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Intrinsic peroxidase-like clay mineral nanozyme-triggered cascade bioplatform with enhanced catalytic performance
Abstract Recently, the combination of nature enzymes and nanozymes provides new opportunities for constructing new generation of high-performance enzymatic cascade system. Herein, an enzyme cascade bioplatform (GOx-BSA/NAu-2) has been constructed by combining clay mineral nanozymes (nontronite, NAu-2) and natural enzyme (glucose oxidase, GOx). NAu-2 can be used both as a carrier for GOx immobilization and as a mimic of peroxidase (POD) guiding an enzyme cascade bioplatform. Owing to the stabilizing effect of bovine serum albumin (BSA) on enzymes and proper immobilization method, the GOx-BSA/NAu-2 possess better thermal stability, acid-base stability, storage stability and reusability than free enzymes system. Given the substrate channel effect, the acquired GOx-BSA/NAu-2 exhibits higher catalytic efficiency than the BSA/NAu-2 system and the GOx + HRP system. This work provides an efficient and simple reference for the design of clay mineral nanozyme-enzyme bioplatform, and also broadens the application field of clay minerals.
Graphical abstract In this work, a promising enzyme cascade bioplatform has been prepared based on the natural enzyme integrated clay mineral nanozyme (nontronite), in which nontronite can be used both as a carrier for GOx immobilization and as a mimic of peroxidase (POD) guiding an enzyme cascade bioplatform, which realizing the sensitive detection of glucose. Display Omitted
Highlights Nontronite is confirmed to have intrinsic peroxidase-like activity. An enzyme cascade bioplatform has been constructed by combining nontronite and glucose oxidase. GOx-BSA/NAu-2 possess better operational stability and catalytic activities than free enzymes. GOx-BSA/NAu-2 is used for glucose detection with a LOD of 5.3 μM.
Intrinsic peroxidase-like clay mineral nanozyme-triggered cascade bioplatform with enhanced catalytic performance
Abstract Recently, the combination of nature enzymes and nanozymes provides new opportunities for constructing new generation of high-performance enzymatic cascade system. Herein, an enzyme cascade bioplatform (GOx-BSA/NAu-2) has been constructed by combining clay mineral nanozymes (nontronite, NAu-2) and natural enzyme (glucose oxidase, GOx). NAu-2 can be used both as a carrier for GOx immobilization and as a mimic of peroxidase (POD) guiding an enzyme cascade bioplatform. Owing to the stabilizing effect of bovine serum albumin (BSA) on enzymes and proper immobilization method, the GOx-BSA/NAu-2 possess better thermal stability, acid-base stability, storage stability and reusability than free enzymes system. Given the substrate channel effect, the acquired GOx-BSA/NAu-2 exhibits higher catalytic efficiency than the BSA/NAu-2 system and the GOx + HRP system. This work provides an efficient and simple reference for the design of clay mineral nanozyme-enzyme bioplatform, and also broadens the application field of clay minerals.
Graphical abstract In this work, a promising enzyme cascade bioplatform has been prepared based on the natural enzyme integrated clay mineral nanozyme (nontronite), in which nontronite can be used both as a carrier for GOx immobilization and as a mimic of peroxidase (POD) guiding an enzyme cascade bioplatform, which realizing the sensitive detection of glucose. Display Omitted
Highlights Nontronite is confirmed to have intrinsic peroxidase-like activity. An enzyme cascade bioplatform has been constructed by combining nontronite and glucose oxidase. GOx-BSA/NAu-2 possess better operational stability and catalytic activities than free enzymes. GOx-BSA/NAu-2 is used for glucose detection with a LOD of 5.3 μM.
Intrinsic peroxidase-like clay mineral nanozyme-triggered cascade bioplatform with enhanced catalytic performance
Wang, Ke (author) / Sun, Shiyong (author) / Golubev, Yevgeny Aleksandrovich (author) / Lin, Sen (author) / Liu, Jin (author) / Dong, Faqin (author) / Kotova, Elena Leonidovna (author) / Kotova, Olga Borisovna (author)
Applied Clay Science ; 246
2023-10-28
Article (Journal)
Electronic Resource
English
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