Trends in Biosensors and Role of Enzymes as Their Sensing Element for Healthcare Applications

Adhikary, Tathagata; Nanda, Amalesh; Thangapandi, K.; Roy, Shantonu; Jana, Saikat Kumar

doi:10.1201/9780429061257-10

Cited by 2 publications

(1 citation statement)

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“…However, the efficiency corresponding to such enzyme-devoid biosensors, is not on par with the enzymeimmobilized, nanomaterial-based biosensors [69,70]. Hence, heat-resistant nanomaterials, as nanosized composites, are used recently for protecting the enzymes from the heat, as well as to improve their biosensing efficiency [71]. In the future, the addition of nanocomposites, and thermal resistive DNA nanomaterial combined with enzymes, can be beneficial for improving the efficiency of biosensors [72].…”

Section: Future Perspectivesmentioning

confidence: 99%

Enzyme Immobilized Nanoparticles Towards Biosensor Fabrication

Jeevanandam

2022

Nanomaterial-Supported Enzymes

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In recent times, nanomaterials with semiconductor properties are introduced as a potential transducer in biosensors, which can be credited to their intrinsic, elevated surface-to-volume proportion, enhanced sensitivity, and improved surface properties. The surface properties of nanomaterials have made them a significant transducer matrix towards the immobilization of bioreceptors, which eventually enhances the identification threshold and the biosensor sensing capability. Several nanomaterials, such as polymer, metal oxide, metal and carbon-based, as well as nanocomposites, are used towards transducer manufacturing, eventually being incorporated in the biosensors. The current chapter lays an outline with respect to biosensors that are fabricated with nanomaterials as a transducer, where enzymes acting as a bioreceptor, are immobilized on their surface. In addition, the biosensing mechanisms of the enzyme immobilized nanomaterials, their efficiency, detection limit, and sensitivity, are also discussed.

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Section: Future Perspectivesmentioning

confidence: 99%

Enzyme Immobilized Nanoparticles Towards Biosensor Fabrication

Jeevanandam

2022

Nanomaterial-Supported Enzymes

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Zwitterionic poly(carboxybetaine) microgels for enzyme (chymotrypsin) covalent immobilization with extended stability and activity

Erfani

Zarrintaj

Seaberg

et al. 2021

J of Applied Polymer Sci

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There is emerging evidence that biocompatible zwitterionic materials can prevent nonspecific interactions within protein systems and increase protein stability. Here, a zwitterionic microgel was synthesized from poly (carboxybetaine methyl methacrylate) (pCB) using an inverse emulsion, free radical polymerization reaction technique. The microgel was loaded with a model enzyme, α‐chymotrypsin (ChT), using a post‐fabrication loading technique. A reaction scheme was developed and studied for covalent immobilization of ChT within the microgel. Confocal laser microscopy studies showed that immobilized ChT (i‐ChT) was distributed within the hydrogel. The enzyme‐immobilized microgels showed excellent reusability (72% of its initial activity after 10 uses) and could undergo several freezing/drying/rehydration cycles while retaining enzymatic activity. The i‐ChT activity, half‐life, and conformational stability were studied at varying pH and temperatures with results compared to free ChT in buffer. ChT immobilized within pCB hydrogel showed increased enzymatic stability as observed by a 13°C increase in the temperature at which i‐ChT loses activity compared to free ChT. Furthermore, enzyme half‐life increased up to seven‐fold for the pCB immobilized ChT, and the increased stability resulted in higher activity at elevated pH. The i‐ChT was most active at pH of 8.5 and was partially active up to the pH of 10.2.

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Trends in Biosensors and Role of Enzymes as Their Sensing Element for Healthcare Applications

Cited by 2 publications

References 1 publication

Enzyme Immobilized Nanoparticles Towards Biosensor Fabrication

Enzyme Immobilized Nanoparticles Towards Biosensor Fabrication

Zwitterionic poly(carboxybetaine) microgels for enzyme (chymotrypsin) covalent immobilization with extended stability and activity

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