This paper presents a previously unexplored biosensing strategy for detecting gliadin which exploits the crosslinking of gliadin with collagen, catalyzed by transglutaminase at the interfacial electron transfer rate, on a modified electrode. The process is monitored by electrochemical impedance spectroscopy using a glassy carbon electrode coated with a collagen layer. To validate the specificity of the response as well as to eliminate possible interferences from other proteins, such as soy protein or casein, the captured gliadin is further reacted with a specific anti-gliadin antibody. Changes in charge transfer resistance, measured from the Nyquist plots, scale linearly with the gliadin concentration in the range 5–20 mg/L, a range suitable for testing the gliadin concentration in gluten-free food commodities.

本文提出了一种用于检测麦醇溶蛋白的先前未曾探索过的生物传感策略，该方法利用了谷氨酰胺与胶原的交联反应，该蛋白在修饰的电极上被谷氨酰胺转移酶以界面电子转移速率催化。使用涂有胶原蛋白层的玻璃碳电极通过电化学阻抗光谱法监测该过程。为了验证反应的特异性以及消除其他蛋白（例如大豆蛋白或酪蛋白）的可能干扰，将捕获的麦醇溶蛋白进一步与特定的抗麦醇溶蛋白抗体反应。从耐奎斯特图中测得的电荷转移阻力变化随麦醇溶蛋白浓度在5-20 mg / L的范围内线性变化，该范围适用于测试无麸质食品中麦醇溶蛋白的浓度。