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, the authors reviewed the current technologies available for dye wastewater treatment; different methods utilized for enzyme immobilization; and the application and performance of enzyme incorporated nanotechnology for the treatment of dye wastewater.
Abstract: Enzymes are known to catalyze reactions at high efficiency, operate at milder conditions and are biodegradable. Due to enzyme limitations such as sensitivity to environmental conditions, enzyme immobilization is often used. The commonly employed immobilization methods include adsorption, entrapment, covalent attachment and cross-linking. Many research works have now focused on the immobilization of enzymes on nanoscale support due to the higher surface area to volume ratio, effective enzyme loading, significantly enhanced mass transfer efficiency and minimization of diffusional problems. The application of enzyme incorporated nanotechnology in the treatment of dye wastewater is thus, of high interest. Therefore, this paper has critically reviewed (1) the current technologies available for dye wastewater treatment; (2) different methods utilized for enzyme immobilization; and (3) the application and performance of enzyme incorporated nanotechnology for dye wastewater treatment. We identified that there is high potential for enzyme incorporated nanotechnology to be implemented in dye wastewater treatment due to the high decolorization performance (e.g. laccase immobilized on Fe3O4/SiO2 nanoparticles achieved 99% decolorization of Procion Red MX-5B in 20 min). We have also identified the key challenges faced by enzyme incorporated nanotechnology in dye wastewater treatment that includes: (i) realization of lab scale experiments to industrial applications; (ii) lack of understanding of enzymes incorporated nanotechnology; (iii) recovery of immobilized enzyme; (iv) synthesis of hybrid nanoflowers; and (v) sustainability of the nanomaterials used.
105 citations
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TL;DR: In this article, the authors discussed the recent development of enzyme immobilization methods and applications relating the final properties of the produced biocatalysts with the desired goals, focusing on the opportunities and disadvantages for each method presented.
Abstract: The enzymatic processes are increasingly highlights, especially in the synthesis of chemical products with high added value. The enzyme immobilization can improve industrial biocatalytic processes. The immobilization of enzymes provides the production of efficient, stable biocatalysts, possibility of reuse and easy purification of the products, when compared to the free enzymes. There is a growing research for more efficient methods of enzyme immobilization. In this context, the choice of support and immobilization strategy can significantly improve the final enzymatic properties. In this review paper, we aimed to discuss the versatility of biocatalysts immobilized enzymes design, focusing on the opportunities and disadvantages for each method presented. They discussed the recent development of enzyme immobilization methods and applications relating the final properties of the produced biocatalysts with the desired goals.
105 citations
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TL;DR: Bioaffinity based immobilization procedures usually yield preparations exhibiting high catalytic activity and improved stability against denaturation, facilitating the reuse of support matrix, orient the enzymes favourably and offer the possibility of enzyme immobilization directly from partially pure enzyme preparations or even cell lysates.
Abstract: Procedures that utilize the affinities of biomolecules and ligands for the immobilization of enzymes are gaining increasing acceptance in the construction of sensitive enzyme-based analytical devices as well as for other applications. The strong affinity of polyclonal/monoclonal antibodies for specific enzymes and those of lectins for glycoenzymes bearing appropriate oligosaccharides have been generally employed for the purpose. Potential of affinity pairs like cellulose-cellulose binding domain bearing enzymes and immobilized metal ion-surface histidine bearing enzymes has also been recognised. The bioaffinity based immobilization procedures usually yield preparations exhibiting high catalytic activity and improved stability against denaturation. Bioaffinity based immobilizations are usually reversible facilitating the reuse of support matrix, orient the enzymes favourably and offer the possibility of enzyme immobilization directly from partially pure enzyme preparations or even cell lysates. Enzyme lacking innate ability to bind to various affinity supports can be made to bind to them by chemically or genetically linking the enzymes with appropriate polypeptides/domains like the cellulose binding domain, protein A, histidine-rich peptides, single chain antibodies, etc.
105 citations
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TL;DR: A new protocol for carrying out the preparation of cross-linked aggregates of enzymes with a low number of lysines on its surface is developed.
105 citations
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TL;DR: The molecular cloning and expression of the structural gene encoding sucrose phosphorylase from Leuconostoc mesenteroides (LmSPase) in Escherichia coli DH10B was overproduced 60-fold and D- and L-arabitol were found to be good glucosyl acceptors.
105 citations