science > Departement Chemie
05 Faculty of Science > Departement Chemie > Chemie > Makromolekulare Chemie (Meier)
UniBasel Contributors:Meier, Wolfgang P.
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Wiley
ISSN:0006-3592
e-ISSN:1097-0290
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:23 Mar 2020 16:33
Deposited On:23 Mar 2020 16:21

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