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首页> 外文期刊>Electroanalysis >Nonfaradaic impedance probing of potato glycoalkaloids interaction with butyrylcholinesterase immobilized onto gold electrode
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Nonfaradaic impedance probing of potato glycoalkaloids interaction with butyrylcholinesterase immobilized onto gold electrode

机译：非法拉第阻抗探测马铃薯生物碱与固定在金电极上的丁酰胆碱酯酶的相互作用

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摘要

In this paper, we report the development of enzyme-based nonfaradaic impedimetric biosensor for direct detection of potato glycoalkaloids alpha-chaconine and alpha-solanine. The sensors were prepared by cross-linking of horse butyrylcholinesterase (BuChE) onto gold electrodes. Affinity interaction of both glycoalkaloids with immobilized BuChE caused an essential decrease of the total impedance and of the interfacial polarization resistance as well. No effect was observed after alpha-chaconine contact with bovine serum albumin and bacterial carboxylesterase immobilized onto gold. BuChE-modified electrodes were more sensitive to alpha-chaconine, and found I-50 values were in quite good agreement with those measured by biocatalytic ISFET-based sensors.
机译：在本文中，我们报告了基于酶的非法拉第阻抗生物传感器的发展，该传感器可直接检测马铃薯的生物碱α-查茄碱和α-茄碱。通过将马丁酰胆碱酯酶（BuChE）交联到金电极上来制备传感器。两种糖类生物碱与固定化的BuChE的亲和力相互作用都导致总阻抗和界面极化电阻的显着降低。 α-查茄碱与牛血清白蛋白和固定在金上的细菌羧酸酯酶接触后未观察到作用。 BuChE修饰的电极对α-查茄碱更敏感，发现I-50值与基于生物催化ISFET的传感器测得的I-50值非常吻合。

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