Enzymatic activity regulated by a surfactant and hydroxypropyl β-cyclodextrin
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Updated: May 8, 2026

Single Liposome Measurements for the Study of Proton-Pumping Membrane Enzymes Using Electrochemistry and Fluorescent Microscopy
Published on: February 21, 2019
Qingzhong Li1, Tao Zhai, Kun Du
1Beijing Key Lab of Bioprocess, Department of Biochemical Engineering, Beijing University of Chemical Technology, Beijing, China.
Abstract:
Circular dichroism spectra reveal that sodium dodecyl benzene sulfonate (SDBS) at low concentrations can effectively prevent the aggregation of lysozyme molecules, while SDBS at high concentrations can lead to conformational and structural change of the protein. SDBS is able to inhibit the enzymatic activity of lysozyme in a highly efficient dose-dependent manner. The interaction mechanism of SDBS with lysozyme has been investigated by measuring optical spectra. Based on fluorescence and UV-vis spectra, microenvironmental change in and around the active site region induced by SDBS has been revealed and explained. Two-dimensional FTIR spectra have been analyzed to identify the secondary structures and residues of lysozyme, which have a preferential interaction with SDBS. Hydroxypropyl β-cyclodextrin (HP-β-CD) was used to detach SDBS from the inactivated enzyme, and complete recovery of enzymatic activity was achieved. Thus, the enzymatic activity of lysozyme can be regulated by SDBS and HP-β-CD.
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