title: Stabilization of enzymes through encapsulation in liposomes.
abstract: Phospholipid vesicle (liposome) offers an aqueous compartment surrounded by lipid bilayer membranes. Various enzyme molecules were reported to be encapsulated in liposomes. The liposomal enzyme shows peculiar catalytic activity and selectivity to the substrate in the bulk liquid, which are predominantly derived from the substrate permeation resistance through the membrane. We reported that the quaternary structure of bovine liver catalase and alcohol dehydrogenase was stabilized in liposomes through their interaction with lipid membranes. The method and condition for preparing the enzyme-containing liposomes with well-defined size, lipid composition, and enzyme content are of particular importance, because these properties dominate the catalytic performance and stability of the liposomal enzymes.
authors.affiliation: Department of Applied Molecular Bioscience, Yamaguchi University, Ube, Japan.
authors.forename: Makoto
authors.initials: M
authors.lastname: Yoshimoto
mesh_terms: D000426:Alcohol Dehydrogenase / Q000737:chemistry*; D000818:Animals; D057005:Bioengineering; D002374:Catalase / Q000737:chemistry*; D002384:Catalysis; D002417:Cattle; D004795:Enzyme Stability; D008051:Lipid Bilayers / Q000737:chemistry*; D008081:Liposomes / Q000737:chemistry*; D020836:Protein Structure, Quaternary; D013379:Substrate Specificity; D013997:Time Factors
chemical_list: D008051:Lipid Bilayers; D008081:Liposomes; D000426:Alcohol Dehydrogenase; D002374:Catalase