Abstract
The lipase VII (from Candida rugosa) activity was studied as a function of the content of pentanol and water in cethyltrimethylammonium bromide (CTAB)/water/pentanol/hexane reverse micelles. The turn-over numbers for the hydrolysis of p-nitrophenyl butyrate (p-NPB) were determined spectrophotometrically. Reverse micelles size and the partition of p-NPB between the aggregates and the oil continuous phase were determined by means of pulsed gradient spin-echo NMR experiments. A strong correlation between enzyme activity and micellar size was found.
Acknowledgements The financial support of Italian Ministry for University and Scientific and Technological Research (MURST), grant PRIN/1998 is acknowledged.
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Lopez, F., Palazzo, G., Colafemmina, G., Cinelli, G., Ambrosone, L., Ceglie, A. Enzymatic activity of lipase entrapped in CTAB/water/pentanol/hexane reverse micelles: a functional and microstructural investigation. In: Miguel, M., Burrows, H. (eds) Trends in Colloid and Interface Science XVI. Progress in Colloid and Polymer Science, vol 123. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-36462-7_39
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DOI: https://doi.org/10.1007/978-3-540-36462-7_39
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