Temperature behavior of glucose oxidase immobilized into surface-attached stimuli-sensitive copolymer microgel

Sigolaeva, Larisa V.; Efremova, O V; Pergushov, Dmitry V.

doi:10.1016/j.mencom.2023.06.038

Cited by 7 publications

(3 citation statements)

References 29 publications

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“…Then, an enzyme was loaded (via electrostatic immobilization) into the P(NIPAM-co-DMAPMA) microgel at "mild" conditions (typically, ambient temperature and neutral pH), provided that the microgel and the enzyme were oppositely charged. As described in our former publications [20,21,22,23,24,25], maintaining the right ("best") conditions at any stage of fabrication of the microgel-enzyme coatings is very important to provide a large amount of the enzyme at the surface, which is safely immobilized into the adsorbed microgels via the electrostatic binding. Previously, we exploited two-stage sequential adsorption (Figure 2, Way 1) for engineering the microgel-enzyme coatings.…”

Section: Resultsmentioning

confidence: 99%

“…Then, an enzyme was loaded (via electrostatic immobilization) into the P(NIPAM-co-DMAPMA) microgel at "mild" conditions (typically, ambient temperature and neutral pH), provided that the microgel and the enzyme were oppositely charged. As described in our former publications [20][21][22][23][24][25], maintaining the right ("best") conditions at any stage of fabrication of the microgel-enzyme coatings is very important to provide a large amount of the enzyme at the surface, which is safely immobilized into the adsorbed microgels via the electrostatic binding. Another way to fabricate the microgel-enzyme coatings includes at first complex formation between the microgel and the enzyme in solution at the pH values, wherein they are oppositely charged and can form complexes stabilized via the electrostatic interaction, followed by adsorption of the preformed complex (Figure 2, Way 2).…”

Section: Resultsmentioning

confidence: 99%

“…In our previous publications [ 20 , 21 , 22 , 23 , 24 , 25 ], beneficial application of the pH- and temperature-sensitive copolymer microgels based on poly( N -isopropylacrylamide) (PNIPAM) for the efficient modification of gold and graphite (or graphite-based) surfaces and further capacious electrostatic immobilization of a number of enzymes (including multisubunit ones) was demonstrated. In those cases, the electrostatic binding of enzymes by the microgels, which resulted in the build-up of microgel–enzyme coatings, was performed at the interface when the microgels were in the adsorbed state.…”

Section: Introductionmentioning

confidence: 99%

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Adsorption of Preformed Microgel–Enzyme Complexes as a Novel Strategy toward Engineering Microgel-Based Enzymatic Biosensors

Sigolaeva,

Shalybkova,

Sharifullin

et al. 2023

Micromachines

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A novel approach to surface modification, which consists of the adsorption of microgel–enzyme complexes preformed in solution, is highlighted. Accordingly, the microgel–enzyme complexes were formed due to the electrostatic interaction of the oppositely charged interacting components, that is, a cationic poly(N-isopropylacrylamide)-based microgel and glucose oxidase taken as a model enzyme. The spontaneous adsorption of the prepared microgel–enzyme complexes, examined by means of quartz crystal microbalance with dissipation monitoring and atomic force microscopy, was observed, resulting in the formation of well-adhered microgel–enzyme coatings. Further, the preformed microgel–enzyme complexes were adsorbed onto the modified graphite-based screen-printed electrodes, and their enzymatic responses were determined by means of amperometry, demonstrating a remarkable analytical performance toward the quantification of β-D-glucose in terms of high sensitivity (0.0162 A × M−1 × cm−2), a low limit of detection (1 μM), and an expanded linear range (1–2000 μM). The fabricated microgel–enzyme biosensor constructs were found to be very stable against manifold-repeated measurements. Finally, the pH- or salt-induced release of glucose oxidase from the adsorbed preformed microgel–enzyme complexes was demonstrated. The findings obtained for the microgel–enzyme coatings prepared via adsorption of the preformed microgel–enzyme complexes were compared to those found for the microgel–enzyme coatings fabricated via a previously exploited two-stage sequential adsorption, which includes the adsorption of the microgel first, followed by the electrostatic binding of glucose oxidase by the adsorbed microgel.

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Section: Resultsmentioning

confidence: 99%

“…Then, an enzyme was loaded (via electrostatic immobilization) into the P(NIPAM-co-DMAPMA) microgel at "mild" conditions (typically, ambient temperature and neutral pH), provided that the microgel and the enzyme were oppositely charged. As described in our former publications [20][21][22][23][24][25], maintaining the right ("best") conditions at any stage of fabrication of the microgel-enzyme coatings is very important to provide a large amount of the enzyme at the surface, which is safely immobilized into the adsorbed microgels via the electrostatic binding. Another way to fabricate the microgel-enzyme coatings includes at first complex formation between the microgel and the enzyme in solution at the pH values, wherein they are oppositely charged and can form complexes stabilized via the electrostatic interaction, followed by adsorption of the preformed complex (Figure 2, Way 2).…”

Section: Resultsmentioning

confidence: 99%