A biosensor based on the self-entrapment of glucose oxidase within biomimetic silica nanoparticles induced by a fusion enzyme

Choi, Okkyoung; Kim, Byung Chun; An, Ji Hye; Min, Kyoungseon; Kim, Yong Hwan; Um, Youngsoon; Oh, Min Kyu; Sang, Byoung In

doi:10.1016/j.enzmictec.2011.07.005

Cited by 59 publications

(36 citation statements)

References 32 publications

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“…Biosilicification has provided important inspiration for the design of novel biomaterials for tissue engineering [2,11] and biosensors [13]. Silaffin, a peptide implicated in the biogenesis and deposition of silica in diatoms and sea snails, is of interest for the synthesis of materials with specific properties because of its ability to promote silica formation in vitro [14,15].…”

Section: Introductionmentioning

confidence: 99%

“…Silaffin, a peptide implicated in the biogenesis and deposition of silica in diatoms and sea snails, is of interest for the synthesis of materials with specific properties because of its ability to promote silica formation in vitro [14,15]. A short silica-binding peptide (SiBP), R5, which is derived from the silaffin protein of the diatom, Cylindrotheca fusiformis [14], was fused with glucose oxidase [13] and protein polymers [11,16] to precipitate silica in vitro, forming novel materials with different properties. Our previous work described a chimera, consisting of the spider dragline silk polymer and R5, resulting in the precipitation of nanoscale silica particles [11].…”

Section: Introductionmentioning

confidence: 99%

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Control of silicification by genetically engineered fusion proteins: Silk–silica binding peptides

et al. 2015

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In the present study, an artificial spider silk gene, 6mer, derived from the consensus sequence of Nephila clavipes dragline silk gene, was fused with different silica-binding peptides (SiBPs), A1, A3 and R5, to study the impact of the fusion protein sequence chemistry on silica formation and the ability to generate a silk–silica composite in two different bioinspired silicification systems: solution–solution and solution– solid. Condensed silica nanoscale particles (600–800 nm) were formed in the presence of the recombinant silk and chimeras, which were smaller than those formed by 15mer-SiBP chimeras [1], revealing that the molecular weight of the silk domain correlated to the sizes of the condensed silica particles in the solution system. In addition, the chimeras (6mer-A1/A3/R5) produced smaller condensed silica particles than the control (6mer), revealing that the silica particle size formed in the solution system is controlled by the size of protein assemblies in solution. In the solution–solid interface system, silicification reactions were performed on the surface of films fabricated from the recombinant silk proteins and chimeras and then treated to induce β-sheet formation. A higher density of condensed silica formed on the films containing the lowest β-sheet content while the films with the highest β-sheet content precipitated the lowest density of silica, revealing an inverse correlation between the β-sheet secondary structure and the silica content formed on the films. Intriguingly, the 6mer-A3 showed the highest rate of silica condensation but the lowest density of silica deposition on the films, compared with 6mer-A1 and -R5, revealing antagonistic crosstalk between the silk and the SiBP domains in terms of protein assembly. These findings offer a path forward in the tailoring of biopolymer–silica composites for biomaterial related needs.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Control of silicification by genetically engineered fusion proteins: Silk–silica binding peptides

et al. 2015

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“…In many other examples, hydrogen peroxide is a side-product of the target reaction, like in the case of FADH-depending oxidases [51], where the cofactor is regenerated with molecular oxygen producing hydrogen peroxide. The production of hydrogen peroxide by these enzymes has been utilized in many examples as an electrochemical signal in the design of biosensors using oxidases [52,53].…”

mentioning

confidence: 99%

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Hernández

Berenguer-Murcia²,

Rodrigues³

et al. 2012

COC

140

107

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Hydrogen peroxide is a substrate or side-product in many enzyme-catalyzed reactions. For example, it is a side-product of oxidases, resulting from the re-oxidation of FAD with molecular oxygen, and it is a substrate for peroxidases and other enzymes. However, hydrogen peroxide is able to chemically modify the peptide core of the enzymes it interacts with, and also to produce the oxidation of some cofactors and prostetic groups (e.g., the hemo group). Thus, the development of strategies that may permit to increase the stability of enzymes in the presence of this deleterious reagent is an interesting target. This enhancement in enzyme stability has been attempted following almost all available strategies: site-directed mutagenesis (eliminating the most reactive moieties), medium engineering (using stabilizers), immobilization and chemical modification (trying to generate hydrophobic environments surrounding the enzyme, to confer higher rigidity to the protein or to generate oxidation-resistant groups), or the use of systems capable of decomposing hydrogen peroxide under very mild conditions. If hydrogen peroxide is just a side-product, its immediate removal has been reported to be the best solution. In some cases, when hydrogen peroxide is the substrate and its decomposition is not a sensible solution, researchers coupled one enzyme generating hydrogen peroxide "in situ" to the target enzyme resulting in a continuous supply of this reagent at low concentrations thus preventing enzyme inactivation.This review will focus on the general role of hydrogen peroxide in biocatalysis, the main mechanisms of enzyme inactivation produced by this reactive and the different strategies used to prevent enzyme inactivation caused by this "dangerous liaison". Outlook

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“…GOx was self-entrapped by the biosilification and the self-entrapped GOx-R5 was used to immobilize GOx on a graphite electrode for the amperometric glucose biosensor. The sensitivity and the detection limit of the biosensor was 1.58 µA/mM/cm 2 and 0.68 mM (S/N = 3), respectively [39]. In section 2.1.2, SENs were introduced as innovative nanoscaled enzymepolymer conjugates.…”

Section: Biosensormentioning

confidence: 99%

“…Comparing the traditional encapsulation using a sol-gel matrix or mesoporous silica, the biosilification usually displayed improved stability, immobilization efficiency, and loading density. Furthermore, the biosilification can be employed for practical use in bioreactors [34] and bioelectronics [39,40].…”

Section: Self-entrapment Using Silaffinmentioning

confidence: 99%

Recent progress in nanobiocatalysis for enzyme immobilization and its application

Min

Yoo

2014

Biotechnol Bioproc E

Self Cite

146

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Recent advances in nanotechnology have provided various nanoscale materials that can be used as support for enzyme immobilization. Nanobiocatalysis integrating the biocatalyst and nanoscale materials is drawing great attention as innovative technology. Nanobiocatalysis could achieve not only a much higher enzyme loading capacity and a significantly enhanced mass transfer efficiency, but also unbelievable stabilization. In this review, we will present and discuss the recent progress in nanobiocatalysis and its applications in the fields of bioelectronics, bioconversion, and proteomics.

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A biosensor based on the self-entrapment of glucose oxidase within biomimetic silica nanoparticles induced by a fusion enzyme

Cited by 59 publications

References 32 publications

Control of silicification by genetically engineered fusion proteins: Silk–silica binding peptides

Control of silicification by genetically engineered fusion proteins: Silk–silica binding peptides

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Recent progress in nanobiocatalysis for enzyme immobilization and its application

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