Journal articles: 'Biocatalysis – Industrial applications'

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Hecht, Katrin, Hans-Peter Meyer, Roland Wohlgemuth, and Rebecca Buller. "Biocatalysis in the Swiss Manufacturing Environment." Catalysts 10, no. 12 (December 4, 2020): 1420. http://dx.doi.org/10.3390/catal10121420.

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Biocatalysis has undergone a remarkable transition in the last two decades, from being considered a niche technology to playing a much more relevant role in organic synthesis today. Advances in molecular biology and bioinformatics, and the decreasing costs for gene synthesis and sequencing contribute to the growing success of engineered biocatalysts in industrial applications. However, the incorporation of biocatalytic process steps in new or established manufacturing routes is not always straightforward. To realize the full synthetic potential of biocatalysis for the sustainable manufacture of chemical building blocks, it is therefore important to regularly analyze the success factors and existing hurdles for the implementation of enzymes in large scale small molecule synthesis. Building on our previous analysis of biocatalysis in the Swiss manufacturing environment, we present a follow-up study on how the industrial biocatalysis situation in Switzerland has evolved in the last four years. Considering the current industrial landscape, we record recent advances in biocatalysis in Switzerland as well as give suggestions where enzymatic transformations may be valuably employed to address some of the societal challenges we face today, particularly in the context of the current Coronavirus disease 2019 (COVID-19) pandemic.

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Kuo, Chia-Hung, and Chwen-Jen Shieh. "Biocatalytic Process Optimization." Catalysts 10, no. 11 (November 12, 2020): 1303. http://dx.doi.org/10.3390/catal10111303.

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Biocatalysis refers to the use of microorganisms and enzymes in chemical reactions, has become increasingly popular and is frequently used in industrial applications due to the high efficiency and selectivity of biocatalysts [...]

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Littlechild, Jennifer A. "Archaeal Enzymes and Applications in Industrial Biocatalysts." Archaea 2015 (2015): 1–10. http://dx.doi.org/10.1155/2015/147671.

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Archaeal enzymes are playing an important role in industrial biotechnology. Many representatives of organisms living in “extreme” conditions, the so-called Extremophiles, belong to the archaeal kingdom of life. This paper will review studies carried by the Exeter group and others regarding archaeal enzymes that have important applications in commercial biocatalysis. Some of these biocatalysts are already being used in large scale industrial processes for the production of optically pure drug intermediates and amino acids and their analogues. Other enzymes have been characterised at laboratory scale regarding their substrate specificity and properties for potential industrial application. The increasing availability of DNA sequences from new archaeal species and metagenomes will provide a continuing resource to identify new enzymes of commercial interest using both bioinformatics and screening approaches.

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Sime, John T. "Applications of Biocatalysis to Industrial Processes." Journal of Chemical Education 76, no. 12 (December 1999): 1658. http://dx.doi.org/10.1021/ed076p1658.

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Wu, Shuke, Radka Snajdrova, Jeffrey C. Moore, Kai Baldenius, and Uwe T. Bornscheuer. "Biocatalysis: Enzymatic Synthesis for Industrial Applications." Angewandte Chemie International Edition 60, no. 1 (August 17, 2020): 88–119. http://dx.doi.org/10.1002/anie.202006648.

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Trincone, Antonio. "Application-Oriented Marine Isomerases in Biocatalysis." Marine Drugs 18, no. 11 (November 21, 2020): 580. http://dx.doi.org/10.3390/md18110580.

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The class EC 5.xx, a group of enzymes that interconvert optical, geometric, or positional isomers are interesting biocatalysts for the synthesis of pharmaceuticals and pharmaceutical intermediates. This class, named “isomerases,” can transform cheap biomolecules into expensive isomers with suitable stereochemistry useful in synthetic medicinal chemistry, and interesting cases of production of l-ribose, d-psicose, lactulose, and d-phenylalanine are known. However, in two published reports about potential biocatalysts of marine origin, isomerases are hardly mentioned. Therefore, it is of interest to deepen the knowledge of these biocatalysts from the marine environment with this specialized in-depth analysis conducted using a literature search without time limit constraints. In this review, the focus is dedicated mainly to example applications in biocatalysis that are not numerous confirming the general view previously reported. However, from this overall literature analysis, curiosity-driven scientific interest for marine isomerases seems to have been long-standing. However, the major fields in which application examples are framed are placed at the cutting edge of current biotechnological development. Since these enzymes can offer properties of industrial interest, this will act as a promoter for future studies of marine-originating isomerases in applied biocatalysis.

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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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Santi, Micol, Luca Sancineto, Vanessa Nascimento, Juliano Braun Azeredo, Erika V. M. Orozco, Leandro H. Andrade, Harald Gröger, and Claudio Santi. "Flow Biocatalysis: A Challenging Alternative for the Synthesis of APIs and Natural Compounds." International Journal of Molecular Sciences 22, no. 3 (January 20, 2021): 990. http://dx.doi.org/10.3390/ijms22030990.

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Biocatalysts represent an efficient, highly selective and greener alternative to metal catalysts in both industry and academia. In the last two decades, the interest in biocatalytic transformations has increased due to an urgent need for more sustainable industrial processes that comply with the principles of green chemistry. Thanks to the recent advances in biotechnologies, protein engineering and the Nobel prize awarded concept of direct enzymatic evolution, the synthetic enzymatic toolbox has expanded significantly. In particular, the implementation of biocatalysts in continuous flow systems has attracted much attention, especially from industry. The advantages of flow chemistry enable biosynthesis to overcome well-known limitations of “classic” enzymatic catalysis, such as time-consuming work-ups and enzyme inhibition, as well as difficult scale-up and process intensifications. Moreover, continuous flow biocatalysis provides access to practical, economical and more sustainable synthetic pathways, an important aspect for the future of pharmaceutical companies if they want to compete in the market while complying with European Medicines Agency (EMA), Food and Drug Administration (FDA) and green chemistry requirements. This review focuses on the most recent advances in the use of flow biocatalysis for the synthesis of active pharmaceutical ingredients (APIs), pharmaceuticals and natural products, and the advantages and limitations are discussed.

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Volmer, Jan, Christoph Neumann, Bruno Bühler, and Andreas Schmid. "Engineering of Pseudomonas taiwanensis VLB120 for Constitutive Solvent Tolerance and Increased Specific Styrene Epoxidation Activity." Applied and Environmental Microbiology 80, no. 20 (August 15, 2014): 6539–48. http://dx.doi.org/10.1128/aem.01940-14.

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ABSTRACTThe application of whole cells as biocatalysts is often limited by the toxicity of organic solvents, which constitute interesting substrates/products or can be used as a second phase forin situproduct removal and as tools to control multistep biocatalysis. Solvent-tolerant bacteria, especiallyPseudomonasstrains, are proposed as promising hosts to overcome such limitations due to their inherent solvent tolerance mechanisms. However, potential industrial applications suffer from tedious, unproductive adaptation processes, phenotypic variability, and instable solvent-tolerant phenotypes. In this study, genes described to be involved in solvent tolerance were identified inPseudomonastaiwanensisVLB120, and adaptive solvent tolerance was proven by cultivation in the presence of 1% (vol/vol) toluene. Deletion ofttgV, coding for the specific transcriptional repressor of solvent efflux pump TtgGHI gene expression, led to constitutively solvent-tolerant mutants ofP. taiwanensisVLB120 and VLB120ΔC. Interestingly, the increased amount of solvent efflux pumps enhanced not only growth in the presence of toluene and styrene but also the biocatalytic performance in terms of stereospecific styrene epoxidation, although proton-driven solvent efflux is expected to compete with the styrene monooxygenase for metabolic energy. Compared to that of theP. taiwanensisVLB120ΔCparent strain, the maximum specific epoxidation activity ofP. taiwanensisVLB120ΔCΔttgVdoubled to 67 U/g of cells (dry weight). This study shows that solvent tolerance mechanisms, e.g., the solvent efflux pump TtgGHI, not only allow for growth in the presence of organic compounds but can also be used as tools to improve redox biocatalysis involving organic solvents.

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Guo, Fei, and Per Berglund. "Transaminase biocatalysis: optimization and application." Green Chemistry 19, no. 2 (2017): 333–60. http://dx.doi.org/10.1039/c6gc02328b.

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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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Guajardo, Nadia, and Pablo Domínguez de María. "Production of Bulk Chemicals with Biocatalysis: Drivers and Challenges Reflected in Recent Industrial Granted Patents (2015–2020)." Molecules 26, no. 3 (January 31, 2021): 736. http://dx.doi.org/10.3390/molecules26030736.

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The application of biocatalysis and White Biotechnology tools in chemical areas concerning the production of bulk compounds and other related low-added value products (with high volumes) has been gaining importance in recent years. The expected drivers of biocatalysis for these sectors are energy savings, regioselectivity (leading to cleaner products), the possibility of using thermolabile substrates, as well as the generation of less by-products and manageable wastes. This paper explores some recent industrial granted patents related to biocatalysis and bulk chemicals. Several patents have been identified in fields such as biodiesel and esterification reactions, and sugar or furan chemistry. Overall, innovative strategies involve the identification of novel enzymes, the set-up of improved immobilization methods, as well as novel reactor designs that can offer improved performances and economics. The reported examples indicate that biocatalysis can certainly offer opportunities for these areas as well, far from the typical pharmaceutical and fine chemical applications often reported in the literature.

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Burek, B. O., S. Bormann, F. Hollmann, J. Z. Bloh, and D. Holtmann. "Hydrogen peroxide driven biocatalysis." Green Chemistry 21, no. 12 (2019): 3232–49. http://dx.doi.org/10.1039/c9gc00633h.

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Peroxyzymes – biocatalysts utilizing environmentally benign hydrogen peroxide as a co-substrate – are a promising class of enzymes catalyzing a variety of important C–H and CC oxidations. This review critically examines recent developments in this field and the opportunities for industrial applications.

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Domínguez de María, Pablo. "Biocatalysis, sustainability, and industrial applications: Show me the metrics." Current Opinion in Green and Sustainable Chemistry 31 (October 2021): 100514. http://dx.doi.org/10.1016/j.cogsc.2021.100514.

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Choi, Jung-Min, Sang-Soo Han, and Hak-Sung Kim. "Industrial applications of enzyme biocatalysis: Current status and future aspects." Biotechnology Advances 33, no. 7 (November 2015): 1443–54. http://dx.doi.org/10.1016/j.biotechadv.2015.02.014.

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Tether, Angela L., Garry Laverty, Alberto V. Puga, Kenneth R. Seddon, Brendan F. Gilmore, and Stephen A. Kelly. "High-throughput toxicity screening of novel azepanium and 3-methylpiperidinium ionic liquids." RSC Advances 10, no. 39 (2020): 22864–70. http://dx.doi.org/10.1039/d0ra03107k.

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Ionic liquids have been employed as potentially environmentally friendly replacements for organic solvents, but have also been studied for their use in bioelectrochemical applications, such as bioenergy production, or in industrial biocatalysis.

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Toogood, Helen S., and Nigel S. Scrutton. "Discovery, Characterization, Engineering, and Applications of Ene-Reductases for Industrial Biocatalysis." ACS Catalysis 8, no. 4 (March 20, 2018): 3532–49. http://dx.doi.org/10.1021/acscatal.8b00624.

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Rodrigues, Carlos J. C., and Carla C. C. R. de Carvalho. "Marine Bioprospecting, Biocatalysis, and Process Development." Microorganisms 10, no. 10 (October 5, 2022): 1965. http://dx.doi.org/10.3390/microorganisms10101965.

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Oceans possess tremendous diversity in microbial life. The enzymatic machinery that marine bacteria present is the result of extensive evolution to assist cell survival under the harsh and continuously changing conditions found in the marine environment. Several bacterial cells and enzymes are already used at an industrial scale, but novel biocatalysts are still needed for sustainable industrial applications, with benefits for both public health and the environment. Metagenomic techniques have enabled the discovery of novel biocatalysts, biosynthetic pathways, and microbial identification without their cultivation. However, a key stage for application of novel biocatalysts is the need for rapid evaluation of the feasibility of the bioprocess. Cultivation of not-yet-cultured bacteria is challenging and requires new methodologies to enable growth of the bacteria present in collected environmental samples, but, once a bacterium is isolated, its enzyme activities are easily measured. High-throughput screening techniques have also been used successfully, and innovative in vitro screening platforms to rapidly identify relevant enzymatic activities continue to improve. Small-scale approaches and process integration could improve the study and development of new bioprocesses to produce commercially interesting products. In this work, the latest studies related to i. the growth of marine bacteria under laboratorial conditions, ii. screening techniques for bioprospecting, and iii. bioprocess development using microreactors and miniaturized systems are reviewed and discussed.

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Kazimírová, Veronika, and Martin Rebroš. "Production of Aldehydes by Biocatalysis." International Journal of Molecular Sciences 22, no. 9 (May 6, 2021): 4949. http://dx.doi.org/10.3390/ijms22094949.

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The production of aldehydes, highly reactive and toxic chemicals, brings specific challenges to biocatalytic processes. Absence of natural accumulation of aldehydes in microorganisms has led to a combination of in vitro and in vivo strategies for both, bulk and fine production. Advances in genetic and metabolic engineering and implementation of computational techniques led to the production of various enzymes with special requirements. Cofactor synthesis, post-translational modifications and structure engineering are applied to prepare active enzymes for one-step or cascade reactions. This review presents the highlights in biocatalytical production of aldehydes with the potential to shape future industrial applications.

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Bhatt, Ashish, Darshankumar Prajapati, and Akshaya Gupte. "Current Status and Future of Nitrile Catalysis using Key Nitrilases Enzymes and their Biotechnological Impact." Open Biotechnology Journal 15, no. 1 (August 27, 2021): 71–81. http://dx.doi.org/10.2174/1874070702115010071.

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Nitriles are organic compounds consisting of −C≡N group. They are frequently known to occur in nature and as intermediate by-products and waste products of various chemical, pharmaceutical, and agricultural industries. They are also found in fruit pits, cabbage, cauliflower, and sprouts, which are released upon hydrolysis. Nitrile converting enzymes like nitrilases have been extracted from microorganisms and plants. Nitrilase-mediated biocatalysis reactions have continuously aroused widespread interest to scientists and entrepreneurs in organic synthesis. Nitrile converting biocatalysts (Nitrilases) are now of substantial industrial interest from the perspective of treating toxic nitrile and cyanide-containing compounds. Nitrile degrading enzymes generally consist of nitrilases and amidases. The aim of the current review is to summarize the recent advancements on regioselective nitrilases concerning their fundamental researches and their application in the synthesis of series of high-value fine chemicals and pharmaceuticals. The present review also focuses on the utility of nitrile converting enzyme, sources, properties, classification, structure, and applications as well.

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Hasan, Khomaini. "A mini review of haloalkane dehalogenase: From molecular characterization to applications." Communications in Science and Technology 3, no. 1 (June 14, 2018): 15–18. http://dx.doi.org/10.21924/cst.3.1.2018.70.

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Haloalkane dehalogenases (HLDs) are hydrolytic enzymes that catalyze a removal of halogenated species in many toxic halogenated compounds. These enzymes belong to hydrolase family that mostly adopt a typically a/b hydrolase structure. They have many potential applications, such as industrial biocatalysis, pharmaceutics, biosensors, or detoxification of chemical weapons. In this review, structure, mechanism and applications of these enzymes will be discussed.

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Yang, Yan, Min-Zhi Liu, Yun-Song Cao, Chang-Kun Li, and Wei Wang. "Low-Level Organic Solvents Improve Multienzyme Whole-Cell Catalytic Synthesis of Myricetin-7-O-Glucuronide." Catalysts 9, no. 11 (November 18, 2019): 970. http://dx.doi.org/10.3390/catal9110970.

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Multienzyme whole-cell biocatalysts are preferred in industrial applications, and two major concerns regarding the use of these biocatalysts, cell viability and cell membrane integrity, must be addressed. In this work, the transformation of myricetin to myricetin-7-O-glucuronide catalyzed by an engineered Escherichia coli strain was taken as the model reaction to examine the impacts of low-level organic solvents on whole-cell biocatalysis. Low-level organic solvents (2%, v/v) showed a significant increase (roughly 13-fold) in myricetin-7-O-glucuronide yields. No obvious compromises of cellular viability and integrity were observed by a flow cytometry assay or in the determination of extracellular protein leakage, suggesting the addition of low-level organic solvents accommodates whole E. coli cells. Furthermore, a scaled-up reaction was conducted to test the capability and efficiency of whole-cell catalysis in the presence of organic solvents. This study presents a promising and simple means to enhance the productivity of multienzyme whole-cell catalysis without losing the barrier functions of the cell membrane.

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Bassanini, Ivan, Erica Elisa Ferrandi, Sergio Riva, and Daniela Monti. "Biocatalysis with Laccases: An Updated Overview." Catalysts 11, no. 1 (December 28, 2020): 26. http://dx.doi.org/10.3390/catal11010026.

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Laccases are multicopper oxidases, which have been widely investigated in recent decades thanks to their ability to oxidize organic substrates to the corresponding radicals while producing water at the expense of molecular oxygen. Besides their successful (bio)technological applications, for example, in textile, petrochemical, and detoxifications/bioremediations industrial processes, their synthetic potentialities for the mild and green preparation or selective modification of fine chemicals are of outstanding value in biocatalyzed organic synthesis. Accordingly, this review is focused on reporting and rationalizing some of the most recent and interesting synthetic exploitations of laccases. Applications of the so-called laccase-mediator system (LMS) for alcohol oxidation are discussed with a focus on carbohydrate chemistry and natural products modification as well as on bio- and chemo-integrated processes. The laccase-catalyzed Csp2-H bonds activation via monoelectronic oxidation is also discussed by reporting examples of enzymatic C-C and C-O radical homo- and hetero-couplings, as well as of aromatic nucleophilic substitutions of hydroquinones or quinoids. Finally, the laccase-initiated domino/cascade synthesis of valuable aromatic (hetero)cycles, elegant strategies widely documented in the literature across more than three decades, is also presented.

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Nicotra, Francesco, and Mary Garson. "Preface." Pure and Applied Chemistry 80, no. 8 (January 1, 2008): vi. http://dx.doi.org/10.1351/pac20088008vi.

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In August 2007, IUPAC‚ Organic and Biomolecular Chemistry Division launched a combined Biomolecular-Biotechnology Symposium as a major component of the 41st IUPAC Congress in Turin, Italy. This four-day CHEM-BIO-TECH 2007 Symposium comprised IUPAC‚ 1st Symposium on Biotechnology held jointly with IUPAC‚ 8th Symposium on Bioorganic Chemistry, ISBOC-8.In designing the program, the goal was to focus on work at the interface of biotechnology and biomolecular chemistry from which many key industrial and academic advances have sprung. The program embraced topics ranging from novel drug discovery, biosynthesis, biocatalysis, and organic synthesis through artificial biomolecules and other emerging biotechnological applications. Attention was also devoted to industrial experience in drug research and in biotechnological productions.The special topics discussed during the symposium included:- natural products synthesis, biosynthesis, and isolation- industrial application of bioorganic chemistry and biotechnology- bioorganic and bioinorganic chemistry, biosynthesis, and biocatalysis- analytical methods applied to molecular recognitionThis issue of Pure and Applied Chemistry comprises a collection of 11 papers based upon the invited lectures delivered at CHEM-BIO-TECH 2007. It offers readers an enduring record of the representative scientific contributions announced during the symposium, in an area of interface between chemistry and biology of great interest and relevant potential applications.Francesco Nicotra and Mary GarsonConference Chair and Co-chair

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Toogood, Helen S., and Nigel S. Scrutton. "Correction to “Discovery, Characterization, Engineering and Applications of Ene-Reductases for Industrial Biocatalysis”." ACS Catalysis 8, no. 5 (April 13, 2018): 4333. http://dx.doi.org/10.1021/acscatal.8b01375.

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Curci, Nicola, Andrea Strazzulli, Roberta Iacono, Federica De Lise, Luisa Maurelli, Mauro Di Fenza, Beatrice Cobucci-Ponzano, and Marco Moracci. "Xyloglucan Oligosaccharides Hydrolysis by Exo-Acting Glycoside Hydrolases from Hyperthermophilic Microorganism Saccharolobus solfataricus." International Journal of Molecular Sciences 22, no. 7 (March 24, 2021): 3325. http://dx.doi.org/10.3390/ijms22073325.

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In the field of biocatalysis and the development of a bio-based economy, hemicellulases have attracted great interest for various applications in industrial processes. However, the study of the catalytic activity of the lignocellulose-degrading enzymes needs to be improved to achieve the efficient hydrolysis of plant biomasses. In this framework, hemicellulases from hyperthermophilic archaea show interesting features as biocatalysts and provide many advantages in industrial applications thanks to their stability in the harsh conditions encountered during the pretreatment process. However, the hemicellulases from archaea are less studied compared to their bacterial counterpart, and the activity of most of them has been barely tested on natural substrates. Here, we investigated the hydrolysis of xyloglucan oligosaccharides from two different plants by using, both synergistically and individually, three glycoside hydrolases from Saccharolobus solfataricus: a GH1 β-gluco-/β-galactosidase, a α-fucosidase belonging to GH29, and a α-xylosidase from GH31. The results showed that the three enzymes were able to release monosaccharides from xyloglucan oligosaccharides after incubation at 65 °C. The concerted actions of β-gluco-/β-galactosidase and the α-xylosidase on both xyloglucan oligosaccharides have been observed, while the α-fucosidase was capable of releasing all α-linked fucose units from xyloglucan from apple pomace, representing the first GH29 enzyme belonging to subfamily A that is active on xyloglucan.

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Schwarz, Jenny, Katrin Rosenthal, Radka Snajdrova, Matthias Kittelmann, and Stephan Lütz. "The Development of Biocatalysis as a Tool for Drug Discovery." CHIMIA International Journal for Chemistry 74, no. 5 (May 27, 2020): 368–77. http://dx.doi.org/10.2533/chimia.2020.368.

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Enzymes are versatile biocatalysts capable of performing selective reactions. The advantages of enzymes in comparison to classical chemistry including chemical catalysts are the generally milder process conditions and avoidance of harmful reactants. Their high selectivity and specificity are especially beneficial for the enzymatic synthesis of new products with potential applications in drug research. Therefore, in the past decades, the utilization of isolated enzymes or whole-cell biocatalysts has spread through a growing number of biotechnological industries. The applications comprise the production of chiral building blocks for the pharmaceutical and fine chemical industry, the enzymatic synthesis of drug metabolites for testing of toxicity, function, biological activity, degradation and the production of biocatalytically modified natural products, which all play a role in drug discovery. Especially Oreste Ghisalba's contributions, which paved the way for the industrial use of enzymes, will be considered in this review.

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Bié, Joaquim, Bruno Sepodes, Pedro C. B. Fernandes, and Maria H. L. Ribeiro. "Enzyme Immobilization and Co-Immobilization: Main Framework, Advances and Some Applications." Processes 10, no. 3 (March 1, 2022): 494. http://dx.doi.org/10.3390/pr10030494.

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Enzymes are outstanding (bio)catalysts, not solely on account of their ability to increase reaction rates by up to several orders of magnitude but also for the high degree of substrate specificity, regiospecificity and stereospecificity. The use and development of enzymes as robust biocatalysts is one of the main challenges in biotechnology. However, despite the high specificities and turnover of enzymes, there are also drawbacks. At the industrial level, these drawbacks are typically overcome by resorting to immobilized enzymes to enhance stability. Immobilization of biocatalysts allows their reuse, increases stability, facilitates process control, eases product recovery, and enhances product yield and quality. This is especially important for expensive enzymes, for those obtained in low fermentation yield and with relatively low activity. This review provides an integrated perspective on (multi)enzyme immobilization that abridges a critical evaluation of immobilization methods and carriers, biocatalyst metrics, impact of key carrier features on biocatalyst performance, trends towards miniaturization and detailed illustrative examples that are representative of biocatalytic applications promoting sustainability.

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Ran, Ningqing, Lishan Zhao, Zhenming Chen, and Junhua Tao. "Recent applications of biocatalysis in developing green chemistry for chemical synthesis at the industrial scale." Green Chem. 10, no. 4 (2008): 361–72. http://dx.doi.org/10.1039/b716045c.

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Garcia, Sergio, and Cong T. Trinh. "Comparison of Multi-Objective Evolutionary Algorithms to Solve the Modular Cell Design Problem for Novel Biocatalysis." Processes 7, no. 6 (June 11, 2019): 361. http://dx.doi.org/10.3390/pr7060361.

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A large space of chemicals with broad industrial and consumer applications could be synthesized by engineered microbial biocatalysts. However, the current strain optimization process is prohibitively laborious and costly to produce one target chemical and often requires new engineering efforts to produce new molecules. To tackle this challenge, modular cell design based on a chassis strain that can be combined with different product synthesis pathway modules has recently been proposed. This approach seeks to minimize unexpected failure and avoid task repetition, leading to a more robust and faster strain engineering process. In our previous study, we mathematically formulated the modular cell design problem based on the multi-objective optimization framework. In this study, we evaluated a library of state-of-the-art multi-objective evolutionary algorithms (MOEAs) to identify the most effective method to solve the modular cell design problem. Using the best MOEA, we found better solutions for modular cells compatible with many product synthesis modules. Furthermore, the best performing algorithm could provide better and more diverse design options that might help increase the likelihood of successful experimental implementation. We identified key parameter configurations to overcome the difficulty associated with multi-objective optimization problems with many competing design objectives. Interestingly, we found that MOEA performance with a real application problem, e.g., the modular strain design problem, does not always correlate with artificial benchmarks. Overall, MOEAs provide powerful tools to solve the modular cell design problem for novel biocatalysis.

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de Sousa, Ronaldo Rodrigues, Rui de Paula Vieira de Castro, Nadinne Medeiros Assis, Ayla Sant’Ana da Silva, Denise Maria Guimarães Freire, Roberto Fernandez-Lafuente, and Viridiana Santana Ferreira-Leitão. "Technical–Economic Assessment—The Missing Piece for Increasing the Attractiveness of Applied Biocatalysis in Ester Syntheses?" Catalysts 13, no. 2 (January 18, 2023): 223. http://dx.doi.org/10.3390/catal13020223.

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Although the current literature describes significant advances in biocatalytic ester syntheses, few industrial plants worldwide are currently producing esters using biocatalysts. Green and sustainable esters can be obtained via a biocatalytic route, including some operational advantages over conventional syntheses. An analysis of the literature revealed that most articles neglect or describe the economic issues generically, without quantitative information. Scaling-up studies are also scarce in this field. The main disadvantage of biocatalysis using immobilized lipases—their cost—has not been studied at the same level of depth as other technical aspects. This gap in the literature is less intense in enzymatic biodiesel production studies and, despite the lack of a strict correlation, enzymatic biodiesel commercial plants are relatively more common. Preliminary techno-economic assessments are crucial to identify and circumvent the economic drawbacks of biocatalytic ester syntheses, opening the way to broader application of this technology in a large-scale context.

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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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Mohamed, Nehal Farouk, Mohamed Ibrahim Abdul Mutalib, Mohammad Azmi Bustam, Jean Marc Leveque, and Mohanad El-Harabawi. "Ecotoxicity of Pyridinium Based Ionic Liquids: A Review." Applied Mechanics and Materials 625 (September 2014): 152–55. http://dx.doi.org/10.4028/www.scientific.net/amm.625.152.

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Ionic Liquids (ILs) are an exciting class of compounds with unique properties that make them attractive for industrial applications. Pyridinium-based ILs have been used in many applications, such as organic synthesis, electrochemical applications, biocatalysis, and polymerization. Although intensive information and data regarding to the physical and thermodynamic properties of ILs have been reported and continuously published, only limited data with regards to the toxicity and ecotoxicity of ILs were reported. Toxicity tests are conducted against many aquatic organisms such as: Guppy fish, Gold fish, and Zebra fish, besides many different strains of Microorganisms such as: Staphylococcus aureus, E. coli, and Salmonella typhi, and yet more research regarding the toxicity of ionic liquids is yet to be conducted to increase the toxicity profile for these valuable chemicals.

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Dadashipour, Mohammad, Yuko Ishida, Kazunori Yamamoto, and Yasuhisa Asano. "Discovery and molecular and biocatalytic properties of hydroxynitrile lyase from an invasive millipede,Chamberlinius hualienensis." Proceedings of the National Academy of Sciences 112, no. 34 (August 10, 2015): 10605–10. http://dx.doi.org/10.1073/pnas.1508311112.

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Hydroxynitrile lyase (HNL) catalyzes the degradation of cyanohydrins and causes the release of hydrogen cyanide (cyanogenesis). HNL can enantioselectively produce cyanohydrins, which are valuable building blocks for the synthesis of fine chemicals and pharmaceuticals, and is used as an important biocatalyst in industrial biotechnology. Currently, HNLs are isolated from plants and bacteria. Because industrial biotechnology requires more efficient and stable enzymes for sustainable development, we must continuously explore other potential enzyme sources for the desired HNLs. Despite the abundance of cyanogenic millipedes in the world, there has been no precise study of the HNLs from these arthropods. Here we report the isolation of HNL from the cyanide-emitting invasive millipedeChamberlinius hualienensis, along with its molecular properties and application in biocatalysis. The purified enzyme displays a very high specific activity in the synthesis of mandelonitrile. It is a glycosylated homodimer protein and shows no apparent sequence identity or homology with proteins in the known databases. It shows biocatalytic activity for the condensation of various aromatic aldehydes with potassium cyanide to produce cyanohydrins and has high stability over a wide range of temperatures and pH values. It catalyzes the synthesis of (R)-mandelonitrile from benzaldehyde with a 99% enantiomeric excess, without using any organic solvents. Arthropod fauna comprise 80% of terrestrial animals. We propose that these animals can be valuable resources for exploring not only HNLs but also diverse, efficient, and stable biocatalysts in industrial biotechnology.

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Gheorghita, Giulia Roxana, Victoria Ioana Paun, Simona Neagu, Gabriel-Mihai Maria, Madalin Enache, Cristina Purcarea, Vasile I. Parvulescu, and Madalina Tudorache. "Cold-Active Lipase-Based Biocatalysts for Silymarin Valorization through Biocatalytic Acylation of Silybin." Catalysts 11, no. 11 (November 17, 2021): 1390. http://dx.doi.org/10.3390/catal11111390.

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Extremophilic biocatalysts represent an enhanced solution in various industrial applications. Integrating enzymes with high catalytic potential at low temperatures into production schemes such as cold-pressed silymarin processing not only brings value to the silymarin recovery from biomass residues, but also improves its solubility properties for biocatalytic modification. Therefore, a cold-active lipase-mediated biocatalytic system has been developed for silybin acylation with methyl fatty acid esters based on the extracellular protein fractions produced by the psychrophilic bacterial strain Psychrobacter SC65A.3 isolated from Scarisoara Ice Cave (Romania). The extracellular production of the lipase fraction was enhanced by 1% olive-oil-enriched culture media. Through multiple immobilization approaches of the cold-active putative lipases (using carbodiimide, aldehyde-hydrazine, or glutaraldehyde coupling), bio-composites (S1–5) with similar or even higher catalytic activity under cold-active conditions (25 °C) have been synthesized by covalent attachment to nano-/micro-sized magnetic or polymeric resin beads. Characterization methods (e.g., FTIR DRIFT, SEM, enzyme activity) strengthen the biocatalysts’ settlement and potential. Thus, the developed immobilized biocatalysts exhibited between 80 and 128% recovery of the catalytic activity for protein loading in the range 90–99% and this led to an immobilization yield up to 89%. The biocatalytic acylation performance reached a maximum of 67% silybin conversion with methyl decanoate acylating agent and nano-support immobilized lipase biocatalyst.

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Chen, Huayou, Jawad Ullah, and Jinru Jia. "Progress in Bacillus subtilis Spore Surface Display Technology towards Environment, Vaccine Development, and Biocatalysis." Journal of Molecular Microbiology and Biotechnology 27, no. 3 (2017): 159–67. http://dx.doi.org/10.1159/000475177.

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Spore surface display is the most desirable with enhanced effects, low cost, less time consuming and the most promising technology for environmental, medical, and industrial development. Spores have various applications in industry due to their ability to survive in harsh industrial processes including heat resistance, alkaline tolerance, chemical tolerance, easy recovery, and reusability. Yeast and bacteria, including gram-positive and -negative, are the most frequently used organisms for the display of various proteins (eukaryotic and prokaryotic), but unlike spores, they can rupture easily due to nutritive properties, susceptibility to heat, pH, and chemicals. Hence, spores are the best choice to avoid these problems, and they have various applications over nonspore formers due to amenability for laboratory purposes. Various strains of Clostridium and Bacillus are spore formers, but the most suitable choice for display is Bacillus subtilis because, according to the WHO, it is safe to humans and considered as “GRAS” (generally recognized as safe). This review focuses on the application of spore surface display towards industries, vaccine development, the environment, and peptide library construction, with cell surface display for enhanced protein expression and high enzymatic activity. Different vectors, coat proteins, and statistical analyses can be used for linker selection to obtain greater expression and high activity of the displayed protein.

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Ramzi, Ahmad Bazli, Matthlessa Matthew Minggu, Ummul Syafiqah Ruslan, Fikri Khairi Mohamad Hazwan, and Peer Mohamed Abdul. "Expression of Furfural Reductase Improved Furfural Tolerance in Antarctic Bacterium Pseudomonas extremaustralis." Sains Malaysiana 51, no. 10 (October 31, 2022): 3163–70. http://dx.doi.org/10.17576/jsm-2022-5110-04.

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Whole-cell biocatalysis using Antarctic bacteria is presently hampered by a lack of genetic information, limited gene tools and critically, a poor range of cultivation conditions. In this work, biological engineering strategy was employed for developing Pseudomonas extremaustralis, a metabolically-versatile and biopolymer-producing Antarctic bacterium, as a new whole-cell biocatalytic host. For this purpose, gene cloning and plasmid construction were carried out for overexpression of furfural reductase (FucO), an industrially-important enzyme for degradation of toxic furfural compound commonly found in lignocellulosic biorefinery. FucO gene from Escherichia coli BL21 was cloned in pJM105 plasmid and transformed into competent cells of P. extremaustralis to generate a biologically-engineered pFucO strain. For functional characterization of the enzyme, furfural reductase activity was assayed, where the P. extremaustralis pFucO strain exhibited increased furfural reductase activity of about 15.6 U/mg, an 18.8-fold higher than empty plasmid-carrying control pJM105 strain (0.83 U/mg). Furfural detoxification activity using whole cells was also determined by which the overexpression of FucO led to increased tolerance and cell growth with an OD600 value of 5.3 as compared to the control pJM105 strain that was inhibited with 10 mM furfural during 48-hour cultivation. Therefore, the findings obtained in this study successfully demonstrated the development of P. extremaustralis as biocatalytic host for the production of recombinant furfural reductase. The bioengineering would serve as a modular biotechnological platform for polar strain and bioproduct development tailored towards industrial biotechnology applications.

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Cavalcante, Francisco T. T., Antônio L. G. Cavalcante, Isamayra G. de Sousa, Francisco S. Neto, and José C. S. dos Santos. "Current Status and Future Perspectives of Supports and Protocols for Enzyme Immobilization." Catalysts 11, no. 10 (October 11, 2021): 1222. http://dx.doi.org/10.3390/catal11101222.

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The market for industrial enzymes has witnessed constant growth, which is currently around 7% a year, projected to reach $10.5 billion in 2024. Lipases are hydrolase enzymes naturally responsible for triglyceride hydrolysis. They are the most expansively used industrial biocatalysts, with wide application in a broad range of industries. However, these biocatalytic processes are usually limited by the low stability of the enzyme, the half-life time, and the processes required to solve these problems are complex and lack application feasibility at the industrial scale. Emerging technologies create new materials for enzyme carriers and sophisticate the well-known immobilization principles to produce more robust, eco-friendlier, and cheaper biocatalysts. Therefore, this review discusses the trending studies and industrial applications of the materials and protocols for lipase immobilization, analyzing their advantages and disadvantages. Finally, it summarizes the current challenges and potential alternatives for lipases at the industrial level.

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Miličić, Nevena, Ivana Ćevid, Mehmet Mervan Çakar, Martina Sudar, and Zvjezdana Findrik Blažević. "Enzyme Reaction Engineering as a Tool to Investigate the Potential Application of Enzyme Reaction Systems." Hungarian Journal of Industry and Chemistry 50, no. 1 (September 27, 2022): 45–55. http://dx.doi.org/10.33927/hjic-2022-08.

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It is widely recognized and accepted that although biocatalysis is an exquisite tool to synthesize natural and unnatural compounds under mild process conditions, much can be done to better understand these processes as well as detect resulting bottlenecks and help to resolve them. This is the precise purpose of enzyme reaction engineering, a scientific discipline that focuses on investigating enzyme reactions with the goal of facilitating their implementation on an industrial scale. Even though reaction schemes of enzyme reactions often seem simple, in practice, the interdependence of differentvariables is unknown, very complex and may prevent further applications. Therefore, in this work, important aspects of the implementation of enzyme reactions are discussed using simple and complex examples, along with principles of mathematical modelling that provide explanations for why some reactions do not proceed as planned.

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Behrendorff, James B. Y. H., Weiliang Huang, and Elizabeth M. J. Gillam. "Directed evolution of cytochrome P450 enzymes for biocatalysis: exploiting the catalytic versatility of enzymes with relaxed substrate specificity." Biochemical Journal 467, no. 1 (March 20, 2015): 1–15. http://dx.doi.org/10.1042/bj20141493.

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Cytochrome P450 enzymes are renowned for their ability to insert oxygen into an enormous variety of compounds with a high degree of chemo- and regio-selectivity under mild conditions. This property has been exploited in Nature for an enormous variety of physiological functions, and representatives of this ancient enzyme family have been identified in all kingdoms of life. The catalytic versatility of P450s makes them well suited for repurposing for the synthesis of fine chemicals such as drugs. Although these enzymes have not evolved in Nature to perform the reactions required for modern chemical industries, many P450s show relaxed substrate specificity and exhibit some degree of activity towards non-natural substrates of relevance to applications such as drug development. Directed evolution and other protein engineering methods can be used to improve upon this low level of activity and convert these promiscuous generalist enzymes into specialists capable of mediating reactions of interest with exquisite regio- and stereo-selectivity. Although there are some notable successes in exploiting P450s from natural sources in metabolic engineering, and P450s have been proven repeatedly to be excellent material for engineering, there are few examples to date of practical application of engineered P450s. The purpose of the present review is to illustrate the progress that has been made in altering properties of P450s such as substrate range, cofactor preference and stability, and outline some of the remaining challenges that must be overcome for industrial application of these powerful biocatalysts.

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Peters, Christin, and Rebecca Buller. "Industrial Application of 2-Oxoglutarate-Dependent Oxygenases." Catalysts 9, no. 3 (February 28, 2019): 221. http://dx.doi.org/10.3390/catal9030221.

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C–H functionalization is a chemically challenging but highly desirable transformation. 2-oxoglutarate-dependent oxygenases (2OGXs) are remarkably versatile biocatalysts for the activation of C–H bonds. In nature, they have been shown to accept both small and large molecules carrying out a plethora of reactions, including hydroxylations, demethylations, ring formations, rearrangements, desaturations, and halogenations, making them promising candidates for industrial manufacture. In this review, we describe the current status of 2OGX use in biocatalytic applications concentrating on 2OGX-catalyzed oxyfunctionalization of amino acids and synthesis of antibiotics. Looking forward, continued bioinformatic sourcing will help identify additional, practical useful members of this intriguing enzyme family, while enzyme engineering will pave the way to enhance 2OGX reactivity for non-native substrates.

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Greening, Chris, F. Hafna Ahmed, A. Elaaf Mohamed, Brendon M. Lee, Gunjan Pandey, Andrew C. Warden, Colin Scott, John G. Oakeshott, Matthew C. Taylor, and Colin J. Jackson. "Physiology, Biochemistry, and Applications of F420- and Fo-Dependent Redox Reactions." Microbiology and Molecular Biology Reviews 80, no. 2 (April 27, 2016): 451–93. http://dx.doi.org/10.1128/mmbr.00070-15.

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SUMMARY5-Deazaflavin cofactors enhance the metabolic flexibility of microorganisms by catalyzing a wide range of challenging enzymatic redox reactions. While structurally similar to riboflavin, 5-deazaflavins have distinctive and biologically useful electrochemical and photochemical properties as a result of the substitution of N-5 of the isoalloxazine ring for a carbon. 8-Hydroxy-5-deazaflavin (Fo) appears to be used for a single function: as a light-harvesting chromophore for DNA photolyases across the three domains of life. In contrast, its oligoglutamyl derivative F420is a taxonomically restricted but functionally versatile cofactor that facilitates many low-potential two-electron redox reactions. It serves as an essential catabolic cofactor in methanogenic, sulfate-reducing, and likely methanotrophic archaea. It also transforms a wide range of exogenous substrates and endogenous metabolites in aerobic actinobacteria, for example mycobacteria and streptomycetes. In this review, we discuss the physiological roles of F420in microorganisms and the biochemistry of the various oxidoreductases that mediate these roles. Particular focus is placed on the central roles of F420in methanogenic archaea in processes such as substrate oxidation, C1pathways, respiration, and oxygen detoxification. We also describe how two F420-dependent oxidoreductase superfamilies mediate many environmentally and medically important reactions in bacteria, including biosynthesis of tetracycline and pyrrolobenzodiazepine antibiotics by streptomycetes, activation of the prodrugs pretomanid and delamanid byMycobacterium tuberculosis, and degradation of environmental contaminants such as picrate, aflatoxin, and malachite green. The biosynthesis pathways of Foand F420are also detailed. We conclude by considering opportunities to exploit deazaflavin-dependent processes in tuberculosis treatment, methane mitigation, bioremediation, and industrial biocatalysis.

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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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Mukherjee, Anindya, and Martin Koller. "Polyhydroxyalkanoate (PHA) Biopolyesters - Emerging and Major Products of Industrial Biotechnology." EuroBiotech Journal 6, no. 2 (April 1, 2022): 49–60. http://dx.doi.org/10.2478/ebtj-2022-0007.

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Abstract Background: Industrial Biotechnology (“White Biotechnology”) is the large-scale production of materials and chemicals using renewable raw materials along with biocatalysts like enzymes derived from microorganisms or by using microorganisms themselves (“whole cell biocatalysis”). While the production of ethanol has existed for several millennia and can be considered a product of Industrial Biotechnology, the application of complex and engineered biocatalysts to produce industrial scale products with acceptable economics is only a few decades old. Bioethanol as fuel, lactic acid as food and PolyHydroxyAlkanoates (PHA) as a processible material are some examples of products derived from Industrial Biotechnology. Purpose and Scope: Industrial Biotechnology is the sector of biotechnology that holds the most promise in reducing our dependence on fossil fuels and mitigating environmental degradation caused by pollution, since all products that are made today from fossil carbon feedstocks could be manufactured using Industrial Biotechnology – renewable carbon feedstocks and biocatalysts. To match the economics of fossil-based bulk products, Industrial Biotechnology-based processes must be sufficiently robust. This aspect continues to evolve with increased technological capabilities to engineer biocatalysts (including microorganisms) and the decreasing relative price difference between renewable and fossil carbon feedstocks. While there have been major successes in manufacturing products from Industrial Biotechnology, challenges exist, although its promise is real. Here, PHA biopolymers are a class of product that is fulfilling this promise. Summary and Conclusion: The authors illustrate the benefits and challenges of Industrial Biotechnology, the circularity and sustainability of such processes, its role in reducing supply chain issues, and alleviating societal problems like poverty and hunger. With increasing awareness among the general public and policy makers of the dangers posed by climate change, pollution and persistent societal issues, Industrial Biotechnology holds the promise of solving these major problems and is poised for a transformative upswing in the manufacture of bulk chemicals and materials from renewable feedstocks and biocatalysts.

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Illeová, Viera, and Milan Polakovič. "Design of operational temperature for immobilized glucose isomerise using an accelerated inactivation method." Acta Chimica Slovaca 11, no. 2 (October 1, 2018): 157–62. http://dx.doi.org/10.2478/acs-2018-0022.

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AbstractThermal inactivation of immobilized glucose isomerase in a concentrated glucose solution was investigated in the batch mode and temperature range of 83–95 °C, which is substantially higher than the temperature used in the industrial production of high-fructose corn syrup. Simultaneous evaluation of all inactivation data showed that first-order kinetics with the Arrhenius temperature dependence of the rate constant provided a good approximation of the biocatalyst stability under the investigated conditions. The model parameters were then used to predict the operational temperature for this biocatalyst in the production of high-fructose corn syrup based on the set operational life-time of the biocatalyst. The simulation predicted a window of operational temperature of 60–65 °C, which corresponds very well with the industrial applications of this biocatalyst. This observation demonstrates that the multi-temperature method of enzyme inactivation can provide a good estimate of biocatalyst process stability and is thus a useful tool in the development of biocatalytic processes.

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Burton, Stephanie G. "Development of bioreactors for application of biocatalysts in biotransformations and bioremediation." Pure and Applied Chemistry 73, no. 1 (January 1, 2001): 77–83. http://dx.doi.org/10.1351/pac200173010077.

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Biotransformation systems, whether used for environmentally benign biocatalysis of synthetic reactions, or bioremediation of pollutants, require suitable biocatalysts and suitable bioreactor systems with particular characteristics. Our research focuses on the bioconversion of organic compounds, many of which are industrial residues, such as phenols, poly-aromatic hydrocarbons, heterocyclic compounds, and polychlorinated biphenyls. The purpose of such biotransformations can be twofold: firstly, to remove them from effluents and convert them to less toxic forms, and secondly, to convert them into products with economic value. We conduct research in utilizing various isolated-enzyme and whole-cell biological agents; bioreactors, including novel membrane bioreactors, are used as a means of supporting/immobilizing, and hence applying, these biocatalysts in continuous systems. In addition, the enzyme systems are characterized biochemically, to provide information which is required in modification, adaptation, and scale-up of the bioreactors. The paper summarizes research on application of biofilms of fungal and bacterial cells and their enzymes, including hydrolases, polyphenol oxidase, peroxidase and laccase, in bioreactor systems including continuously operating membrane bioreactors.

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Xu, Meng-Qiu, Shuang-Shuang Wang, Li-Na Li, Jian Gao, and Ye-Wang Zhang. "Combined Cross-Linked Enzyme Aggregates as Biocatalysts." Catalysts 8, no. 10 (October 17, 2018): 460. http://dx.doi.org/10.3390/catal8100460.

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Enzymes are efficient biocatalysts providing an important tool in many industrial biocatalytic processes. Currently, the immobilized enzymes prepared by the cross-linked enzyme aggregates (CLEAs) have drawn much attention due to their simple preparation and high catalytic efficiency. Combined cross-linked enzyme aggregates (combi-CLEAs) including multiple enzymes have significant advantages for practical applications. In this review, the conditions or factors for the preparation of combi-CLEAs such as the proportion of enzymes, the type of cross-linker, and coupling temperature were discussed based on the reaction mechanism. The recent applications of combi-CLEAs were also reviewed.

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Xu, Huan, Guilhem Boeuf, Kairuo Zhu, Zixian Jia, Andrei Kanaev, Rabah Azouani, Zhengyan Wu, Mamadou Traore, and Abdellatif Elm’selmi. "Laccase Cross-Linked Ultraporous Aluminas for Sustainable Biodegradation of Remazol Brilliant Blue R." Catalysts 12, no. 7 (July 6, 2022): 744. http://dx.doi.org/10.3390/catal12070744.

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Over the past few decades, enzyme-based green and sustainable chemistry has attracted extensive research attention, which provides a promising alternative to the conventional treatment methods of recalcitrant micropollutants. However, enzyme denaturation and stability loss remain critical challenges for its potential applications in industrial wastewater treatment. In this study, laccase from Trametes versicolor (laccase T.) was cross-linked immobilized by ultraporous alumina (UPA) for the sustainable biodegradation of Remazol Brilliant Blue R (RBBR). Through sequential use of an aminosilane coupling agent (3-aminopropyl)triethoxysilane (APTES) and bifunctional cross-linker glutaraldehyde (GA), the synthesized biocatalysts showed better immobilization performances (about 4-fold to physical adsorption). The GA concentration considerably affected the laccase T. cross-linking degree, while the GA post-treatment protocol showed the highest laccase T. immobilization yield with lower activity recovery. Moreover, the biocatalyst stabilities including pH stability, thermal stability, storage stability, and reusability were also studied. Tolerance to broader pH and temperature ranges, better storage stability, good reusability of laccase T. cross-linked UPA(γ) biocatalysts, and their continuous RBRR biodegradation efficiency highlight the potentials of enzyme-based inorganic materials in industrial wastewater treatment, which can broaden our understanding of their practical applications in environmental fields.

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Blank, Marshal, and Paul Schweiger. "Surface display for metabolic engineering of industrially important acetic acid bacteria." PeerJ 6 (April 6, 2018): e4626. http://dx.doi.org/10.7717/peerj.4626.

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Acetic acid bacteria have unique metabolic characteristics that suit them for a variety of biotechnological applications. They possess an arsenal of membrane-bound dehydrogenases in the periplasmic space that are capable of regiospecific and enantioselective partial oxidations of sugars, alcohols, and polyols. The resulting products are deposited directly into the medium where they are easily recovered for use as pharmaceutical precursors, industrial chemicals, food additives, and consumer products. Expression of extracytoplasmic enzymes to augment the oxidative capabilities of acetic acid bacteria is desired but is challenging due to the already crowded inner membrane. To this end, an original surface display system was developed to express recombinant enzymes at the outer membrane of the model acetic acid bacteriumGluconobacter oxydans. Outer membrane porin F (OprF) was used to deliver alkaline phosphatase (PhoA) to the cell surface. Constitutive high-strength p264 and moderate-strength p452 promoters were used to direct expression of the surface display system. This system was demonstrated for biocatalysis in whole-cell assays with the p264 promoter having a twofold increase in PhoA activity compared to the p452 promoter. Proteolytic cleavage of PhoA from the cell surface confirmed proper delivery to the outer membrane. Furthermore, a linker library was constructed to optimize surface display. A rigid (EAAAK)1linker led to the greatest improvement, increasing PhoA activity by 69%. This surface display system could be used both to extend the capabilities of acetic acid bacteria in current biotechnological processes, and to broaden the potential of these microbes in the production of value-added products.

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Johannes, Tyler W., Ryan D. Woodyer, and Huimin Zhao. "Directed Evolution of a Thermostable Phosphite Dehydrogenase for NAD(P)H Regeneration." Applied and Environmental Microbiology 71, no. 10 (October 2005): 5728–34. http://dx.doi.org/10.1128/aem.71.10.5728-5734.2005.

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ABSTRACT NAD(P)H-dependent oxidoreductases are valuable tools for synthesis of chiral compounds. The expense of the cofactors, however, requires in situ cofactor regeneration for preparative applications. We have attempted to develop an enzymatic system based on phosphite dehydrogenase (PTDH) from Pseudomonas stutzeri to regenerate the reduced nicotinamide cofactors NADH and NADPH. Here we report the use of directed evolution to address one of the main limitations with the wild-type PTDH enzyme, its low stability. After three rounds of random mutagenesis and high-throughput screening, 12 thermostabilizing amino acid substitutions were identified. These 12 mutations were combined by site-directed mutagenesis, resulting in a mutant whose T 50 is 20°C higher and half-life of thermal inactivation at 45°C is >7,000-fold greater than that of the parent PTDH. The engineered PTDH has a half-life at 50°C that is 2.4-fold greater than the Candida boidinii formate dehydrogenase, an enzyme widely used for NADH regeneration. In addition, its catalytic efficiency is slightly higher than that of the parent PTDH. Various mechanisms of thermostabilization were identified using molecular modeling. The improved stability and effectiveness of the final mutant were shown using the industrially important bioconversion of trimethylpyruvate to l-tert-leucine. The engineered PTDH will be useful in NAD(P)H regeneration for industrial biocatalysis.

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Journal articles on the topic 'Biocatalysis – Industrial applications'

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