Abstract
The possibility of using a microemulsion system based on the natural surfactant lecithin for enzymic studies was examined. Trypsin was solubilized in water-in-oil microemulsions of lecithin in isooctane and tested for activity. The enzyme activity was found higher in the microemulsion than in an aqueous solution. The “superactive” behavior was attributed to high local concentrations of the substrate, induced by the presence of the surfactant. Luminescence quenching measurements using Ru(biPy) 2+3 as a lumophore and Fe(CN) 3−6 as a quencher showed that the system is compartmentalized and that the microemulsion is percolating. The presence of trypsin influences the dispersed microenvironment by further restricting it, whereas by increasing the water content the interphase composition is altered.
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© 1996 Dr. Dietrich Steinkopff Verlag GmbH & Co. KG
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Avramiotis, S., Xenakis, A., Lianos, P. (1996). Lecithin W/O microemulsions as a host for trypsin. Enzyme activity and luminescence decay studies. In: Solans, C., Infante, M.R., García-Celma, M.J. (eds) Trends in Colloid and Interface Science X. Progress in Colloid & Polymer Science, vol 100. Steinkopff. https://doi.org/10.1007/BFb0115795
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DOI: https://doi.org/10.1007/BFb0115795
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