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Catalysts
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Biocatalytic Cascade Reactions
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Biocatalytic Cascade Reactions

A special issue of Catalysts (ISSN 2073-4344). This special issue belongs to the section "Biocatalysis".

Deadline for manuscript submissions: closed (31 December 2022) | Viewed by 12934

Special Issue Editors

Dr. Nicholas Harmer

E-Mail Website
Guest Editor
Living Systems Institute, University of Exeter, Exeter, UK
Interests: enzymes; synthetic biology; polysaccharides; cascade reactions; modelling; structural biology
Prof. Dr. Jennifer Littlechild

E-Mail Website
Guest Editor
The Henry Wellcome Building for Biocatalysis, Biosciences, Biocatalysis Centre, University of Exeter, Stocker Road, Exeter EX4 4QD, UK
Interests: industrial biotechnology; biocatalysis; enzyme mechanisms
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The use of enzymes for Green Chemistry is already embedded in many industrial processes. Enzyme cascades represent the next generation of biocatalysis, making many more reactions, chemicals, and processes accessible. These developments will drive ecological improvements in the manufacturing of pharmaceuticals, fine chemicals, and fragrances, among others. This Special Issue will focus on recent developments in enzyme-based cascades reactions in vitro and in vivo. Enzyme cascades have shown enormous potential to extend biocatalysis and green chemistry from single enzyme reactions into more complicated biotransformations. This Special Issue will cover all aspects of cascade reactions, including cofactor recycling, optimisation of metabolic flux, suppression of side reactions, metabolic engineering, modelling, and the use of microfluidics.

Prof. Nicholas Harmer
Prof. Jennifer Littlechild
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Catalysts is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Enzymes
  • Enzyme cascades
  • Cofactor recycling
  • Green chemistry
  • Microfluidics
  • In vitro biotransformations
  • In vivo biocatalysis
  • Metabolic engineering
  • Cascade modelling

Published Papers (6 papers)

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Research

12 pages, 1284 KiB  
Article
Bayesian Optimization for an ATP-Regenerating In Vitro Enzyme Cascade
by Regine Siedentop, Maximilian Siska, Niklas Möller, Hannah Lanzrath, Eric von Lieres, Stephan Lütz and Katrin Rosenthal
Catalysts 2023, 13(3), 468; https://0-doi-org.brum.beds.ac.uk/10.3390/catal13030468 - 23 Feb 2023
Cited by 6 | Viewed by 2115
Abstract
Enzyme cascades are an emerging synthetic tool for the synthesis of various molecules, combining the advantages of biocatalysis and of one-pot multi-step reactions. However, the more complex the enzyme cascade is, the more difficult it is to achieve adequate productivities and product concentrations. [...] Read more.
Enzyme cascades are an emerging synthetic tool for the synthesis of various molecules, combining the advantages of biocatalysis and of one-pot multi-step reactions. However, the more complex the enzyme cascade is, the more difficult it is to achieve adequate productivities and product concentrations. Therefore, the whole process must be optimized to account for synergistic effects. One way to deal with this challenge involves data-driven models in combination with experimental validation. Here, Bayesian optimization was applied to an ATP-producing and -regenerating enzyme cascade consisting of polyphosphate kinases. The enzyme and co-substrate concentrations were adjusted for an ATP-dependent reaction, catalyzed by mevalonate kinase (MVK). With a total of 16 experiments, we were able to iteratively optimize the initial concentrations of the components used in the one-pot synthesis to improve the specific activity of MVK with 10.2 U mg−1. The specific activity even exceeded the results of the reference reaction with stoichiometrically added ATP amounts, with which a specific activity of 8.8 U mg−1 was reached. At the same time, the product concentrations were also improved so that complete yields were achieved. Full article
(This article belongs to the Special Issue Biocatalytic Cascade Reactions)
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10 pages, 3405 KiB  
Article
Green Synthesis of Spirooxindoles via Lipase-Catalyzed One-Pot Tandem Reaction in Aqueous Media
by Yong Tang, Ciduo Wang, Hanqing Xie, Yuelin Xu, Chunyu Wang, Chuang Du, Zhi Wang and Lei Wang
Catalysts 2023, 13(1), 143; https://0-doi-org.brum.beds.ac.uk/10.3390/catal13010143 - 07 Jan 2023
Cited by 2 | Viewed by 1616
Abstract
The development of non-natural enzymatic catalysis is important for multicomponent tandem organic transformations. However, the delicate acting environments of biological enzymes still present some challenges in the synthesis of spirooxindole skeleton via enzymatic catalysis. To address these issues, a lipase-catalyzed method was developed [...] Read more.
The development of non-natural enzymatic catalysis is important for multicomponent tandem organic transformations. However, the delicate acting environments of biological enzymes still present some challenges in the synthesis of spirooxindole skeleton via enzymatic catalysis. To address these issues, a lipase-catalyzed method was developed for the synthesis of spirooxindole frameworks. Using easily available isatins, cycloketones, and malononitriles as substrates, mild reaction conditions, and a reasonable reaction time, moderate to good yields (67–92%) and excellent functional group tolerance were accomplished via this protocol. The related mechanism explanation is also speculated in this paper. Full article
(This article belongs to the Special Issue Biocatalytic Cascade Reactions)
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14 pages, 3359 KiB  
Article
Sustainable Chemoenzymatic Cascade Transformation of Corncob to Furfuryl Alcohol with Rice Husk-Based Heterogeneous Catalyst UST-Sn-RH
by Qizhen Yang, Zhengyu Tang, Jiale Xiong and Yucai He
Catalysts 2023, 13(1), 37; https://0-doi-org.brum.beds.ac.uk/10.3390/catal13010037 - 25 Dec 2022
Cited by 4 | Viewed by 1335
Abstract
Valorization of the abundant renewable lignocellulose through an efficient chemoenzymatic strategy to produce the furan-based platform compounds has raised great interest in recent years. In this work, a newly prepared sulfonated tin-loaded rice husk-based heterogeneous chemocatalyst UST-Sn-RH was utilized to transform corncob (75.0 [...] Read more.
Valorization of the abundant renewable lignocellulose through an efficient chemoenzymatic strategy to produce the furan-based platform compounds has raised great interest in recent years. In this work, a newly prepared sulfonated tin-loaded rice husk-based heterogeneous chemocatalyst UST-Sn-RH was utilized to transform corncob (75.0 g/L) into furfural (72.1 mM) at 170 °C for 30 min in an aqueous system. To upgrade furfural into furfuryl alcohol, whole cells of recombinant E. coli KPADH harboring alcohol dehydrogenase were employed to transform corncob-derived furfural into furfuryl alcohol at 30 °C and pH 7.5. In the established chemoenzymatic cascade process, corncob was efficiently transformed to furfuryl alcohol with a productivity of 0.304 g furfuryl alcohol/(g xylan in corncob). In general, biomass could be efficiently valorized into valuable furan-based chemicals in this tandem reaction with the chemocatalyst (bio-based UST-Sn-RH) and the biocatalyst (KPADH cell) in an aqueous system, which has potential application. Full article
(This article belongs to the Special Issue Biocatalytic Cascade Reactions)
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13 pages, 3154 KiB  
Article
Chemoenzymatic One-Pot Process for the Synthesis of Tetrahydroisoquinolines
by Andreas Sebastian Klein, Anna Christina Albrecht and Jörg Pietruszka
Catalysts 2021, 11(11), 1389; https://0-doi-org.brum.beds.ac.uk/10.3390/catal11111389 - 17 Nov 2021
Cited by 4 | Viewed by 2395
Abstract
1,2,3,4-Tetrahydroisoquinolines form a valuable scaffold for a variety of bioactive secondary metabolites and commercial pharmaceuticals. Due to the harsh or complex conditions of the conventional chemical synthesis of this molecular motif, alternative mild reaction pathways are in demand. Here we present an easy-to-operate [...] Read more.
1,2,3,4-Tetrahydroisoquinolines form a valuable scaffold for a variety of bioactive secondary metabolites and commercial pharmaceuticals. Due to the harsh or complex conditions of the conventional chemical synthesis of this molecular motif, alternative mild reaction pathways are in demand. Here we present an easy-to-operate chemoenzymatic one-pot process for the synthesis of tetrahydroisoquinolines starting from benzylic alcohols and an amino alcohol. We initially demonstrate the oxidation of 12 benzylic alcohols by a laccase/TEMPO system to the corresponding aldehydes, which are subsequently integrated in a phosphate salt mediated Pictet–Spengler reaction with m-tyramine. The reaction conditions of both individual reactions were analyzed separately, adapted to each other, and a straightforward one-pot process was developed. This enables the production of 12 1,2,3,4-tetrahydroisoquinolines with yields of up to 87% with constant reaction conditions in phosphate buffer and common laboratory glass bottles without the supplementation of any additives. Full article
(This article belongs to the Special Issue Biocatalytic Cascade Reactions)
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9 pages, 1253 KiB  
Article
Enhanced In Vitro Cascade Catalysis of Glycerol into Pyruvate and Acetoin by Integration with Dihydroxy Acid Dehydratase from Paralcaligenes ureilyticus
by Shiting Guo, Xiaoxu Tan, Yuxian Wang, Kai Li, Chuanjuan Lü, Cuiqing Ma and Chao Gao
Catalysts 2021, 11(11), 1282; https://0-doi-org.brum.beds.ac.uk/10.3390/catal11111282 - 23 Oct 2021
Cited by 5 | Viewed by 2013
Abstract
Recently, an in vitro enzymatic cascade was constructed to transform glycerol into the high-value platform chemical pyruvate. However, the low activity of dihydroxy acid dehydratase from Sulfolobus solfataricus (SsDHAD) limited the efficiency. In this study, the enzymatic reduction of pyruvate catalyzed by d [...] Read more.
Recently, an in vitro enzymatic cascade was constructed to transform glycerol into the high-value platform chemical pyruvate. However, the low activity of dihydroxy acid dehydratase from Sulfolobus solfataricus (SsDHAD) limited the efficiency. In this study, the enzymatic reduction of pyruvate catalyzed by d-lactate dehydrogenase from Pseudomonas aeruginosa PAO1 was used to assay the activities of dihydroxy acid dehydratases. Dihydroxy acid dehydratase from Paralcaligenes ureilyticus (PuDHT) was identified as the most efficient candidate for glycerate dehydration. After the optimization of the catalytic temperature for the enzymatic cascade, comprising alditol oxidase from Streptomyces coelicolor A3, PuDHT, and catalase from Aspergillus niger, 20.50 ± 0.27 mM of glycerol was consumed in 4 h to produce 18.95 ± 0.97 mM of pyruvate with a productivity 12.15-fold higher than the previous report using SsDHAD. The enzymatic cascade was further coupled with the pyruvate decarboxylase from Zymomonas mobile for the production of another platform compound, acetoin. Acetoin at a concentration of 8.52 ± 0.12 mM was produced from 21.62 ± 0.19 mM of glycerol with a productivity of 1.42 ± 0.02 mM h−1. Full article
(This article belongs to the Special Issue Biocatalytic Cascade Reactions)
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13 pages, 2292 KiB  
Article
Cascading Old Yellow Enzyme, Alcohol Dehydrogenase and Glucose Dehydrogenase for Selective Reduction of (E/Z)-Citral to (S)-Citronellol
by Yunpeng Jia, Qizhou Wang, Jingjing Qiao, Binbin Feng, Xueting Zhou, Lijun Jin, Yingting Feng, Duxia Yang, Chenze Lu and Xiangxian Ying
Catalysts 2021, 11(8), 931; https://0-doi-org.brum.beds.ac.uk/10.3390/catal11080931 - 30 Jul 2021
Cited by 8 | Viewed by 2451
Abstract
Citronellol is a kind of unsaturated alcohol with rose-like smell and its (S)-enantiomer serves as an important intermediate for organic synthesis of (-)-cis-rose oxide. Chemical methods are commonly used for the synthesis of citronellol and its (S)-enantiomer, [...] Read more.
Citronellol is a kind of unsaturated alcohol with rose-like smell and its (S)-enantiomer serves as an important intermediate for organic synthesis of (-)-cis-rose oxide. Chemical methods are commonly used for the synthesis of citronellol and its (S)-enantiomer, which suffers from severe reaction conditions and poor selectivity. Here, the first one-pot double reduction of (E/Z)-citral to (S)-citronellol was achieved in a multi-enzymatic cascade system: N-ethylmaleimide reductase from Providencia stuartii (NemR-PS) was selected to catalyze the selective reduction of (E/Z)-citral to (S)-citronellal, alcohol dehydrogenase from Yokenella sp. WZY002 (YsADH) performed the further reduction of (S)-citronellal to (S)-citronellol, meanwhile a variant of glucose dehydrogenase from Bacillus megaterium (BmGDHM6), together with glucose, drove efficient NADPH regeneration. The Escherichia coli strain co-expressing NemR-PS, YsADH, and BmGDHM6 was successfully constructed and used as the whole-cell catalyst. Various factors were investigated for achieving high conversion and reducing the accumulation of the intermediate (S)-citronellal and by-products. 0.4 mM NADP+ was essential for maintaining high catalytic activity, while the feeding of the cells expressing BmGDHM6 effectively eliminated the intermediate and by-products and shortened the reaction time. Under optimized conditions, the bio-transformation of 400 mM citral caused nearly complete conversion (>99.5%) to enantio-pure (S)-citronellol within 36 h, demonstrating promise for industrial application. Full article
(This article belongs to the Special Issue Biocatalytic Cascade Reactions)
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