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Immobilized enzyme

About: Immobilized enzyme is a research topic. Over the lifetime, 15282 publications have been published within this topic receiving 401860 citations.


Papers
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Journal ArticleDOI
10 May 2018-Chem
TL;DR: Remarkably, LDH immobilized in the large pores of the MOF is accessible to nicotinamide adenine dinucleotide coenzymes (NAD and NADH), allowing for in situ coenzyme regeneration leading to higher activity than that of the free enzyme.

244 citations

Journal ArticleDOI
Guanglei Ren1, Xinhua Xu1, Qiang Liu1, Juan Cheng1, Xiaoyan Yuan1, Lili Wu1, Yizao Wan1 
TL;DR: In this article, a novel technique for enzyme immobilization on the surface of the Au electrode for designing amperometric biosensor by electrospinning polyvinyl alcohol (PVA) and glucose oxidase (GOD) is presented.
Abstract: A novel technique for enzyme immobilization on the surface of the Au electrode for designing amperometric biosensor by electrospinning poly(vinyl alcohol) (PVA) and glucose oxidase (GOD) is presented in this paper. The immobilized GOD remained active inside the electrospun PVA fibrous membranes. The membranes are promising candidates for immobilization of enzymes because of their high specific surface area and porous structure. The infrared spectrum, the UV–Vis spectrum, and the scanning electronic microscope of the membranes showed that the enzyme had been immobilized inside the PVA membranes. Chronoamperometric measurements demonstrated that electrospun fibrous enzymatic electrodes exhibited a rapid response (1 s) and a higher response current (μA level) to glucose in the normal and diabetic level. The linear response range (from 1 to 10 mM) and the lower detection limit (0.05 mM) of the sensor are satisfying. The electrospun method makes it convenient and efficient to prepare the enzymatic electrode for biosensors.

243 citations

Journal ArticleDOI
TL;DR: It is established that the activity of immobilized lipase could be significantly increased when such alcohols were used for an immersion pretreatment of the enzyme.

242 citations

Book
01 May 1984
TL;DR: The specificity of enzymes and their ability to catalyze reactions of substrates at low concentrations is of great use in chemical analysis and has been used for analytical purposes for a long time.
Abstract: Although soluble enzymes can be used as excellent reagents for the analysis of inorganic and organic compounds, they face a serious challenge when attempts are made to utilize them in complex matrices, like blood or crude water. Problems center about the effect of activators, inhibitors, other substrates, pH, and temperature on the soluble enzyme. However, upon immobilization most of these effects can be eliminated or minimized. For example, an enzyme with a narrow pH range of 4–6 can be transformed upon insolubilization to a more viable reagent with a broad pH range of 4–10. Also, following immobilization the enzymes are much more stable; they can be heated to 37, 40 or 50°C, with little loss of activity; and the activity persists after several thousand analysis are performed. However, the biggest advantage, analytically speaking, of immobilization, is that the insolubilized reagent becomes a much more selective reagent. No longer do many activators and inhibitors have an effect; only the most powerful can actually attack the enzyme.

242 citations

Journal ArticleDOI
TL;DR: In this paper, high current density bioanodes are formed from poly(methylene green) modified electrodes that have been coated with a layer of tetrabutylammonium bromide salt-treated Nafion with dehydrogenase enzymes immobilized within the layer.

242 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023219
2022417
2021480
2020548
2019553
2018543