Journal articles: '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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Mestrom, Przypis, Kowalczykiewicz, Pollender, Kumpf, Marsden, Bento, et al. "Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach." International Journal of Molecular Sciences 20, no. 21 (October 23, 2019): 5263. http://dx.doi.org/10.3390/ijms20215263.

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Enzymes are nature’s catalyst of choice for the highly selective and efficient coupling of carbohydrates. Enzymatic sugar coupling is a competitive technology for industrial glycosylation reactions, since chemical synthetic routes require extensive use of laborious protection group manipulations and often lack regio- and stereoselectivity. The application of Leloir glycosyltransferases has received considerable attention in recent years and offers excellent control over the reactivity and selectivity of glycosylation reactions with unprotected carbohydrates, paving the way for previously inaccessible synthetic routes. The development of nucleotide recycling cascades has allowed for the efficient production and reuse of nucleotide sugar donors in robust one-pot multi-enzyme glycosylation cascades. In this way, large glycans and glycoconjugates with complex stereochemistry can be constructed. With recent advances, LeLoir glycosyltransferases are close to being applied industrially in multi-enzyme, programmable cascade glycosylations.

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Sheldon, Roger. "CLEAs, Combi-CLEAs and ‘Smart’ Magnetic CLEAs: Biocatalysis in a Bio-Based Economy." Catalysts 9, no. 3 (March 14, 2019): 261. http://dx.doi.org/10.3390/catal9030261.

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Biocatalysis has emerged in the last decade as a pre-eminent technology for enabling the envisaged transition to a more sustainable bio-based economy. For industrial viability it is essential that enzymes can be readily recovered and recycled by immobilization as solid, recyclable catalysts. One method to achieve this is via carrier-free immobilization as cross-linked enzyme aggregates (CLEAs). This methodology proved to be very effective with a broad selection of enzymes, in particular carbohydrate-converting enzymes. Methods for optimizing CLEA preparations by, for example, adding proteic feeders to promote cross-linking, and strategies for making the pores accessible for macromolecular substrates are critically reviewed and compared. Co-immobilization of two or more enzymes in combi-CLEAs enables the cost-effective use of multiple enzymes in biocatalytic cascade processes and the use of “smart” magnetic CLEAs to separate the immobilized enzyme from other solids has raised the CLEA technology to a new level of industrial and environmental relevance. Magnetic-CLEAs of polysaccharide-converting enzymes, for example, are eminently suitable for use in the conversion of first and second generation biomass.

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Sharikov, A. Y., E. N. Sokolova, M. V. Amelyakina, T. V. Yuraskina, V. V. Ivanov, and E. M. Serba. "Development of a concept for the production of wheat snacks with the elimination of gluten by the biocatalysis." Proceedings of the Voronezh State University of Engineering Technologies 82, no. 4 (January 20, 2021): 77–83. http://dx.doi.org/10.20914/2310-1202-2020-4-77-83.

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The increase in the number of cases of allergic reactions and celiac disease is an important problem. The solution to this problem is the search and development of relevant and effective ways to eliminate gluten. Specific amino acid sequences glutamine and proline determine the resistance to protease hydrolysis of the structural domains of gluten fractions. The analysis of the literature data showed that an alternative to the gluten-free diet is the use of biotechnological methods for modifying ingredients containing gluten. Such methods include the use of leavens on the base of lactic acid bacteria or enzyme preparations containing peptidases specific to gluten biocatalysis. In addition, the pretreatment of raw materials by extrusion cooking contributes to an increase in the degree of gluten hydrolysis. The effect of the thermoplastic extrusion and various enzyme systems containing proteases, amylolytic, cellulolytic and hemicellulolytic enzymes on the changes in the molecular weights of wheat protein fractions was studied. It was found that extrusion as a factor of protein modification significantly affects the proteolysis of wheat proteins using enzyme systems of different substrate specificity. The most effective hydrolysis was shown by the use of a complex enzyme preparation Amyloprotoorizin. including The effect was also noted after bioconversion of non-extruded wheat. An algorithm for the technology of wheat snacks based on the processes of extrusion and biocatalysis of proteins with specific proteases for the elimination of gluten is devepoped. The practical implementation of the technology will make it possible to obtain ready-to-eat snacks, which will be investigated for the preservation or elimination of antigenic properties during clinical trials.

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Zhu, Lin‐Lin, Chang‐Tong Zhu, Meng Xiong, Chuan‐Qi Jin, Sheng Sheng, Fu‐An Wu, and Jun Wang. "Enzyme immobilization on photopatterned temperature‐response poly (N‐isopropylacrylamide) for microfluidic biocatalysis." Journal of Chemical Technology & Biotechnology 94, no. 5 (March 5, 2019): 1670–78. http://dx.doi.org/10.1002/jctb.5946.

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15

Lee, Jae Kwan, and Mahn-Joo Kim. "Ionic liquid co-lyophilized enzyme for biocatalysis in organic solvent: Remarkably enhanced activity and enantioselectivity." Journal of Molecular Catalysis B: Enzymatic 68, no. 3-4 (March 2011): 275–78. http://dx.doi.org/10.1016/j.molcatb.2010.11.017.

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16

Reeve, Holly A., Philip A. Ash, HyunSeo Park, Ailun Huang, Michalis Posidias, Chloe Tomlinson, Oliver Lenz, and Kylie A. Vincent. "Enzymes as modular catalysts for redox half-reactions in H2-powered chemical synthesis: from biology to technology." Biochemical Journal 474, no. 2 (January 6, 2017): 215–30. http://dx.doi.org/10.1042/bcj20160513.

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The present study considers the ways in which redox enzyme modules are coupled in living cells for linking reductive and oxidative half-reactions, and then reviews examples in which this concept can be exploited technologically in applications of coupled enzyme pairs. We discuss many examples in which enzymes are interfaced with electronically conductive particles to build up heterogeneous catalytic systems in an approach which could be termed synthetic biochemistry. We focus on reactions involving the H+/H2 redox couple catalysed by NiFe hydrogenase moieties in conjunction with other biocatalysed reactions to assemble systems directed towards synthesis of specialised chemicals, chemical building blocks or bio-derived fuel molecules. We review our work in which this approach is applied in designing enzyme-modified particles for H2-driven recycling of the nicotinamide cofactor NADH to provide a clean cofactor source for applications of NADH-dependent enzymes in chemical synthesis, presenting a combination of published and new work on these systems. We also consider related photobiocatalytic approaches for light-driven production of chemicals or H2 as a fuel. We emphasise the techniques available for understanding detailed catalytic properties of the enzymes responsible for individual redox half-reactions, and the importance of a fundamental understanding of the enzyme characteristics in enabling effective applications of redox biocatalysis.

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Won, Kee Hoon, Eulaia Siu, and Chan Beum Park. "Conductive Sol-Gel Hybrid Materials for Novel Cofactor Regeneration in Biocatalysis." Solid State Phenomena 124-126 (June 2007): 1087–90. http://dx.doi.org/10.4028/www.scientific.net/ssp.124-126.1087.

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The electrochemical recycling of cofactors during enzymatic biocatalysis has long been acknowledged as a potentially powerful technology in fine chemical synthesis. Major obstacle for this approach is that cofactors only in the immediate vicinity of the electrode surface are productive. This problem further causes high overpotential at electrode surfaces leading to undesired side reactions producing enzymatically-inactive dimer and isomer of cofactor. So far, several attempts had been made to address these problems by focusing on surface modifications, which explored to retain the enzyme and/or cofactor close to the working electrode including electrode deposition and membranes surrounding the electrode. In this work, we demonstrate a new concept of cofactor regeneration by using ‘electronically-conductive’ sol-gel hybrid materials. When conductive hybrid gels were added to the reaction medium, we found that cofactor could be efficiently recycled throughout the whole reactor system leading to high yield of product, which was unattainable with conventional technologies.

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Taylor, I. N., R. C. Brown, M. Bycroft, G. King, J. A. Littlechild, M. C. Lloyd, C. Praquin, H. S. Toogood, and S. J. C. Taylor. "Application of thermophilic enzymes in commercial biotransformation processes." Biochemical Society Transactions 32, no. 2 (April 1, 2004): 290–92. http://dx.doi.org/10.1042/bst0320290.

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Biocatalysis is a useful tool in the provision of chiral technology and extremophilic enzymes are just one component in that toolbox. Their role is not always attributable to their extremophilic properties; as with any biocatalyst certain other criteria should be satisfied. Those requirements for a useful biocatalyst will be discussed including issues of selectivity, volume efficiency, security of supply, technology integration, intellectual property and regulatory compliance. Here we discuss the discovery and commercialization of an l-aminoacylase from Thermococcus litoralis, the product of a LINK project between Chirotech Technology and the University of Exeter. The enzyme was cloned into Escherichia coli to aid production via established mesophilic fermentation protocols. A simple downstream process was then developed to assist in the production of the enzyme as a genetically modified-organism-free reagent. The fermentation and downstream processes are operated at the 500 litre scale. Characterization of the enzyme demonstrated a substrate preference for N-benzoyl groups over N-acetyl groups. The operational parameters have been defined in part by substrate-concentration tolerances and also thermostabilty. Several examples of commercial biotransformations will be discussed including a process that is successful by virtue of the enzyme's thermotolerance.

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Gkantzou, Elena, Michaela Patila, and Haralambos Stamatis. "Magnetic Microreactors with Immobilized Enzymes—From Assemblage to Contemporary Applications." Catalysts 8, no. 7 (July 14, 2018): 282. http://dx.doi.org/10.3390/catal8070282.

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Microfluidics, as the technology for continuous flow processing in microscale, is being increasingly elaborated on in enzyme biotechnology and biocatalysis. Enzymatic microreactors are a precious tool for the investigation of catalytic properties and optimization of reaction parameters in a thriving and high-yielding way. The utilization of magnetic forces in the overall microfluidic system has reinforced enzymatic processes, paving the way for novel applications in a variety of research fields. In this review, we hold a discussion on how different magnetic particles combined with the appropriate biocatalyst under the proper system configuration may constitute a powerful microsystem and provide a highly explorable scope.

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Zhao, Hua. "Effect of ions and other compatible solutes on enzyme activity, and its implication for biocatalysis using ionic liquids." Journal of Molecular Catalysis B: Enzymatic 37, no. 1-6 (December 2005): 16–25. http://dx.doi.org/10.1016/j.molcatb.2005.08.007.

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Silva, Allison R. M., Jeferson Y. N. H. Alexandre, José E. S. Souza, José G. Lima Neto, Paulo G. de Sousa Júnior, Maria V. P. Rocha, and José C. S. dos Santos. "The Chemistry and Applications of Metal–Organic Frameworks (MOFs) as Industrial Enzyme Immobilization Systems." Molecules 27, no. 14 (July 15, 2022): 4529. http://dx.doi.org/10.3390/molecules27144529.

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Enzymatic biocatalysis is a sustainable technology. Enzymes are versatile and highly efficient biocatalysts, and have been widely employed due to their biodegradable nature. However, because the three-dimensional structure of these enzymes is predominantly maintained by weaker non-covalent interactions, external conditions, such as temperature and pH variations, as well as the presence of chemical compounds, can modify or even neutralize their biological activity. The enablement of this category of processes is the result of the several advances in the areas of molecular biology and biotechnology achieved over the past two decades. In this scenario, metal–organic frameworks (MOFs) are highlighted as efficient supports for enzyme immobilization. They can be used to ‘house’ a specific enzyme, providing it with protection from environmental influences. This review discusses MOFs as structures; emphasizes their synthesis strategies, properties, and applications; explores the existing methods of using immobilization processes of various enzymes; and lists their possible chemical modifications and combinations with other compounds to formulate the ideal supports for a given application.

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Vartolomei, Ana Maria, Ioan Calinescu, Diana Madalina Dan, and Adina Ionuta Gavrila. "Enzymatic Synthesis of Isoamyl Acetate by Nanoconventional Techniques." Revista de Chimie 72, no. 4 (October 29, 2021): 35–43. http://dx.doi.org/10.37358/rc.21.4.8454.

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Chemical methods for the synthesis of esters require the use of high temperatures in the presence of chemical catalysts resulting in undesirable by-products. To avoid these problems the use of biocatalysis can lead to greener products. The aim of this papar is to study the synergism of enzyme catalysis with unconventional techniques suc as microwave or ultrasound assited processes. The effect of different reaction parameters, such as temperature, enzyme loading, ultrasonic amplitude and duty cycle, on the enzymatic synthesis of isoamyl acetate has been evaluated. To highlight the efficiency of unconventional techniques, experiments using conventional methods were also performed. The concetrations of isoamyl acetate obtained by unconventional methods were higher than those achieved under conventional heating, as 478 mgester/gmixture was obtained with ultrasounds in 1 h using 25g/L of enzyme loading, at 50ºC as compared to 387 mgester/gmixture by conventional methods. Mild process conditions and using green techniques (microwaves and ultrasounds) make the biocatalytic procedure a useful way to synthetise esters with application on food, pharmaceutical and cosmetic industries.

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Belinska, Anna, Olga Bliznjuk, Olena Shcherbak, Nataliia Masalitina, Liliia Myronenko, Oleksandra Varankina, Serhii Samoilenko, Viktoriia Borovkova, Natalya Kibenko, and Valentina Timchenko. "Improvement of fatty systems biotechnological interesterification with immobilized enzyme preparation usage." Eastern-European Journal of Enterprise Technologies 6, no. 6 (120) (December 31, 2022): 6–13. http://dx.doi.org/10.15587/1729-4061.2022.268373.

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This work research object was fat systems interesterification biotechnology using the Lipozyme TL IM immobilized enzyme preparation. The problem of enzyme preparation activation by moistening with sodium bicarbonate aqueous solution with 7.4 ... 7.7 (3 % wt.) pH was solved in the work. The obtained results made it possible to minimize the interesterification process duration with high-quality product obtaining. The proposed enzyme preparation processing made it possible to reduce the duration of the biointeresterification process in a model fat mixture (palm stearin, coconut and soybean oils in a ratio of 1:1:1, respectively) to 3.5...3.7 hours. The product with high quality indicators, namely up to 0.26 mg KOH/g acid number, up to 0.60 mmol ½ O/kg peroxide number and 1.70 c.u. anisidine number, was obtained as a result. The obtained data can be explained by a fact that effective biocatalysis with lipolytic enzymes as the protein molecules requires the existence of two phases – lipid and water. This fact was provided by the activation parameters justified in the study. The obtained results feature was possibility of enzyme preparation activation, which is not provided under industrial conditions due to the threat of raw materials and finished products hydrolytic processes, which leads to the finished product quality deterioration. The research results made it possible to minimize hydrolytic processes in fat system during interesterification with simultaneous process efficiency increase. From a practical point of view, the discovered activation mechanism made it possible to adjust the enzyme preparation processing conditions in fat systems interesterification technology. The applied aspect of scientific result using was the possibility of improving the typical technological process of fat interesterification

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Chu, Jianlin, Jiheng Yue, Song Qin, Yuqiang Li, Bin Wu, and Bingfang He. "Biocatalysis for Rare Ginsenoside Rh2 Production in High Level with Co-Immobilized UDP-Glycosyltransferase Bs-YjiC Mutant and Sucrose Synthase AtSuSy." Catalysts 11, no. 1 (January 18, 2021): 132. http://dx.doi.org/10.3390/catal11010132.

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Rare ginsenoside Rh2 exhibits diverse pharmacological effects. UDP-glycosyltransferase (UGT) catalyzed glycosylation of protopanaxadiol (PPD) has been of growing interest in recent years. UDP-glycosyltransferase Bs-YjiC coupling sucrose synthase in one-pot reaction was successfully applied to ginsenoside biosynthesis with UDP-glucose regeneration from sucrose and UDP, which formed a green and sustainable approach. In this study, the his-tagged UDP-glycosyltransferase Bs-YjiC mutant M315F and sucrose synthase AtSuSy were co-immobilized on heterofunctional supports. The affinity adsorption significantly improved the capacity of specific binding of the two recombinant enzymes, and the dual enzyme covalently cross-linked by the acetaldehyde groups significantly promoted the binding stability of the immobilized bienzyme, allowing higher substrate concentration by easing substrate inhibition for the coupled reaction. The dual enzyme amount used for ginsenoside Rh2 biosynthesis is Bs-YjiC-M315F: AtSuSy = 18 mU/mL: 25.2 mU/mL, a yield of 79.2% was achieved. The coimmobilized M315F/AtSuSy had good operational stability of repetitive usage for 10 cycles, and the yield of ginsenoside Rh2 was kept between 77.6% and 81.3%. The high titer of the ginsenoside Rh2 cumulatively reached up to 16.6 mM (10.3 g/L) using fed-batch technology, and the final yield was 83.2%. This study has established a green and sustainable approach for the production of ginsenoside Rh2 in a high level of titer, which provides promising candidates for natural drug research and development.

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Wang, Fangqin, Shu He, Changtong Zhu, Ulrich Rabausch, Wolfgang Streit, and Jun Wang. "The combined use of a continuous-flow microchannel reactor and ionic liquid cosolvent for efficient biocatalysis of unpurified recombinant enzyme." Journal of Chemical Technology & Biotechnology 93, no. 9 (April 10, 2018): 2671–80. http://dx.doi.org/10.1002/jctb.5621.

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Winnikoff, Jacob R., Telissa M. Wilson, Erik V. Thuesen, and Steven H. D. Haddock. "Enzymes feel the squeeze: biochemical adaptation to pressure in the deep sea." Biochemist 39, no. 6 (December 1, 2017): 26–29. http://dx.doi.org/10.1042/bio03906026.

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To the human observer, the deep sea is as extreme an environment as Earth has to offer. Below about 200 metres, there is no light from the surface, the water can be frigid (-2 to 5°C), oxygen and food are scarce, and the pressure is staggering. Of course, to the countless species that inhabit the deep sea, these conditions are not so extreme, and in a statistical sense, they fall fairly close to average, since the deep comprises the planet's largest habitat by volume. Despite its expanse, we know little about how life persists in an environment so different from our own. Only in the last half-century has technology emerged that allows us to collect and study live deep-sea animals. Diversity, Evolution and EcoPhysiology of Ctenophores (DEEPC, deepc.org, a US NSF-supported research effort) is opening a window on biochemistry in the deep, and specifically on its relationship to high pressure. By determining structural constraints on enzyme function under pressure, we aim to inform models focusing on deep-sea animal colonization, and to find general patterns of protein adaptation with possible applications in protein engineering and biocatalysis.

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Sharikov, Anton, Maria Amelyakina, Elena Serba, Viktor Ivanov, Darya Polivanovskaya, and Irina Abramova. "Steam Extraction System Use in the Gluten-Free Cereal Snacks Technology." Food Industry 7, no. 4 (December 21, 2022): 6–14. http://dx.doi.org/10.29141/2500-1922-2022-7-4-1.

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When developing new types of gluten-free products, the extrusion and biocatalysis technologies use is promising. Extrusion enables to obtain ready-to-eat products of the high consumer demand with a porous structure from gluten-free cereals (snacks, ready-made breakfasts, crispbreads and various types of food concentrates), without using the functional structure-forming properties of gluten. In turn, biocatalytic technologies can provide enzymatic proline and glutamine protein bond hydrolysis of structural protein domains resistant to the digestive enzyme action. The main extrusion processing problem of wheat hydrolysates with a reduced gluten amount mixed with other raw materials is the high moisture content in the extruder. The work aimed at studying the process of additional steam extraction from the extruder cabinet during the high-moisture mixtures extrusion and its influence on the quality of finished products, i.e. gluten-free snacks. The study object was rice flour and wheat hydrolysate mixtures with a mass fermentolysate fraction of 25 and 35 %, extruded using a steam extraction system. As a result of the conducted studies, a man revealed that with an increase in steam extraction, the pressure in the extruder cabinet and the shear moment significantly increased, the process temperature slightly increased. This effect is due to the moisture content decrease in the extruder cabinet after steam extraction and, accordingly, the shear deformations energy increase. There was an additional steam extraction accompanied by an increase in specific electricity consumption by 64–79 %. The texture samples analysis demonstrated that the steam extraction and the amount of hydrolysate introduced had a significant effect on the snacks texture: the hardness decreased from 10.5 to 3.5 N, while the number of micro-fractures characterizing the crispness increased from 11.4 to 13.6. The color characteristics evaluation of the obtained snacks showed their insignificant dependence on the steam extraction. The use of a steam extraction device enables to increase the hydrolysate content in the extruded mixture and improve finished products quality during high-moisture mixtures processing.

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Sharikov, A. Yu, M. V. Amelyakina, V. V. Ivanov, and D. V. Polivanovskaya. "Enzymatic hydrolysis of high gravity extruded corn starch media." Agricultural Science Euro-North-East 21, no. 4 (August 22, 2020): 425–33. http://dx.doi.org/10.30766/2072-9081.2020.21.4.425-433.

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Increase of solubles concentration in processable liquid media is one of the trends of technological development of starchy materials bioconversion. It promotes the reduction in operating costs, in heat and energy consumption and increases the efficiency of using capacitive equipment. The use of thermoplastic extrusion in the bioconversion processes as a pretreatment stage is perspective. Extrusion provides intensive gelatinization of starch with a moisture content of 15-30 % that has become a prerequisite for the development of extrusion-hydrolytic technology for obtaining of concentrated hydrolysates from starch-containing raw materials. As a part of the technology development, the effect of the key factors of biocatalysis on the formation of hydrolysis products and the rheological properties of highly concentrated hydrolysates of corn starch has been studied. The dosage of thermostable α-amylase and the concentration of the medium were taken as independent variables. The ranges of variation of the factors were set in the range of 5-13 units of amylolytic activity per 1 g of starch and 40- 60 % soluble concentration in accordance with the central orthogonal second-order design of the experiment. The value of dextrose equivalent in the area of the studied factor space varied from 23 to 40. Dynamic viscosity values were in the range from 89 to 2219 mPa·s. The analysis of the results and the mathematical model showed that an increase in the dextrose equivalent in the hydrolysis products was facilitated by a decrease of the concentration of the medium and an increase in the dosage of α-amylase. The growth dynamics of the dextrose equivalent value decreased with an excess of the dosage of the enzyme preparation of 9 units of amylolytic activity per 1 g of starch. Rheological studies have shown that a dosage of α-amylase of 1- 13 units of amylolytic activity per gram of starch at 40 % concentration of the medium provided dynamic viscosity values in the range 89-780 mPa·s, which is sufficient for the subsequent stages of hydrolyzate processing. Increasing the concentration to 50-60 % requires the introduction of α-amylase at a dosage of more than 5 units of amylolytic activity to ensure a rheologically safe process.

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Zolotarev Nikita A., Fedotova Olga B.,, Agarkova Evgeniya Yu.,, Akhremko Anastasya G.,, and Sokolova Olga V.,. "DIRECTIONAL PROTEOLYSIS OF SECONDARY RAW MATERIALS." SERIES CHEMISTRY AND TECHNOLOGY 5, no. 443 (October 15, 2020): 77–84. http://dx.doi.org/10.32014/2020.2518-1491.83.

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For the food industry, technologies for processing secondary raw materials are of interest. Curd whey is a typical complex secondary bioproduct. It has a high acidity, so it is difficult to recycle. The scope of use of curd whey is limited. There are technologies for processing whey from cheese. In the manufacture of rennet cheese, whey is formed, which is successfully processed. The technology for processing whey from cheese can only partially be applied for processing whey from cottage cheese. In particular, the use of ultrafiltration can be used for the concentration of curd whey protein. The whey protein concentrate from cottage cheese can be hydrolyzed. Curd whey after proteolytic biocatalysis has a higher potential for use in the food industry The use of hydrolyzed whey rather than native is promising. According to studies of domestic and foreign scientists, peptides of medium length (3-10 kDa) have the highest biological value. However, during hydrolysis, a proteolytic process occurs, the consequence of which is the appearance of a bitter taste due to the formation of bitter amino acids. The aim of the study was to obtain a whey protein hydrolyzate with minimally altered sensory characteristics. The problem with whey protein hydrolysis is that a bitter taste appears during hydrolysis. The aim of the study was to obtain a whey protein hydrolyzate of curd whey. The resulting hydrolyzis should not have a bitter taste, and the length of its peptides should be medium. To obtain curd whey hydrolysates with harmonized sensory characteristics, an enzyme preparation from the group of fungal proteases produced by Aspergillus oryzae was selected. The experimental data made it possible to optimize the parameters of the hydrolysis process. The results of the study and analysis confirm that the whey protein hydrolyzate has minimal changes in organoleptic characteristics compared to native serum. In the hydrolyzate there is no bitterness in the taste and aftertaste. It has been proven that the resulting peptides are of medium size.

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Yaseen, F., A. Siddique, N. Idrees, A. Fateh, R. Ahmad, A. Ali, and Ali I. "ENZYME BIOCATALYSIS IN ORGANIC SYNTHESIS." Biological and Clinical Sciences Research Journal 2021, no. 1 (June 24, 2021). http://dx.doi.org/10.54112/bcsrj.v2021i1.73.

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The factor that makes enzyme biocatalysts for organic synthesis both fascinating and challenging from a scientific standpoint is the field's higher interdisciplinarity, and which necessitates expertise from a wide range of disciplines, including microbiology, organic synthesis, molecular biology, genetics, and reaction engineering. Enzymes can now carry out a wide variety of organic reactions, including hydrolytic reactions, redox reactions, and C-C bond formations, with higher performance. Enzyme catalysis has also evolved into a widely used manufacturing technology in the chemical industry, especially in the fields of fine organic chemicals and pharmaceuticals. More advances in molecular modeling for enzyme-catalysis syntheses are expected, allowing for a greater number of biocatalytic techniques based on the enzymes that have been optimized or engineered by rationalized protein engineering. The organic chemists mostly have successfully used these custom-made biocatalysts (the isolated pure enzymes, the recombinant genetically modified microorganisms, also known as the designer cells), an important milestone in the enzyme catalysis process in organic synthesis is into generally accepted synthetic technology for academia as well as industries.

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Tian, Qikai, Jing Zhang, Jing Yan, Shaobin Zhang, and Ziyi Yu. "Enzyme Anchoring Amphiphilic Polymer Nanoparticles for Enhanced Pickering Interfacial Biocatalysis." ACS Applied Polymer Materials, January 4, 2023. http://dx.doi.org/10.1021/acsapm.2c01868.

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"New High-Throughput Screening Assays for Biocatalysis." CHIMIA 55, no. 12 (December 19, 2001): 1049. http://dx.doi.org/10.2533/chimia.2001.1049.

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High-throughput screening for catalysis is a critical technology in all experiments aimed at modifying or creating enzymes by directed evolution, as well as for biodiversity mining for new catalysts. We have developed a series of enzyme assays based on fluorogenic substrates and on fluorescent product sensors. These new assays offer the possibility to assay chemically non-activated functional groups within chiral molecules with unprecedented sensibility and selectivity. Assays are exemplified for alcohol dehydrogenases, aldolases, lipases and esterases, amidases and acylases, phosphatases, and epoxide hydrolases. The assays can also be used to isolate catalytic antibodies by screening libraries produced by immunization with transition-state analogs. These assays are suitable for microtiter plate and higher miniaturization formats.

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Kazan, Aslihan, Xihua Hu, Alina Stahl, Heike Frerichs, Irina Smirnova, and Ozlem Yesil‐Celiktas. "An enzyme immobilized microreactor for continuous‐flow biocatalysis of ginsenoside Rb1." Journal of Chemical Technology & Biotechnology, August 31, 2021. http://dx.doi.org/10.1002/jctb.6887.

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Choudhary, Malvi, Suruchi Gupta, Manoj K. Dhar, and Sanjana Kaul. "Endophytic Fungi-Mediated Biocatalysis and Biotransformations Paving the Way Toward Green Chemistry." Frontiers in Bioengineering and Biotechnology 9 (June 16, 2021). http://dx.doi.org/10.3389/fbioe.2021.664705.

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Catalysis is a process carried out in the presence of a heterogenous catalyst for accelerating the rate of a chemical reaction. It plays a pivotal role in transition from take, make, and dispose technology to sustainable technology via chemo- and biocatalytic processes. However, chemocatalyzed reactions are usually associated with copious amounts of perilous/hazardous environmental footprints. Therefore, whole-cell biotransformations or enzyme cocktails serve as cleaner biocatalytic alternatives in replacing the classical chemical procedures. These benchmark bioconversion reactions serve as important key technology in achieving the goals of green chemistry by eliminating waste generation at source. For this, nature has always been a driving force in fuelling natural product discovery and related applications. The fungal endophytic community, in particular, has undergone co-evolution with their host plant and has emerged as a powerful tool of genetic diversity. They can serve as a treasure trove of biocatalysts, catalyzing organic transformations of a wide range of substances into enantiopure compounds with biotechnological relevance. Additionally, the biocatalytic potential of endophytic fungi as whole-intact organisms/isolated enzyme systems has been greatly expanded beyond the existing boundaries with the advancement in high-throughput screening, molecular biology techniques, metabolic engineering, and protein engineering. Therefore, the present review illustrates the promising applications of endophytic fungi as biocatalysts for the synthesis of new structural analogs and pharmaceutical intermediates and refinement of existing proteins for novel chemistries.

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Birch-Price, Zachary, Christopher J. Taylor, Mary Ortmayer, and Anthony P. Green. "Engineering enzyme activity using an expanded amino acid alphabet." Protein Engineering, Design and Selection, November 12, 2022. http://dx.doi.org/10.1093/protein/gzac013.

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Abstract Enzyme design and engineering strategies are typically constrained by the limited size of nature’s genetic alphabet, comprised of only twenty canonical amino acids. In recent years, site-selective incorporation of non-canonical amino acids (ncAAs) via an expanded genetic code has emerged as a powerful means of inserting new functional components into proteins, and hundreds of structurally diverse amino acids are now available. Here, we highlight how the emergence of an expanded repertoire of amino acids has opened new avenues in enzyme design and engineering. ncAAs have been used to probe complex biological mechanisms, augment enzyme function and, most ambitiously, to embed new catalytic mechanisms into protein active sites that would be challenging to access within the constraints of nature’s genetic code. We predict that the studies reviewed in this article, along with further advances in genetic code expansion technology, will establish ncAA incorporation as an increasingly important tool for biocatalysis in the coming years.

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Küsters, Kira, Ronja Saborowski, Christian Wagner, Rebecca Hamel, Jan-Dirk Spöring, Wolfgang Wiechert, and Marco Oldiges. "Construction and characterization of BsGDH-CatIB variants and application as robust and highly active redox cofactor regeneration module for biocatalysis." Microbial Cell Factories 21, no. 1 (June 2, 2022). http://dx.doi.org/10.1186/s12934-022-01816-2.

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Abstract Background Catalytically active inclusion bodies (CatIBs) are known for their easy and cost efficient production, recyclability as well as high stability and provide an alternative purely biological technology for enzyme immobilization. Due to their ability to self-aggregate in a carrier-free, biodegradable form, no further laborious immobilization steps or additional reagents are needed. These advantages put CatIBs in a beneficial position in comparison to traditional immobilization techniques. Recent studies outlined the impact of cooperative effects of the linker and aggregation inducing tag on the activity level of CatIBs, requiring to test many combinations to find the best performing CatIB variant. Results Here, we present the formation of 14 glucose dehydrogenase CatIB variants of Bacillus subtilis, a well-known enzyme in biocatalysis due to its capability for substrate coupled regeneration of reduced cofactors with cheap substrate glucose. Nine variants revealed activity, with highest productivity levels for the more rigid PT-Linker combinations. The best performing CatIB, BsGDH-PT-CBDCell, was characterized in more detail including long-term storage at −20 °C as well as NADH cofactor regeneration performance in repetitive batch experiments with CatIB recycling. After freezing, BsGDH-PT-CBDCell CatIB only lost approx. 10% activity after 8 weeks of storage. Moreover, after 11 CatIB recycling cycles in repetitive batch operation 80% of the activity was still present. Conclusions This work presents a method for the effective formation of a highly active and long-term stable BsGDH-CatIB as an immobilized enzyme for robust and convenient NADH regeneration.

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Ryazantseva, Ksenia, Eugeniya Agarkova, and Olga Fedotova. "Continuous hydrolysis of milk proteins in membrane reactors of various configurations." Foods and Raw Materials, July 13, 2021, 271–81. http://dx.doi.org/10.21603/2308-4057-2021-2-271-281.

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Introduction. The article provides a review of technologies for membrane fractionation of various hydrolyzed food substrates in membrane bioreactors (MBR). In food industry, MBRs are popular in functional food production, especially in the processing of whey, which is a very promising raw material due to its physicochemical composition. Study objects and methods. The research was based on a direct validated analysis of scientific publications and featured domestic and foreign experience in MBR hydrolysis of protein raw material. Results and discussion. The MBR hydrolysis of proteins combines various biocatalytic and membrane processes. This technology makes it possible to intensify the biocatalysis, optimize the use of the enzyme preparation, and regulate the molecular composition of hydrolysis products. The paper reviews MBRs based on batch or continuous stirring, gradient dilution, ceramic capillary, immobilized enzyme, etc. Immobilized enzymes reduce losses that occur during the production of fractionated peptides. Continuous MBRs are the most economically profitable type, as they are based on the difference in molecular weight between the enzyme and the hydrolysis products. Conclusion. Continuous stirred tank membrane reactors have obvious advantages over other whey processing reactors. They provide prompt separation of hydrolysates with the required biological activity and make it possible to reuse enzymes.

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Kołodziejczak-Radzimska, Agnieszka, Long D. Nghiem, and Teofil Jesionowski. "Functionalized Materials as a Versatile Platform for Enzyme Immobilization in Wastewater Treatment." Current Pollution Reports, June 1, 2021. http://dx.doi.org/10.1007/s40726-021-00193-5.

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Abstract Purpose of Review Untreated wastewater discharge can significantly and negatively impact the state of the environment. Rapid industrialization and economic development have directly contributed to land and water pollution resulting from the application of many chemicals such as organic dyes, pharmaceuticals, and industrial reagents. The removal of these chemicals before effluent discharge is crucial for environmental protection. This review aims to explore the importance of functionalized materials in the preparation of biocatalytic systems and consider their application in eliminating water pollutants. Recent Findings Wastewater treatment methods can be classified into three groups: (i) chemical (e.g., chemical oxidation and ozonation), (ii) physical (e.g., membrane separation and ion exchange), and (iii) biological processes. Biological treatment is the most widely used method due to its cost-effectiveness and eco-friendliness. In particular, the use of immobilized enzymes has recently become more attractive as a result of scientific progress in advanced material synthesis. The selection of an appropriate support plays an important role in the preparation of such biologically active systems. Recent studies have demonstrated the use of various materials for enzyme immobilization in the purification of water. Summary This review identifies and discusses different biocatalytic systems used in the enzymatic degradation of various water pollutants. Materials functionalized by specific groups can serve as good support matrices for enzyme immobilization, providing chemical and thermal stability to support catalytic reactions. Enzymatic biocatalysis converts the pollutants into simpler products, which are usually less toxic than their parents. Due to immobilization, the enzyme can be used over multiple cycles to reduce the cost of wastewater treatment. Future studies in this field should focus on developing new platforms for enzyme immobilization in order to improve degradation efficiency.

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Xu, Qi, Markus Alahuhta, Patrick Hewitt, Nicholas S. Sarai, Hui Wei, Neal N. Hengge, Ashutosh Mittal, Michael E. Himmel, and Yannick J. Bomble. "Self-Assembling Metabolon Enables the Cell Free Conversion of Glycerol to 1,3-Propanediol." Frontiers in Energy Research 9 (July 15, 2021). http://dx.doi.org/10.3389/fenrg.2021.680313.

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Cell free biocatalysis is showing promise as a replacement or complement to conventional microbial biocatalysts due to the potential for achieving high yields, titers, and productivities. However, there exist several challenges that need to be addressed before its broader industrial adoption is achieved. New paradigms and innovative solutions are needed to overcome these challenges. In this study we demonstrate high levels of glycerol conversion to 1,3-propanediol using a self-assembling metabolic pathway leveraging the arraying strategy (protein scaffolds) used by thermophilic cellulolytic bacteria to assemble their biomass degrading enzymes. These synthetic metabolons were capable of producing 1,3-PDO at a yield more than 95% at lower glycerol concentration and close to 70% at higher concentrations at a higher productivity rate than the equivalent microbial strain. One of the benefits of our approach is the fact that no enzyme purification is required, and that the assembly of the complex is accomplished in vivo before immobilization, while product formation is conducted in vitro. We also report the recovery of enzymatic activity upon fusion enzymes binding to these protein scaffolds, which could have broader applications when assembling arrayed protein complexes.

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

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