Chemically glycosylation improves the stability of an amperometric horseradish peroxidase biosensor.

摘要: We constructed a biosensor by electrodeposition of gold nano-particles (AuNPs) on glassy carbon (GC) and subsequent formation 4-mercaptobenzoic acid self-assembled monolayer (SAM). The enzyme horseradish peroxidase (HRP) was then covalently immobilized onto the SAM. Two forms HRP were employed: non-modified chemically glycosylated with lactose. Circular dichroism (CD) spectra showed that chemical glycosylation did neither change tertiary structure nor heme environment. highest sensitivity to hydroquinone obtained for HRP-lactose (414 nA μM(-1)) compared 378 μM(-1) one employing HRP. form catalyzed reduction more rapidly than native enzyme. sensor lactose-modified also had lower limit detection (74 μM) (83 μM). However, most importantly, improved long-term stability biosensor, which retained 60% its activity over four-month storage period only 10% These results highlight improvements an innovative stabilization method when previously reported enzyme-based biosensors.