In order to evaluate the effect of ultrasound to chitinase from a molecular level, atomic force microscopy (AFM) was employed to investigate the interaction force of chitinase binding onto chitin surface. In the measurement of force-distance curve, a series of pull-off events were discovered using the immobilized AFM tips with chitinase either treated by ultrasound or not, whereas no interaction peak was observed by the AFM tips without chitinase, indicating that the obtained adhesion forces were coming from the binding functions between chitinase and chitin. Through the analysis of these force curves, at the loading velocity of 0.3 μm/s, the maximum binding force of the chitinase treated by ultrasound for 20 min onto chitin was measured to be 105.33 ± 23.51 pN, while the untreated onto chitin was 71.05 ± 12.73 pN, suggesting the stronger binding force between ultrasonic treated chitinase and chitin substrate. Therefore, AFM has provided a useful method to directly and quantitatively characterize the interactions between chitinase and chitin, and successfully proved that ultrasound could activate chitinase by enhancing the binding ability of chitinase onto chitin.

中文翻译：

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超声增强了几丁质酶与几丁质的结合能力：根据AFM的见解。

为了从分子水平评估超声对几丁质酶的作用，采用原子力显微镜（AFM）研究几丁质酶结合到几丁质表面上的相互作用力。在力-距离曲线的测量中，使用固定化的AFM探针与几丁质酶进行了超声处理或未超声处理，发现了一系列的脱落事件，而没有几丁质酶的AFM探针未观察到相互作用峰，表明获得的粘附力来自几丁质酶和几丁质之间的结合功能。通过这些力曲线的分析，在0.3μm/ s的加载速度下，经超声处理20分钟的几丁质酶对几丁质的最大结合力测得为105.33±23.51 pN，而未处理的几丁质酶为71.05± 12.73 pN，提示超声处理的几丁质酶和几丁质底物之间的结合力更强。因此，原子力显微镜提供了一种直接和定量表征几丁质酶与几丁质之间相互作用的有用方法，并成功地证明了超声可以通过增强几丁质酶与几丁质的结合能力来激活几丁质酶。