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.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsSpringer Nature is developing a new tool to find and evaluate Protocols. Learn more
References
Walde, P. and Ichikawa, S. (2001) Enzymes inside lipid vesicle: preparation, reactivity and applications. Biomol. Eng. 18, 143–177.
Walde, P., Ichikawa, S., and Yoshimoto, M. (2009) The fabrication and applications of enzyme-containing vesicles (Chapter 7). In Ariga, K. and Nalwa, H. S. (Eds.) Bottom-Up Nanofabrication. American Scientific Publishers: Stevenson Ranch, CA, Vol. 2, pp. 199–222.
Treyer, M., Walde, P., and Oberholzer, T. (2002) Permeability enhancement of lipid vesicles to nucleotides by use of sodium cholate: basic studies and application to an enzyme-catalyzed reaction occurring inside the vesicles. Langmuir 18, 1043–1050.
Yoshimoto, M., Wang, S., Fukunaga, K., Treyer, M., Walde, P., Kuboi, R., and Nakao, K. (2004) Enhancement of apparent substrate selectivity of proteinase K encapsulated in liposomes through a cholate-induced alterations of the bilayer permeability. Biotechnol. Bioeng. 85, 222–233.
Yoshimoto, M., Sakamoto, H., Yoshimoto, N., Kuboi, R., and Nakao, K. (2007) Stabilization of quaternary structure and activity of bovine liver catalase through encapsulation in liposomes. Enzyme Microb. Technol. 41, 849–858.
Yoshimoto, M., Sato, M., Yoshimoto, N., and Nakao, K. (2008) Liposomal encapsulation of yeast alcohol dehydrogenase with cofactor for stabilization of the enzyme structure and activity. Biotechnol. Prog. 24, 576–582.
Yoshimoto, M., Miyazaki, Y., Sato, M., Fukunaga, K., Kuboi, R., and Nakao, K. (2004) Mechanism for high stability of liposomal glucose oxidase to inhibitor hydrogen peroxide produced in prolonged glucose oxidation. Bioconjugate Chem. 15, 1055–1061.
Wang, S., Yoshimoto, M., Fukunaga, K., and Nakao, K. (2003) Optimal covalent immobilization of glucose oxidase-contaiing liposomes for highly stable biocatalyst in bioreactor. Biotechnol. Bioeng. 83, 444–453.
Yoshimoto, M., Miyazaki, Y., Kudo, Y., Fukunaga, K., and Nakao, K. (2006) Glucose oxidation catalyzed by liposomal glucose oxidase in the presence of catalase-containing liposomes. Biotechnol. Prog. 22, 704–709.
Yoshimoto, M., Wang, S., Fukunaga, K., Fournier, D., Walde, P., Kuboi, R., and Nakao, K. (2005) Novel immobilized liposomal glucose oxidase system using the channel protein OmpF and catalase. Biotechnol. Bioeng. 90, 231–238.
Kuboi, R., Yoshimoto, M., Walde, P., and Luisi, P. L. (1997) Refolding of carbonic anhydrase assisted by 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine liposomes. Biotechnol. Prog. 13, 828–836.
Walde, P. (2004) Preparation of vesicles (liposomes). In Nalwa, H. S. (Ed.) Encyclopedia of Nanoscience and Nanotechnology. American Scientific Publishers: Los Angeles, Vol. 9, pp. 43–79.
MacDonald, R. C., MacDonald, R. I., Menco, B. P., Takeshita, K., Subbarao, N. K., and Hu, L.-R. (1991) Small-volume extrusion apparatus for preparation of large, unilamellar vesicles. Biochim. Biophys. Acta 1061, 297–303.
Yoshimoto, M., Monden, M., Jiang, Z., and Nakao. K. (2007) Permeabilization of phospholipid bilayer membranes induced by gas–liquid flow in an airlift bubble column. Biotechnol. Prog. 23, 1321–1326.
Dorovska-Taran, V., Wick, R., and Walde, P. (1996) A 1H nuclear magnetic resonance method for investigating the phospholipase D-catalyzed hydrolysis of phosphatidylcholine in liposomes. Anal. Biochem. 240, 37–47.
Yoshimoto, M., Walde, P., Umakoshi, H., and Kuboi, R. (1999) Conformationally changed cytochrome c-induced fusion of enzyme- and substrate-containing liposomes. Biotechnol. Prog. 15, 689–696.
Acknowledgment
The author would like to thank Prof. Emeritus Katsumi Nakao (Yamaguchi Univ.) for his advice on biochemical engineering applications of enzyme-containing liposomes. This work was supported in part by the Japan Society of the Promotion of Science (no. 21760642).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2011 Springer Science+Business Media, LLC
About this protocol
Cite this protocol
Yoshimoto, M. (2011). Stabilization of Enzymes Through Encapsulation in Liposomes. In: Minteer, S. (eds) Enzyme Stabilization and Immobilization. Methods in Molecular Biology, vol 679. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-60761-895-9_2
Download citation
DOI: https://doi.org/10.1007/978-1-60761-895-9_2
Published:
Publisher Name: Humana Press, Totowa, NJ
Print ISBN: 978-1-60761-894-2
Online ISBN: 978-1-60761-895-9
eBook Packages: Springer Protocols