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

被引:58
作者
Nasseau, M
Boublik, Y
Meier, W
Winterhalter, M
Fournier, D
机构
[1] Univ Toulouse 3, UMR CNRS 5068, Grp Biochim Prot, Lab Synth & Physicochim Mol Interet Biol, F-31062 Toulouse, France
[2] CNRS, Inst Pharmacol & Biol Struct, Toulouse, France
[3] Univ Basel, Dept Phys Chem, Basel, Switzerland
关键词
stabilization; enzyme; liposome; protease; denaturation;
D O I
10.1002/bit.10074
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
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. (C) 2001 John Wiley & Sons, Inc.
引用
收藏
页码:615 / 618
页数:4
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