Enzymatic activity of lipase entrapped in CTAB/water/pentanol/hexane reverse micelles: a functional and microstructural investigation

摘要

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.