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

Biotechnology and Bioengineering

Volumn 75, Issue 5, 2001, Pages 615-618

  Nasseau, Mathieu ^a,b   Boublik, Yvan ^a   Meier, Wolfgang ^c   Winterhalter, Mathias ^b   Fournier, Didier ^a  

^a UNIVERSITÉ DE TOULOUSE   (France)

^b INSTITUT DE PHARMACOLOGIE ET DE BIOLOGIE STRUCTURALE   (France)

^c UNIVERSITY OF BASEL   (Switzerland)

Author keywords

Denaturation; Enzyme; Liposome; Protease; Stabilization

Indexed keywords

BIODEGRADATION; CELL MEMBRANES; ENCAPSULATION; LIPIDS;

DENATURATION;

ENZYMES;

LIPOSOME; PORIN; PROTEINASE;

ARTICLE; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME RECONSTITUTION; ENZYME STABILITY; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; LIPID MEMBRANE; NONHUMAN; PERMEABILITY; PROTECTION; PROTEIN DEGRADATION;

ACETYLCHOLINESTERASE; ACETYLTHIOCHOLINE; BIOTECHNOLOGY; CAPSULES; ENZYME STABILITY; LIPOSOMES; PEPTIDE HYDROLASES; PERMEABILITY; PORINS; PROTEIN DENATURATION; RESTRAINT, PHYSICAL;

ESCHERICHIA COLI;

EID: 0035814370     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.10074     Document Type: Article

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14. Understanding the function of bacterial outer membrane channels by reconstituting into black lipid membranes
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