Membrane Bound Enzyme Hosted in Liquid Crystalline Cubic Phase for Sensing and Fuel Cells

Nazaruk, Ewa; Landau, Ehud M.; Bilewicz, Renata

doi:10.1016/j.electacta.2014.05.130

Cited by 32 publications

(18 citation statements)

References 25 publications

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“…Some studies have been reported on FDH with mediators at polypyrrole matrix-modified electrode [6][7][8][9], carbon paste electrode [10], membrane mimetic layer on gold electrode [11], and layer-by-layer assembly of polyelectrolytes [12]. Furthermore, FDH has a high DET activity and several biosensors and biofuel cells based on DET reactions of FDH have been reported [13][14][15][16][17][18][19]. Since various mutations can be induced in FDH, FDH is a suitable enzyme for the elucidation of the DET mechanisms.…”

Section: Introductionmentioning

confidence: 97%

Function of C-terminal hydrophobic region in fructose dehydrogenase

Sugimoto

Kawai

Kitazumi

et al. 2015

Electrochimica Acta

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Section: Introductionmentioning

confidence: 97%

Function of C-terminal hydrophobic region in fructose dehydrogenase

Sugimoto

Kawai

Kitazumi

et al. 2015

Electrochimica Acta

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“…In 2014, Nazaruk et al used liquid crystalline cubic phase (LCP) and CNTs for the immobilisation of FDH in order to enhance the DET of FDH, exploiting the possibility to retain native conformation and bioactivity of FDH [ 153 ]. The calibration curve of FDH/LPC/SWCNTs/GC electrode showed a linear relationship between current density and fructose concentration up to 10 mM.…”

Section: Fructose Dehydrogenasementioning

confidence: 99%

“…In 2014, Nazaruk et al [ 153 ] used monoolein or phytantriol liquid crystalline cubic phase and CNTs for the immobilisation of FDH. Entrapment within the cubic phase prevents the guest protein from chemical and physical degradation, thus facilitating retention of its native conformation and bioactivity.…”

Section: Fructose Dehydrogenasementioning

confidence: 99%

Direct Electron Transfer of Dehydrogenases for Development of 3rd Generation Biosensors and Enzymatic Fuel Cells

Bollella

Gorton

Antiochia

2018

Sensors

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Dehydrogenase based bioelectrocatalysis has been increasingly exploited in recent years in order to develop new bioelectrochemical devices, such as biosensors and biofuel cells, with improved performances. In some cases, dehydrogeases are able to directly exchange electrons with an appropriately designed electrode surface, without the need for an added redox mediator, allowing bioelectrocatalysis based on a direct electron transfer process. In this review we briefly describe the electron transfer mechanism of dehydrogenase enzymes and some of the characteristics required for bioelectrocatalysis reactions via a direct electron transfer mechanism. Special attention is given to cellobiose dehydrogenase and fructose dehydrogenase, which showed efficient direct electron transfer reactions. An overview of the most recent biosensors and biofuel cells based on the two dehydrogenases will be presented. The various strategies to prepare modified electrodes in order to improve the electron transfer properties of the device will be carefully investigated and all analytical parameters will be presented, discussed and compared.

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“…[18] The immobilization of membrane-bound proteins and the design of solid supports mimicking natural membranes are an active field of research. Liposomes, [19] sol-gel materials [20] and lipid crystalline cubic phases [21,22] are some of the membrane mimetic-matrixes developed for IMP immobilization. By contrast, few examples of covalent immobilization have been reported to date.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of γ‐Glutamyl Transpeptidase from Equine Kidney for the Synthesis of kokumi Compounds

et al. 2019

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γ‐Glutamyl transpeptidase from equine kidney (ekGGT, E.C. 2.3.2.2) is an intrinsic membrane enzyme which transfers the γ‐glutamyl moiety of glutathione to amino acids and peptides, thus producing γ‐glutamyl derivatives. An immobilization study of ekGGT was carried out with the aim to develop a robust biocatalyst for the synthesis of γ‐glutamyl amino acids which are known as kokumi compounds. Heterofunctional octyl‐glyoxyl‐agarose resulted in a high immobilization yield and activity recovery (93 % and 88 %, respectively). Immobilized ekGGT retained more than 95 % activity under reaction conditions (Tris‐HCl, pH 9, 0.05 M) after 6 days, whereas the residual activity after 6 reaction cycles (18 days) was 85 %. The synthesis of γ‐glutamylmethionine catalyzed by octyl‐glyoxyl‐agarose‐ekGGT afforded the product in 42 % yield (101 mg). The immobilized ekGGT was characterized by Raman spectroscopy. The immobilization protocol developed for ekGGT could be of general applicability to membrane proteins.

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Membrane Bound Enzyme Hosted in Liquid Crystalline Cubic Phase for Sensing and Fuel Cells

Cited by 32 publications

References 25 publications

Function of C-terminal hydrophobic region in fructose dehydrogenase

Function of C-terminal hydrophobic region in fructose dehydrogenase

Direct Electron Transfer of Dehydrogenases for Development of 3rd Generation Biosensors and Enzymatic Fuel Cells

Immobilization of γ‐Glutamyl Transpeptidase from Equine Kidney for the Synthesis of kokumi Compounds

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