Topic
Immobilized enzyme
About: Immobilized enzyme is a research topic. Over the lifetime, 15282 publications have been published within this topic receiving 401860 citations.
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TL;DR: In this article, a transesterification reaction was performed using triglycerides and short-chain alcohol by immobilized lipase in non-aqueous conditions and the long-chain fatty acid ester, which is the product of this reaction, can be used as a diesel fuel that does not produce sulfur oxide and minimize the soot particulate.
Abstract: Transesterification reaction was performed using triglycerides and short-chain alcohol by immobilized lipase in non-aqueous conditions. The long-chain fatty acid ester, which is the product of this reaction, can be used as a diesel fuel that does not produce sulfur oxide and minimize the soot particulate. Immobilized Pseudomonas fluorescens lipase showed the highest activity in this reaction. Immobilization of lipase was carried out using porous kaolinite particle as a carrier. When methanol and ethanol were used as alcohol, organic solvent like 1,4-dioxane was required. The reaction could be performed in absence of solvent when 1-propanol and 1-butanol were used as short-chain alcohol. The activity of immobilized lipase was highly increased in comparison with free lipase because its activity sites became more effective. Immobilized enzyme could be repeatedly used without troublesome method of separation and the decrease in its activity was not largely observed.
487 citations
TL;DR: This review focuses on the relation between the progress in ordered mesoporous materials and its corresponding contribution to enzyme immobilization as well as the applications of these materials in biocatalysis.
Abstract: A short time after the discovery of ordered mesoporous materials, which possess unique features such as high specific surface area and pore volume, highly uniform pore distribution and tunable pore size, these materials have been prospected as promising carriers for enzyme immobilization. The immobilization of enzymes in ordered mesoporous materials has been studied for almost two decades. With the development of tailored ordered mesoporous materials and advances in enzyme technology, this field attracted increasing interest due to its quickly expanded functions and applications. This review focuses on the relation between the progress in ordered mesoporous materials and its corresponding contribution to enzyme immobilization as well as the applications of these materials in biocatalysis. The potential trends in the future development of this field are also pointed out.
480 citations
TL;DR: In this paper, the authors discuss the recent advances in using nanofibers as hosts for enzyme immobilization by two different methods, surface attachment and encapsulation, and highlight their distinct characteristics.
Abstract: Enzyme immobilization has attracted continuous attention in the fields of fine chemistry, biomedicine, and biosensor. The performance of immobilized enzyme largely depends on the structure of supports. Nanostructured supports are believed to be able to retain the catalytic activity as well as ensure the immobilization efficiency of enzyme to a high extent. Electrospinning provides a simple and versatile method to fabricate nanofibrous supports. Compared with other nanostructured supports (e.g. mesoporous silica, nanoparticles), nanofibrous supports show many advantages for their high porosity and interconnectivity. This review mainly discusses the recent advances in using nanofibers as hosts for enzyme immobilization by two different methods, surface attachment and encapsulation. Surface attachment refers to physical adsorption or covalent attachment of enzymes on pristine or modified nanofibrous supports, and encapsulation means electrospinning a mixture of enzyme and polymer. We make a detailed comparison between these two immobilization approaches and highlight their distinct characteristics. The prospective applications of enzyme immobilized electrospun nanofibers in the development of biosensors, biofuel cells and biocatalysts are also discussed.
479 citations
TL;DR: The overlap of technical expertise in enzyme immobilization, protein and process engineering will define the next generation of immobilized biocatalysts and the successful scale-up of their induced processes.
Abstract: Enzymes as industrial biocatalysts offer numerous advantages over traditional chemical processes with respect to sustainability and process efficiency. Enzyme catalysis has been scaled up for commercial processes in the pharmaceutical, food and beverage industries, although further enhancements in stability and biocatalyst functionality are required for optimal biocatalytic processes in the energy sector for biofuel production and in natural gas conversion. The technical barriers associated with the implementation of immobilized enzymes suggest that a multidisciplinary approach is necessary for the development of immobilized biocatalysts applicable in such industrial-scale processes. Specifically, the overlap of technical expertise in enzyme immobilization, protein and process engineering will define the next generation of immobilized biocatalysts and the successful scale-up of their induced processes. This review discusses how biocatalysis has been successfully deployed, how enzyme immobilization can improve industrial processes, as well as focuses on the analysis tools critical for the multi-scale implementation of enzyme immobilization for increased product yield at maximum market profitability and minimum logistical burden on the environment and user.
470 citations
TL;DR: Glucose oxidase or lactate oxidase were immobilized in an osmium-based three-dimensional redox hydrogel that electrically connected the enzyme's redox centers to electrodes that correlated well with a substrate calibration in phosphate buffer.
Abstract: Glucose oxidase (GOX) or lactate oxidase (LOX) were immobilized in an osmium-based three-dimensional redox hydrogel that electrically connected the enzyme's redox centers to electrodes The enzyme "wiring" hydrogel was formed by cross-linking poly(1-vinylimidazole) (PVI) complexed with Os-(4,4'-dimethylbpy)2Cl (termed PVI15-dmeOs) with poly(ethylene glycol) diglycidyl ether (peg) Glucose and lactate sensors exhibited typical limiting current densities of 250 and 500 microA/cm2, respectively When the electrodes were poised at 200 mV (SCE), the currents resulting from electrooxidation of ascorbate, urate, acetaminophen, and L-cysteine were negligible When a Nafion film was employed, the linear range was extended from 6 to 30 mM glucose and from 4 to 7 mM lactate The redox potential of the gel-forming polymer was 95 mV (SCE) Glucose and lactate measurements performed in bovine calf serum correlated well with a substrate calibration in phosphate buffer
468 citations