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Surfactant as modulating agent of enzyme‐loaded liposome activity
Author(s) -
Annesini Maria Cristina,
Braguglia Camilla M.,
Memoli Adriana,
Palermiti Luisa G.,
Di Sario Sabrina
Publication year - 1997
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/(sici)1097-0290(19970720)55:2<261::aid-bit3>3.0.co;2-g
Subject(s) - pulmonary surfactant , liposome , chemistry , enzyme , biophysics , enzyme assay , biochemistry , biology
Large phosphatydilcholine unilamellar vesicles appear to be suitable controlled and protective delivery systems of β‐galactosidase. Kinetic measurements carried out on intact loaded liposomes show that most of the enzyme is entrapped inside the liposomes and its activity is latent. Nevertheless, intact liposomes also show significant activity, which can be controlled by addition of detergent. At sublytic detergent concentrations, liposome enzymatic activity reaches values two or three times greater than those of intact liposomes. This increase seems to be due to membrane structure modification that also enhances the substrate permeability across the bilayer. © 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 55 : 261–266, 1997.

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