The E factor at 30: a passion for pollution prevention

Green Chemistry, Journal Year: 2023, Volume and Issue: 25(5), P. 1704 - 1728

Published: Jan. 1, 2023

Publication of the E Factor drew attention to problem waste in chemicals manufacture. Thirty yeas later it is abundantly clear that underlying cause global environmental problems, from climate change plastic pollution.

Language: Английский

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Where Chemocatalysis Meets Biocatalysis: In Water

Chemical Reviews, Journal Year: 2022, Volume and Issue: 123(9), P. 5262 - 5296

Published: Dec. 6, 2022

Chemoenzymatic catalysis, by definition, involves the merging of sequential reactions using both chemocatalysis and biocatalysis, typically in a single reaction vessel. A major challenge, solution to which, however, is associated with numerous advantages, run such one-pot processes water: majority enzyme-catalyzed take place water as Nature's medium, thus enabling broad synthetic diversity when due option use virtually all types enzymes. Furthermore, cheap, abundantly available, environmentally friendly, making it, principle, an ideal medium. On other hand, most routinely performed today organic solvents (which might deactivate enzymes), appearing make it difficult combine biocatalysis toward cascades water. Several creative approaches solutions that enable combinations chemo- be realized applied problems are presented herein, reflecting state-of-the-art this blossoming field. Coverage has been sectioned into three parts, after introductory remarks: (1) Chapter 2 focuses on historical developments initiated area research; (2) 3 describes key post-initial discoveries have advanced field; (3) 4 highlights latest achievements provide attractive main question compatibility between (used predominantly aqueous media) (that remains solvents), Chapters covering mainly literature from ca. 2018 present. 5 6 brief overview where field stands, challenges lie ahead, ultimately, prognosis looking future chemoenzymatic catalysis synthesis.

Language: Английский

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Biocatalysis: A smart and green tool for the preparation of chiral drugs

Chirality, Journal Year: 2022, Volume and Issue: 34(11), P. 1403 - 1418

Published: Aug. 5, 2022

Abstract Over the last decades, biocatalysis has achieved growing interest thanks to its potential enable high efficiency, yield, and eco‐friendly processes aimed at production of pharmacologically relevant compounds. Particularly, proved an effective potent tool in preparation chiral molecules, recent innovations biotechnologies nanotechnologies open up a new era further developments this field. Different strategies are now available for synthesis drugs their intermediates. Enzymes green tools that offer several advantages, associated both catalysis environmentally friendly reactants. Specifically, use enzymes isolated from biological sources or whole‐cell represents valuable approach obtain pharmaceutical products. The sustainability, higher cost‐effectiveness biocatalytic reactions result improved performance properties can be translated academia industry. In review, we focus on approaches synthesizing Aiming unveil potentialities systems, discuss different examples innovative applications

Language: Английский

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Glutaraldehyde modification of lipases immobilized on octyl agarose beads: Roles of the support enzyme loading and chemical amination of the enzyme on the final enzyme features

International Journal of Biological Macromolecules, Journal Year: 2023, Volume and Issue: 248, P. 125853 - 125853

Published: July 17, 2023

Lipase B from Candida antarctica (CALB) and lipase Thermomyces lanuginosus (TLL) have been immobilized on octyl agarose at low loading a exceeding the maximum support capacity. Then, enzymes treated with glutaraldehyde inactivated pH 7 in Tris-HCl, sodium phosphate HEPES, giving different stabilities. Stabilization (depending buffer) of highly loaded biocatalysts was found, very likely as consequence detected intermolecular crosslinkings. This did not occur for lowly biocatalysts. Next, were chemically aminated then glutaraldehyde. In case TLL, intramolecular crosslinkings (visible by apparent reduction protein size) increased enzyme stability biocatalysts, an effect that further due to Using CALB, less intense, stabilization lower, even though quite intense biocatalyst. The depended inactivation buffer. interactions between inactivating buffer effects chemical modifications suggest modification studies must be performed under target conditions.

Language: Английский

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Enhancing Lipase Immobilization via Physical Adsorption: Advancements in Stability, Reusability, and Industrial Applications for Sustainable Biotechnological Processes

ACS Omega, Journal Year: 2024, Volume and Issue: 9(47), P. 46698 - 46732

Published: Nov. 14, 2024

Immobilization of lipases by physical adsorption improves their stability, recovery, and reusability in biotechnological processes. The present review provides an advanced bibliometric analysis a comprehensive overview research progress this field. By searching Web Science, 39,575 publications were analyzed, 325 relevant articles selected. Key journals, countries, institutions, authors identified. most cited focus on biofuel production industrial applications. revealed four themes with the biofuel. method is effective when appropriate support used. Despite decrease patent applications, interest remains high. Future studies should optimizing materials exploring new applications technique. detailed understanding immobilization adsorption.

Language: Английский

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Advances in cofactor immobilization for enhanced continuous-flow biocatalysis

Journal of Flow Chemistry, Journal Year: 2024, Volume and Issue: 14(1), P. 219 - 238

Published: Feb. 14, 2024

Abstract The merging of biocatalysis with continuous-flow chemistry opens up new opportunities for sustainable and efficient chemical synthesis. Cofactor-dependent enzymes are essential various industrially attractive biocatalytic reactions. However, implementing these reactions in industry remains challenging due to the inherent cost cofactors requirement their external supply significant quantities. development efficient, low cost, simple versatile methods cofactor immobilization can address this important obstacle flow. This review explores recent progress by analyzing advantages current limitations available that comprise covalent tethering, ionic adsorption, physical entrapment, hybrid variations thereof. Moreover, analyzes all techniques specifically utilization provides a perspective future work area. will serve as guide steering field towards more economically viable biocatalysis. Graphical

Language: Английский

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Precision Engineering of the Co‐immobilization of Enzymes for Cascade Biocatalysis

Angewandte Chemie International Edition, Journal Year: 2024, Volume and Issue: 63(22)

Published: April 1, 2024

Abstract The design and orderly layered co‐immobilization of multiple enzymes on resin particles remain challenging. In this study, the SpyTag/SpyCatcher binding pair was fused to N‐terminus an alcohol dehydrogenase (ADH) aldo‐keto reductase (AKR), respectively. A non‐canonical amino acid (ncAA), p ‐azido‐L‐phenylalanine (p‐AzF), as anchor for covalent bonding enzymes, genetically inserted into preselected sites in AKR ADH. Employing two bioorthogonal counterparts azide–alkyne cycloaddition immobilization ADH enabled sequential dual‐enzyme coating porous microspheres. ordered reactor subsequently used synthesize ( S )‐1‐(2‐chlorophenyl)ethanol asymmetrically from corresponding prochiral ketone, enabling situ regeneration NADPH. exhibited a high catalytic conversion 74 % good reproducibility, retaining 80 its initial activity after six cycles. product had 99.9 ee, which that maintained each cycle. Additionally, double‐layer method significantly increased enzyme loading capacity, approximately 1.7 times greater than traditional single‐layer immobilization. More importantly, it simultaneously both purification carriers, thus providing convenient approach facilitate cascade biocatalysis.

Language: Английский

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Diastereo- and Enantioselective Chemoenzymatic Synthesis of Chiral Tricyclic Intermediate of Anti-HIV Drug Lenacapavir

ACS Catalysis, Journal Year: 2025, Volume and Issue: 15(3), P. 2045 - 2052

Published: Jan. 21, 2025

Despite its great potential, the development and implementation of scalable new-to-nature biocatalytic transformations in chemoenzymatic synthesis clinically significant pharmaceuticals still present a considerable challenge. We developed very recently anti-HIV drug lenacapavir's 5/5/3 fused tricyclic fragment featuring an unusual chiral cyclopropane moiety. Key to this is biocatalyst-controlled, fully diastereo- enantiodivergent cyclopropanation highly functionalized vinylpyrazole substrate, granting access all four possible stereoisomers lenacapavir cyclopropane. High-throughput experimentation led discovery heme-dependent globins, including nitrous oxide dioxygenase (NOD) protoglobin (Pgb), as promising biocatalysts. Directed evolution furnished enantioselective (up 99:1 d.r. e.r.). Further downstream chemical cyclization afforded desired tricycle with stereochemical purity.

Language: Английский

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Process intensification in continuous flow biocatalysis by up and downstream processing strategies

Current Opinion in Biotechnology, Journal Year: 2022, Volume and Issue: 78, P. 102835 - 102835

Published: Nov. 2, 2022

In this review, we focus on the holistic continuous enzymatic production and put special emphasis process intensification by up- downstream processing in flow biocatalysis. After a brief introduction, provide an overview of current examples enzyme immobilization as upstream for Thereafter, unit operations strategies, namely (i) liquid-liquid extraction, (ii) adsorptive processing, (iii) crystallization precipitation. Eventually, present our perspectives future trends research field.

Language: Английский

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Extremophiles in a changing world

Extremophiles, Journal Year: 2024, Volume and Issue: 28(2)

Published: April 29, 2024

Extremophiles and their products have been a major focus of research interest for over 40 years. Through this period, studies these organisms contributed hugely to many aspects the fundamental applied sciences, wider more philosophical issues such as origins life astrobiology. Our understanding cellular adaptations extreme conditions (such acid, temperature, pressure more), mechanisms underpinning stability macromolecules, subtleties, complexities limits biochemical processes has informed by on extremophiles. also numerous fields biotechnology, from diagnostics bioremediation. Yet, after years dedicated research, there remains much be discovered in field. Fortunately, extremophiles remain an active vibrant area research. In third decade twenty-first century, with decreasing global resources steadily increasing human population, world's attention turned urgency sustainability. These concerns were encapsulated formalized United Nations adoption 2030 Agenda Sustainable Development presentation seventeen Goals (SDGs) 2015. run-up 2030, we consider contributions that made, will future make, SDGs.

Language: Английский

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