▎ 摘　　要

NOVELTY - Preparing protein molecular imprinted optical and electrochemical sensor involves immersing cleaned bare carbon electrode in an aqueous solution of 3-aminopropyltriethoxysilane, introducing amino groups on the surface of the bare carbon electrode, preparing an aqueous mixture solution comprising formulating protein, sodium alginate, sodium silicate and carboxylated graphene and allowing for defoaming. The aqueous mixture solution is coated on the bare carbon electrode and soaked into the aqueous calcium chloride solution to obtain a solution containing hybrid hydrogel modified electrode. The protein-containing hybrid hydrogel modified electrode is eluted with an eluent to remove the protein, followed by soaking in an aqueous silver nitrate solution to adsorb silver ions and reducing with an aqueous sodium borohydride solution to obtain a surface containing silver molecularly imprinted hybrid hydrogel modified electrode that identifies proteins of nanoparticles. USE - Method for preparing molecular imprinting optical and electrochemical sensor for detecting and identifying proteins such as bovine serum albumin, ovalbumin, catalase and lysozyme by surface-enhanced Raman spectroscopy. ADVANTAGE - The method enables to prepare protein molecular imprinting optical and electrochemical sensor with rapid detection limit, improved selectivity, sensitivity, reliability and detection efficiency, good biocompatibility and good application prospect in the protein analysis and detection field, without using toxic or harmful reagents, reducing the change of the protein conformation by polymerization heat, and providing mild eluting protein. DETAILED DESCRIPTION - Preparing protein molecular imprinted optical and electrochemical sensor involves immersing cleaned bare carbon electrode in an aqueous solution of 0.01-2 pts. wt. 3-aminopropyltriethoxysilane for 2-24 hours, introducing amino groups on the surface of the bare carbon electrode, preparing an aqueous mixture solution comprising 0.01-5 wt.% formulating protein, 0.1-5 wt.% sodium alginate, 0.01-2 wt.% sodium silicate and 0.01-10 wt.% carboxylated graphene, allowing for defoaming and placing in a sterile container. A calcium chloride aqueous solution containing 0.1-10 wt.% calcium chloride is prepared. The aqueous mixture solution is uniformly coated on the bare carbon electrode such that the interaction between amino groups on the surface of the bare carbon electrode and sodium alginate and carboxyl groups on carboxylated graphene makes sodium alginate molecules and carboxylated graphene on the surface of the bare carbon electrode. The coated bare carbon electrode is soaked into the aqueous calcium chloride solution for 0.5-24 hours to obtain a solution containing hybrid hydrogel modified electrode, where the calcium chloride cross-links sodium silicate to generate uniformly dispersed calcium silicate nanoparticles in the hybrid hydrogel. The protein-containing hybrid hydrogel modified electrode is eluted with an eluent to remove the protein, soaked in an aqueous silver nitrate solution to adsorb silver ions, and reduced with an aqueous sodium borohydride solution to obtain a surface containing silver molecularly imprinted hybrid hydrogel modified electrode that identifies proteins of nanoparticles. The modified electrode is used as the working electrode, the silver electrode is used as the reference electrode, and the platinum sheet is used as auxiliary electrode. The electrodes are assembled into an electrochemical sensor to rapidly detect and identify proteins. The probe of the Raman spectrometer is combined with the molecularly imprinted hybrid hydrogel modified electrode to quickly detect and identify proteins. The molecularly imprinted hybrid hydrogel modified electrode is placed in an aqueous solution of protein to adsorb the protein and taken out. The adsorbed protein is detected by a Raman spectrometer. The silver nanoparticles in the gel are used as the active hot spot of the enhanced substrate, which greatly improves the detection sensitivity of the protein.