Abstract
Small angle x-ray scattering (SAXS) measurements were carried out on w/o microemulsions containing two different enzymatic systems: trypsin or lipase. The results were compared to SAXS measurements in the absence of proteins. When relatively small reverse micelles were used, the presence of enzyme induced a decrease of the aqueous core radius. For larger droplets the presence of the biomolecules did not influence their size.
References
Luisi PL, Magid L (1986) Crit Rev Biochem 20:409
Pileni MP (ed) (1989) Structure and reactivity in reverse micelles. Elsevier, Amsterdam
Stamatis H, Xenakis A, Provelegiou M, Kolisis FN (1993) Biotech Bioeng 42:102–110
Pileni MP, Zemb T, Petit C (1985) Chem Phys Lett 118:414
Sztajer H, Lunsdorf H, Erdmann H, Menge U, Schmid R (1992) Biochim Biophys Acta 1124:253–261
Papadimitriou V, Xenakis A, Evangelopoulos AE (1993) Colloids Surf Biointerfaces 1:295–303
Pitré F, Regnault C, Pileni MP (1993) Langmuir 9:2855
Porod G (1982) In: Glatter O, Kratky O (eds) Small Angle x-ray Scattering, Academic Press New York
Michel F, Pileni MP (1994) Langmuir 10:390
Stamatis H, Xenakis A, Kolisis FN, Malliaris A (1993) Progr Colloid Polym Sci 97:00
Author information
Authors and Affiliations
Editor information
Rights and permissions
Copyright information
© 1994 Dr. Dietrich Steinkopff Verlag GmbH & Co. KG
About this paper
Cite this paper
Papadimitriou, V., Xenakis, A., Petit, C., Pileni, M.P. (1994). Structural modifications of reverse micelles due to enzyme incorporation studied by SAXS. In: Ottewill, R.H., Rennie, A.R. (eds) Trends in Colloid and Interface Science VIII. Progress in Colloid & Polymer Science, vol 97. Steinkopff. https://doi.org/10.1007/BFb0115171
Download citation
DOI: https://doi.org/10.1007/BFb0115171
Received:
Accepted:
Published:
Publisher Name: Steinkopff
Print ISBN: 978-3-7985-0984-9
Online ISBN: 978-3-7985-1673-1
eBook Packages: Springer Book Archive