The study of enzymes at the single molecule level offers new insights into the processes underlying enzymatic catalysis. We have immobilized molecules of the lipase CALB in a silica sol-gel matrix and studied the conversion of a profluorescent substrate into a fluorescent product on a single molecule level by confocal laser spectroscopy. It is found that single CALB molecules display �on-off�-behavior, i.e. the enzyme molecule is only active for a limited period of time (milliseconds) and then stops, after which activity is regained. The enzyme furthermore displays a distribution of turnover rates, which are currently being analyzed in detail. 

Single molecule 
study of sol-gel entrapped lipases by 
confocal fluorescence microscopy

239th National Meeting (2010)

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Single molecule study of sol-gel entrapped lipases by confocal fluorescence microscopy