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Substrate‐permeable encapsulation of enzymes maintains effective activity, stabilizes against denaturation, and protects against proteolytic degradation
Author(s) -
Nasseau Mathieu,
Boublik Yvan,
Meier Wolfgang,
Winterhalter Mathias,
Fournier Didier
Publication year - 2001
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.10074
Subject(s) - denaturation (fissile materials) , proteases , proteolysis , chemistry , liposome , enzyme , porin , biophysics , proteolytic enzymes , biochemistry , lipid bilayer , escherichia coli , membrane , bacterial outer membrane , biology , gene , nuclear chemistry
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: 615–618, 2001.