![]() Precision wasĪlso satisfactory (relative standard deviation, % RSD < 6). Good linearity over the range 0.06–10 μM. Sensitive, and selective with a detection limit of 0.02 μM and For bothĪnalyses, the results indicated that the biosensor is cost-effective, Medium and for evaluating the delivery of H 2O 2 from denture cleaner tablets, as examples of application. To determine H 2O 2 liberated by cells in a culture The performance of the proposed biosensor has been demonstrated Luminol as an oxidizable substrate, with HRP as the catalyst, hasīeen used in order to quantify H 2O 2 as the oxidizingĪgent. The chemiluminescent reaction based on the use of (PDMS) support to quantify in situ hydrogen peroxide (H 2O 2). Immobilization of the horseradish peroxidase (HRP) enzyme on a polydimethylsiloxane The strength of this biosensing system is the simplicity, portability, and reusability of the devices it can be applied up to 60 times with 90% of its activity maintained.Ī chemiluminescent biosensor based on the covalent Precision was also satisfactory (relative standard deviation, % RSD < 6). For both analyses, the results indicated that the biosensor is cost-effective, sensitive, and selective with a detection limit of 0.02 μM and good linearity over the range 0.06-10 μM. The performance of the proposed biosensor has been demonstrated to determine H2O2 liberated by cells in a culture medium and for evaluating the delivery of H2O2 from denture cleaner tablets, as examples of application. The chemiluminescent reaction based on the use of luminol as an oxidizable substrate, with HRP as the catalyst, has been used in order to quantify H2O2 as the oxidizing agent. Herein, we reported a chemiluminescent biosensor based on the covalent immobilization of the horseradish peroxidase (HRP) enzyme on a polydimethylsiloxane (PDMS) support to quantify in situ hydrogen peroxide (H2O2).
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