Single-enzyme kinetics of CALB-catalyzed hydrolysis

Kelly Velonia*, Ophir Flomenbom, Davey Loos, Sadahiro Masuo, Mircea Cotlet, Yves Engelborghs, Johan Hofkens, Alan E. Rowan, Joseph Klafter, Roeland J.M. Nolte, Frans C. De Schryver

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Real-time measurement of the catalysis and substrate kinetics of a single-enzyme hydrolysis reaction is demonstrated with confocal fluorescence microscopy (CFM; see picture, green = CFM beam). A single lipase is shown to have a broad range of conformations; each conformation contributes to the overall enzymatic activity, an observation that is often masked by ensemble measurements.

Original languageEnglish
Pages (from-to)560-564
Number of pages5
JournalAngewandte Chemie - International Edition
Issue number4
StatePublished - 14 Jan 2005


  • Analytical methods
  • Enzymes
  • Fluorescence microscopy
  • Kinetics
  • Single-molecule studies


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