Relevant bibliographies by topics / 100301 Biocatalysis and Enzyme Technology

Academic literature on the topic '100301 Biocatalysis and Enzyme Technology'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "100301 Biocatalysis and Enzyme Technology"

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Nidetzky, Bernd, and Helmut Schwab. "Special issue: Enzyme technology and biocatalysis." Journal of Biotechnology 129, no. 1 (March 2007): 1–2. http://dx.doi.org/10.1016/j.jbiotec.2006.12.002.

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Paradisi, Francesca. "Flow Biocatalysis." Catalysts 10, no. 6 (June 9, 2020): 645. http://dx.doi.org/10.3390/catal10060645.

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Yi, Dong, Thomas Bayer, Christoffel P. S. Badenhorst, Shuke Wu, Mark Doerr, Matthias Höhne, and Uwe T. Bornscheuer. "Recent trends in biocatalysis." Chemical Society Reviews 50, no. 14 (2021): 8003–49. http://dx.doi.org/10.1039/d0cs01575j.

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Technological developments enable the discovery of novel enzymes, the advancement of enzyme cascade designs and pathway engineering, moving biocatalysis into an era of technology integration, intelligent manufacturing and enzymatic total synthesis.
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Bernhardt, Paul V. "Enzyme Electrochemistry — Biocatalysis on an Electrode." Australian Journal of Chemistry 59, no. 4 (2006): 233. http://dx.doi.org/10.1071/ch05340.

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Oxidoreductase enzymes catalyze single- or multi-electron reduction/oxidation reactions of small molecule inorganic or organic substrates, and they are integral to a wide variety of biological processes including respiration, energy production, biosynthesis, metabolism, and detoxification. All redox enzymes require a natural redox partner such as an electron-transfer protein (e.g. cytochrome, ferredoxin, flavoprotein) or a small molecule cosubstrate (e.g. NAD(P)H, dioxygen) to sustain catalysis, in effect to balance the substrate/product redox half-reaction. In principle, the natural electron-transfer partner may be replaced by an electrochemical working electrode. One of the great strengths of this approach is that the rate of catalysis (equivalent to the observed electrochemical current) may be probed as a function of applied potential through linear sweep and cyclic voltammetry, and insight to the overall catalytic mechanism may be gained by a systematic electrochemical study coupled with theoretical analysis. In this review, the various approaches to enzyme electrochemistry will be discussed, including direct and indirect (mediated) experiments, and a brief coverage of the theory relevant to these techniques will be presented. The importance of immobilizing enzymes on the electrode surface will be presented and the variety of ways that this may be done will be reviewed. The importance of chemical modification of the electrode surface in ensuring an environment conducive to a stable and active enzyme capable of functioning natively will be illustrated. Fundamental research into electrochemically driven enzyme catalysis has led to some remarkable practical applications. The glucose oxidase enzyme electrode is a spectacularly successful application of enzyme electrochemistry. Biosensors based on this technology are used worldwide by sufferers of diabetes to provide rapid and accurate analysis of blood glucose concentrations. Other applications of enzyme electrochemistry are in the sensing of macromolecular complexation events such as antigen–antibody binding and DNA hybridization. The review will include a selection of enzymes that have been successfully investigated by electrochemistry and, where appropriate, discuss their development towards practical biotechnological applications.
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Kim, In Jung. "Enzyme Catalysis: Advances, Techniques, and Outlooks." Applied Sciences 12, no. 16 (August 11, 2022): 8036. http://dx.doi.org/10.3390/app12168036.

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Fernandes, Pedro, and Carla C. C. R. de Carvalho. "Multi-Enzyme Systems in Flow Chemistry." Processes 9, no. 2 (January 25, 2021): 225. http://dx.doi.org/10.3390/pr9020225.

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Recent years have witnessed a growing interest in the use of biocatalysts in flow reactors. This merging combines the high selectivity and mild operation conditions typical of biocatalysis with enhanced mass transfer and resource efficiency associated to flow chemistry. Additionally, it provides a sound environment to emulate Nature by mimicking metabolic pathways in living cells and to produce goods through the systematic organization of enzymes towards efficient cascade reactions. Moreover, by enabling the combination of enzymes from different hosts, this approach paves the way for novel pathways. The present review aims to present recent developments within the scope of flow chemistry involving multi-enzymatic cascade reactions. The types of reactors used are briefly addressed. Immobilization methodologies and strategies for the application of the immobilized biocatalysts are presented and discussed. Key aspects related to the use of whole cells in flow chemistry are presented. The combination of chemocatalysis and biocatalysis is also addressed and relevant aspects are highlighted. Challenges faced in the transition from microscale to industrial scale are presented and discussed.
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Kunzendorf, Andreas, and Uwe T. Bornscheuer. "Optimierte Designer-Enzyme für die pharmazeutische Industrie." BIOspektrum 28, no. 7 (November 2022): 760–62. http://dx.doi.org/10.1007/s12268-022-1852-0.

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AbstractEnzymes, the driving biocatalysts in living organisms, are typically not suited for large-scale industrial use. In the last decade, enzyme engineering has evolved into the key technology to design tailor-made enzymes for chemical and pharmaceutical applications. We highlight current trends in enzyme engineering and biocatalysis based on outstanding examples from the pharmaceutical industry.
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Xiang, Lanting, Felix Kaspar, Anett Schallmey, and Iordania Constantinou. "Two-Phase Biocatalysis in Microfluidic Droplets." Biosensors 11, no. 11 (October 21, 2021): 407. http://dx.doi.org/10.3390/bios11110407.

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This Perspective discusses the literature related to two-phase biocatalysis in microfluidic droplets. Enzymes used as catalysts in biocatalysis are generally less stable in organic media than in their native aqueous environments; however, chemical and pharmaceutical compounds are often insoluble in water. The use of aqueous/organic two-phase media provides a solution to this problem and has therefore become standard practice for multiple biotransformations. In batch, two-phase biocatalysis is limited by mass transport, a limitation that can be overcome with the use of microfluidic systems. Although, two-phase biocatalysis in laminar flow systems has been extensively studied, microfluidic droplets have been primarily used for enzyme screening. In this Perspective, we summarize the limited published work on two-phase biocatalysis in microfluidic droplets and discuss the limitations, challenges, and future perspectives of this technology.
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Federsel, Hans-Jürgen, Thomas S. Moody, and Steve J. C. Taylor. "Recent Trends in Enzyme Immobilization—Concepts for Expanding the Biocatalysis Toolbox." Molecules 26, no. 9 (May 10, 2021): 2822. http://dx.doi.org/10.3390/molecules26092822.

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Enzymes have been exploited by humans for thousands of years in brewing and baking, but it is only recently that biocatalysis has become a mainstream technology for synthesis. Today, enzymes are used extensively in the manufacturing of pharmaceuticals, food, fine chemicals, flavors, fragrances and other products. Enzyme immobilization technology has also developed in parallel as a means of increasing enzyme performance and reducing process costs. The aim of this review is to present and discuss some of the more recent promising technical developments in enzyme immobilization, including the supports used, methods of fabrication, and their application in synthesis. The review highlights new support technologies such as the use of well-established polysaccharides in novel ways, the use of magnetic particles, DNA, renewable materials and hybrid organic–inorganic supports. The review also addresses how immobilization is being integrated into developing biocatalytic technology, for example in flow biocatalysis, the use of 3D printing and multi-enzymatic cascade reactions.
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Seo, Min-Ju, and Claudia Schmidt-Dannert. "Organizing Multi-Enzyme Systems into Programmable Materials for Biocatalysis." Catalysts 11, no. 4 (March 24, 2021): 409. http://dx.doi.org/10.3390/catal11040409.

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Significant advances in enzyme discovery, protein and reaction engineering have transformed biocatalysis into a viable technology for the industrial scale manufacturing of chemicals. Multi-enzyme catalysis has emerged as a new frontier for the synthesis of complex chemicals. However, the in vitro operation of multiple enzymes simultaneously in one vessel poses challenges that require new strategies for increasing the operational performance of enzymatic cascade reactions. Chief among those strategies is enzyme co-immobilization. This review will explore how advances in synthetic biology and protein engineering have led to bioinspired co-localization strategies for the scaffolding and compartmentalization of enzymes. Emphasis will be placed on genetically encoded co-localization mechanisms as platforms for future autonomously self-organizing biocatalytic systems. Such genetically programmable systems could be produced by cell factories or emerging cell-free systems. Challenges and opportunities towards self-assembling, multifunctional biocatalytic materials will be discussed.
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Dissertations / Theses on the topic "100301 Biocatalysis and Enzyme Technology"

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Odnell, Anna. "Influencing anaerobic digestion early stage processes for increased biomethane production from different substrate components." Licentiate thesis, Linköpings universitet, Kemi, 2018. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-147721.

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Finding alternatives to petroleum-based energy sources is of interest since it could reduce the emissions of net carbon dioxide to the atmosphere by increasing the usage of renewable energy sources. To do so improvements are needed in the renewable energy production sector. Biogas production is of interest since the anaerobic digestion process can degrade many different biomolecules and is, contrary to e.g. bioethanol and biodiesel, not dependent on specific molecules. Thus, many wastes such as slaughterhouse waste, sludge from waste water treatment and lignocellulose residual material etc. can be used as substrates for biogas production. However, there are limitations in the degradation process depending on the composition of the selected substrate. To overcome these limitations such as inhibition of different microorganisms, or recalcitrant substrate, different methods can be used to increase the biogas production.  In this study different substrates were selected and analyzed/treated for remedies of early stage rate limiting problems of the anaerobic digestion process. Different analyzes and techniques were selected depending on the limitations correlated to the main problematic component of the specific substrate.  Improvements could be reached for the degradation of slaughterhouse waste by augmentation with the clay mineral zeolite. Addition of different enzymes to the substrate environment of different waste water treatment plant sludges resulted in limited life time of the selected enzymes. However, certain enzymes proved to be promising candidates with an effect of increased biogas production rate and yield for the time that the enzyme remained active. In an additional experiment, cellulolytic enzymes, naturally produced by a biogas producing microbial community, were induced, collected and added to a biogas experiment of ensiled forage ley, by which it was shown that these cellulases led to an increase in biogas production rate and yield. Thus, the studies demonstrate different techniques for improving the anaerobic digestion process of different types of substrates.

Handledare saknas

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Semlitsch, Stefan. "Building blocks for polymer synthesis by enzymatic catalysis." Doctoral thesis, KTH, Industriell bioteknologi, 2017. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-212499.

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The search for alternatives to oil-based monomers has sparked interest for scientists to focus on the use of renewable resources for energy production, for the synthesis of polymeric materials and in other areas. With the use of renewable resources, scientists face new challenges to first isolate interesting molecules and then to process them. Enzymes are nature’s own powerful catalysts and display a variety of activities. They regulate important functions in life. They can also be used for chemical synthesis due to their efficiency, selectivity and mild reaction conditions. The selectivity of the enzyme allows specific reactions enabling the design of building blocks for polymers. In the work presented here, a lipase (Candida antarctica lipase B (CalB)) was used to produce building blocks for polymers. An efficient route was developed to selectively process epoxy-functional fatty acids into resins with a variety of functional groups (maleimide, oxetane, thiol, methacrylate). These oligoester structures, based on epoxy fatty acids from birch bark and vegetable oils, could be selectively cured to form thermosets with tailored properties. The specificity of an esterase with acyl transfer activity from Mycobacterium smegmatis (MsAcT) was altered by rational design. The produced variants increased the substrate scope and were then used to synthesize amides in water, where the wild type showed no conversion. A synthetic procedure was developed to form mixed dicarboxylic esters by selectively reacting only one side of divinyl adipate in order to introduce additional functional groups.

QC 20170823

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López, Olvera Enrique Argenis. "Kinetic studies of carrier conjugated protease inhibitors." Thesis, Uppsala universitet, Institutionen för biologisk grundutbildning, 2019. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-397114.

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Conjugates of soybean trypsin inhibitor (SBTI) and potato serine protease inhibitor (PSPI) immobilized on metal oxide particles of ~100nm diameter were prepared. Inhibition of trypsin hydrolysis of BAPA by these conjugates was measured and enzyme kinetics constants kcat, KM, kcat/KM and ki were determined. Metal oxide particles presented an inhibitory effect similar to that of a competitive inhibitor, noticed through the increase value of the K M constant. Furthermore, PSPI conjugates had the highest inhibition of trypsin, illustrated by the significantly higher value of KM relative to the value for particles only.
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Håkansson, Hederos Sofia. "Catalysis and Site-Specific Modification of Glutathione Transferases Enabled by Rational Design." Doctoral thesis, Linköpings universitet, Organisk Kemi, 2005. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-3962.

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This thesis describes the rational design of a novel enzyme, a thiolester hydrolase, derived from human glutathione transferase (GST) A1-1 by the introduction of a single histidine residue. The first section of the thesis describes the design and the determination of the reaction mechanism. The design was based on the crystal structure of human GST A1-1 complexed with S-benzylglutathione. The resulting enzyme, A216H, catalyzed the hydrolysis of the non-natural substrate GSB, a thiolester of glutathione and benzoic acid. The reaction followed saturation kinetics with a kcat of 0.00078 min-1 and KM of 5 μM. The rate constant ratio, (kcat/KM)/kuncat, was found to be more than 107 M-1. The introduction of a single His residue in position 216 opened up a novel reaction pathway in human GST A1-1 and is a nice example of catalytic promiscuity. The substrate requirements were investigated and A216H was found to be selective since only two out of 18 GS-thiolesters tested were substrates for A216H. The reaction mechanism of the A216H-catalyzed hydrolysis of GSB was determined and found to proceed via an acyl intermediate at Y9. The hydrolysis was catalyzed by H216 that acts as a general base and the deacylation was found to be the rate-determining step. The Y9-intermediate could be selectively trapped by oxygen nucleophiles and primary alcohols, in particular 1-propanol and trifluoroethanol, were the most efficient. In addition, saturation kinetics was obtained in the acyl transfer reaction with 1-propanol indicating the presence of a second binding site in A216H. The second section of this thesis describes the site-specific covalent modification of human GST A1-1. The addition of GSB to the wild-type protein results in a site-specific benzoylation of only one tyrosine residue, Y9, out of ten present in the protein (one out of totally 51 nucleophiles). The reaction was tested with five GST classes (Alpha, Mu, Pi, Theta and Omega) and found to be specific for the Alpha class isoenzymes. The covalent modification reaction was further refined to target a single lysine residue, K216, providing a more stable linkage in the form of an amide bond. The reaction was found to be versatile and approximately 50% of the GS-thiolesters tested acylated K216, including a fluorophore.

On the day of the public defence the status of article II was: Submitted and article IV was: In press.

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Blissing, Annica. "Thiopurine S-methyltransferase - characterization of variants and ligand binding." Licentiate thesis, Linköpings universitet, Kemi, 2017. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-136558.

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Thiopurine S-methyltransferase (TPMT) belongs to the Class I S-adenosylmethionine-dependent methyltransferase (SAM-MT) super family of structurally related proteins. Common to the members of this large protein family is the catalysis of methylation reactions using S-adenosylmethionine (SAM) as a methyl group donor, although SAM-MTs act on a wide range of different substrates and carry out numerous biologically important functions. While the natural function of TPMT is unknown, this enzyme is involved in the metabolism of thiopurines, a class of pharmaceutical substances administered in treatment of immune-related disorders. Specifically, methylation by TPMT inactivates thiopurines and their metabolic intermediates, which reduces the efficacy of clinical treatment and increases the risk of adverse side effects. To further complicate matters, TPMT is a polymorphic enzyme with over 40 naturally occurring variants known to date, most of which exhibit lowered methylation activity towards thiopurines. Consequently, there are individual variations in TPMTmediated thiopurine inactivation, and the administered dose has to be adjusted prior to clinical treatment to avoid harmful side effects. Although the clinical relevance of TPMT is well established, few studies have investigated the molecular causes of the reduced methylation activity of variant proteins. In this thesis, the results of biophysical characterization of two variant proteins, TPMT*6 (Y180F) and TPMT*8 (R215H), are presented. While the properties of TPMT*8 were indistinguishable from those of the wild-type protein, TPMT*6 was found to be somewhat destabilized. Interestingly, the TPMT*6 amino acid substitution did not affect the functionality or folding pattern of the variant protein. Therefore, the decreased in vivo functionality reported for TPMT*6 is probably caused by increased proteolytic degradation in response to the reduced stability of this protein variant, rather than loss of function. Also presented herein are novel methodological approaches for studies of TPMT and its variants. Firstly, the advantages of using 8-anilinonaphthalene-1-sulfonic acid (ANS) to probe TPMT tertiary structure and active site integrity are presented. ANS binds exclusively to the native state of TPMT with high affinity (KD ~ 0.2 μm) and a 1:1 ratio. The stability of TPMT was dramatically increased by binding of ANS, which was shown to co-localize with the structurally similar adenine moiety of the cofactor SAM. Secondly, an enzyme activity assay based on isothermal titration calorimetry (ITC) is presented. Using this approach, the kinetics of 6-MP and 6-TG methylation by TPMT has been characterized.
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(9751112), Elena A. Robles Molina. "EVALUATIONS ON ENZYMATIC EPOXIDATION, EFFICIENCY AND DECAY." Thesis, 2020.

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The potential use of enzymes in industrial synthesis of epoxidized soybean oil has been limited through the high cost of the enzyme catalyst, in this work we evaluate the effectiveness of chemo enzymatic epoxidation of high oleic soybean oil (HOSBO) using lipase B from Candida antarctica (CALB) on immobilization support Immobead 150 and H2O2 in a solvent-free system. Additionally, we evaluated the production decay rates for hydrolytic activity and epoxide product formation over consecutive batches to determine half-life of the enzyme catalyst.

Batch epoxidation of HOSBO using CALB on 4wt% loading shows yields higher than 90% after 12 hrs. of reaction, and with a correlation to the consumption of double bonds suggesting that the reaction is selective and limiting side product reactions. Non-selective hydrolysis of oil was not found beyond the initial hydrolysis degree of raw HOSBO. Evaluations of decay given by epoxide product formation and released free fatty acids shows a half-life of the enzyme catalyst on these activities is of 22 ad 25 hrs. respectively. Finally, we evaluated the physical parameters influencing this decay, and found that H2O2 presence is the most important parameter of enzyme inactivation with no significant effect from its slowed addition. We propose a new reactor configuration for the analysis of the specific steps on epoxide formation through peracid intermediates.

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Books on the topic "100301 Biocatalysis and Enzyme Technology"

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Biocatalysts and enzyme technology. Weinheim: Wiley-VCH, 2004.

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Problem Solving In Enzyme Biocatalysis. John Wiley & Sons Inc, 2013.

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Kasche, Volker, Uwe Theo Bornscheuer, and Klaus Buchholz. Biocatalysts and Enzyme Technology. Wiley-VCH Verlag GmbH, 2012.

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Kasche, Volker, Uwe Theo Bornscheuer, and Klaus Buchholz. Biocatalysts and Enzyme Technology. Wiley & Sons, Limited, John, 2012.

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Kasche, Volker, Uwe Theo Bornscheuer, and Klaus Buchholz. Biocatalysts and Enzyme Technology. Wiley-VCH, 2005.

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Kasche, Volker, Uwe Theo Bornscheuer, and Klaus Buchholz. Biocatalysts and Enzyme Technology. Wiley & Sons, Incorporated, John, 2012.

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Kasche, Volker, Uwe Theo Bornscheuer, and Klaus Buchholz. Biocatalysts and Enzyme Technology. Wiley & Sons, Incorporated, John, 2012.

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Book chapters on the topic "100301 Biocatalysis and Enzyme Technology"

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Woodyer, Ryan D., Tyler W. Johannes, and Huimin Zhao. "Regeneration of Cofactors for Enzyme Biocatalysis." In Enzyme Technology, 85–103. New York, NY: Springer New York, 2006. http://dx.doi.org/10.1007/978-0-387-35141-4_5.

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Straathof, Adrie J. J. "Biocatalysis in Organic Media using Enzymes." In Enzyme Technology, 105–21. New York, NY: Springer New York, 2006. http://dx.doi.org/10.1007/978-0-387-35141-4_6.

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Longoria, Adriana, Raunel Tinoco, and Eduardo Torres. "Enzyme Technology of Peroxidases: Immobilization, Chemical and Genetic Modification." In Biocatalysis Based on Heme Peroxidases, 209–43. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-12627-7_9.

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Dinis, Pedro, Benjamin Nji Wandi, Thadée Grocholski, and Mikko Metsä-Ketelä. "Chimeragenesis for Biocatalysis." In Advances in Enzyme Technology, 389–418. Elsevier, 2019. http://dx.doi.org/10.1016/b978-0-444-64114-4.00014-5.

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Singh, Vikram. "Bioremediation." In Biotechnology, 1002–30. IGI Global, 2019. http://dx.doi.org/10.4018/978-1-5225-8903-7.ch039.

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Pollution is the biggest menace to the living being in this planet today. Enzyme bioremediation is a “breakthrough technology” that holds the potential of pollutant eradication through exploiting the enzyme potential by using the various techniques. Enzyme biocatalysis is referred as white biotechnology and work by green chemistry concept. Moreover, developments in the design and application of enzyme cocktails, mutienzyme complexes, promiscuous enzymes and protein families (cupin and VOC superfamily) has recently emerged a new opportunity in bioremediation. The implementation of various enzyme modification approaches intended for potential bioremediation has been done by adopting enzyme immobilization using magnetic nanoparticles, designer enzymes generation through enzyme engineering, nano-technological advancement for single enzyme nanoparticle generations, electro-bioremediation and carbon nanotube construction. Hence, enzyme bioremediation have greater positive effects and propose significant promise to pollutant bioremediation. In conclusion, the enzymatic bioremediation open the new era of pollutant eradication for clean, safe and green environment.
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Singh, Vikram. "Bioremediation." In Handbook of Research on Uncovering New Methods for Ecosystem Management through Bioremediation, 433–60. IGI Global, 2015. http://dx.doi.org/10.4018/978-1-4666-8682-3.ch017.

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Pollution is the biggest menace to the living being in this planet today. Enzyme bioremediation is a “breakthrough technology” that holds the potential of pollutant eradication through exploiting the enzyme potential by using the various techniques. Enzyme biocatalysis is referred as white biotechnology and work by green chemistry concept. Moreover, developments in the design and application of enzyme cocktails, mutienzyme complexes, promiscuous enzymes and protein families (cupin and VOC superfamily) has recently emerged a new opportunity in bioremediation. The implementation of various enzyme modification approaches intended for potential bioremediation has been done by adopting enzyme immobilization using magnetic nanoparticles, designer enzymes generation through enzyme engineering, nano-technological advancement for single enzyme nanoparticle generations, electro-bioremediation and carbon nanotube construction. Hence, enzyme bioremediation have greater positive effects and propose significant promise to pollutant bioremediation. In conclusion, the enzymatic bioremediation open the new era of pollutant eradication for clean, safe and green environment.
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