Abstract
ABSTRACTIn this work, a new approach for enzyme activity monitoring is suggested. It is based on the real-time imaging, by atomic force microscopy (AFM) and magnetic force microscopy (MFM), of the degradation of a nanoparticles-loaded enzyme responsive layer, namely Fe3O4-nanoparticles-loaded gelatin. The roughness analysis allowed the quantification of the trypsin-induced ferrogel degradation and the correlation of the AFM and MFM data obtained.
Highlights
Nowadays, the atomic force microscopy, developed in the mid-1980s [1], is recognized as one of the most important tools for imaging, measuring, analyzing and manipulating matter at the nanometer scale
The principal impetus for the characterization of the ferrogel surface was to demonstrate the possible correlation between surface degradation and trypsin activity
The topological changes were attributed to the strong interaction between the enzyme and its substrate and the rapid dissolution of the obtained products. Such a degradation model was suggested in our previous works to explain the increase of the frequency response of the quartz crystal microbalance (QCM)-based sensors for enzyme activity evaluation [23,24]
Summary
The atomic force microscopy, developed in the mid-1980s [1], is recognized as one of the most important tools for imaging, measuring, analyzing and manipulating matter at the nanometer scale. It is noteworthy to highlight that the ability of the atomic force microscopy to be used in liquid media and to image non-conductive surfaces makes it suitable for biological samples characterisation. The technique has been applied for enzyme–substrate interactions studies and characterization of immobilized enzyme molecules on biosensor surfaces [8,9,10,11], but only a few papers comment on the atomic force microscopy application to enzyme activity exploration. Radmacher et al [12] report direct observations of enzyme activity based on the detection of the height fluctuations of the cantilever. Other enzyme activity and kinetics studies are based on the detection of the molecular byproducts during enzymatic conversion [19,20]. AFM enables several research options [21,22], its capability for enzyme activity imaging remains not completely exploited
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