Enzyme activity assay for horseradish peroxidase encapsulated in peptide nanotubes

Park, Byung-Wook; Ko, Kyoung-A.; Yoon, Do‐Young; Kim, Dong-Shik

doi:10.1016/j.enzmictec.2012.04.004

Cited by 33 publications

(18 citation statements)

References 30 publications

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“…HRP has previously been incorporated into diphenylalanine nanotubes and the authors found that encapsulation enhanced the stability of the enzyme. 40 Enzymes and bacteria have also been incorporated in Fmoc-F/gelatin films. 41 After 48 hours, a 1-2 mm thick gel layer formed, the layer was removed from the growth solution and rinsed.…”

mentioning

confidence: 99%

Surface nucleated growth of dipeptide fibres

et al. 2013

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mentioning

confidence: 99%

Surface nucleated growth of dipeptide fibres

et al. 2013

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“…O espectro de FTIR da HRP livre apresenta bandas intensas em 1658 cm -1 (amida I) e 1536 cm -1 (amida II), características da ligação peptídica da enzima (estiramento C-O da carbonila, deformação N-H e vibração C-N da amida). 11,26,27 Estas bandas aparecem também nos derivados imobilizados. Nos espectros de BC, BCS e biocatalisadores imobilizados a banda de absorção em 897 cm -1 é atribuída ao alongamento (C-O-C) característico de ligações glicosídicas entre as unidades de açúcar presentes na estrutura da celulose.…”

Section: Caracterização Físico-química Do Suporte De Bagaço De Canadeunclassified

Imobilização De Peroxidase De Raiz Forte Em Bagaço De Cana-De-Açúcar

Queiroz¹,

Conceição²,

Melo³

et al. 2018

Quim. Nova

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IMMOBILIZATION OF HORSERADISH PEROXIDASE ON SUGARCANE BAGASSE. The immobilization of horseradish peroxidase (HRP) on raw and alkaline pre-treated sugarcane bagasse by physical adsorption (ADS) and covalent bond (LC) methods was studied. The saturation of the support with 2 mg of HRP/g of support by LC immobilization reached 35% of immobilization efficiency and 39 units of the immobilized enzyme (U). Regarding the HRP immobilization on sugarcane bagasse without pretreatment and using the same HRP loading, it was observed a reduction in the efficiency of immobilization and in the number of immobilized units for both methods, ADS (13.98% and 15.46 U) and LC (15.79% and 17.46 U). The sugarcane bagasse with alkaline pretreatment experiment, on the other hand, exhibited higher potential for HRP immobilization by LC. The supports and biocatalysts were characterized by Fourier transform infrared spectroscopy (FTIR), showing greater availability of hydroxyl groups in the pretreated support and the typical amide I and amide II bands that corroborate the effectiveness of the enzyme immobilization on sugarcane bagasse. In the same way, the thermogravimetric analysis (TGA) confirmed a higher weight loss in the region I for the derivative immobilized by LC, suggesting the presence of water favored enzymatic activity.

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“…Peptide nanotubes (PNTs) have been used to enhance enzyme function and enzyme stability in biosensors [17]. The PNTs serve to protect enzyme activity [18], thereby increasing the shelf-life and performance of the biosensor. Biosensor fabrication may also include the application of a final top-layer component.…”

Section: Introductionmentioning

confidence: 99%

Peptide Nanotube Encapsulated Enzyme Biosensor for Vapor Phase Detection of Malathion, an Organophosphorus Compound

Edwards

Duanghathaipornsuk

Goltz

et al. 2019

Sensors

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This study explores the use of a butyrylcholinesterase (BChE)-based, reversible reaction biosensor using screen-printed electrodes (SPEs) having a smaller working surface area than the single-use electrodes previously studied. Previous research demonstrated the prospective application of a single-use biosensor fabricated with an acetylcholinesterase (AChE) enzyme encapsulated in peptide nanotubes (PNTs) and enhanced with horseradish peroxidase (HRP) to detect organophosphorus compounds (OPCs) in aqueous and gas phases. In the current study, potential improvements to the biosensor are investigated. BChE-based biosensors were fabricated using PNTs, HRP, and Nafion in combination to increase the reactive surface area, enhance sensitivity, and maintain enzyme stability. Cyclic voltammetry (CV) was used along with the new modified sensor to measure malathion concentration in the gas phase. The results show that a BChE-based biosensor could reliably measure gas phase malathion concentrations between 6–25 ppbv by CV with the extent of inhibition linearly proportional to the malathion concentration (R2 = 0.941). This research demonstrated that fabricated BChE-based biosensors could be stored without cold storage requirement for up to six weeks with minimal performance degradation. Moreover, the sensor electrodes were each reused several times, and were still useable at the conclusion of the research. This research demonstrates the potential of fabricating a reusable, inexpensive biosensor that is capable of OPC detection with high sensitivity and a low detection limit without a long-term cold storage requirement.

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Enzyme activity assay for horseradish peroxidase encapsulated in peptide nanotubes

Cited by 33 publications

References 30 publications

Surface nucleated growth of dipeptide fibres

Surface nucleated growth of dipeptide fibres

Imobilização De Peroxidase De Raiz Forte Em Bagaço De Cana-De-Açúcar

Peptide Nanotube Encapsulated Enzyme Biosensor for Vapor Phase Detection of Malathion, an Organophosphorus Compound

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