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10th Anniversary of Catalysts: Biocatalysis in Analysis and Synthesis—Past,...
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10th Anniversary of Catalysts: Biocatalysis in Analysis and Synthesis—Past, Present and Future

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

Deadline for manuscript submissions: closed (31 December 2021) | Viewed by 49341

Printed Edition Available!
A printed edition of this Special Issue is available here.

Special Issue Editors

Prof. Dr. Evangelos Topakas

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Guest Editor
Biotechnology Laboratory, School of Chemical Engineering, National Technical University of Athens, 9 Iroon Polytech Str, Zografou Campus, 15780 Athens, Greece
Interests: biocatalysis; industrial biotechnology; lignocellulose degrading enzymes; novel enzymes; structure-function relationship
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Roland Wohlgemuth

E-Mail Website1 Website2
Guest Editor
MITR, Institute of Applied Radiation Chemistry, Faculty of Chemistry, Lodz University of Technology, Zeromskiego Street 116, 90-924 Lodz, Poland
Interests: bioeconomy; biocatalysis; glycobiology; metabolomics; industrial biotechnology
Special Issues, Collections and Topics in MDPI journals
Dr. David D. Boehr

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Guest Editor
Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA
Interests: enzymes; protein biophysics; allostery; protein engineering; NMR; microbiology
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

In view of the key importance of biocatalysis and as a way of celebrating the 10th anniversary of Catalysts, the “Biocatalysis” section has taken the initiative to launch a Special Issue entitled “10th Anniversary of Catalysts: Biocatalysis in Analysis and Synthesis—Past, Present and Future”. The “Biocatalysis” section in Catalysts continues to grow, with 46 Special Issues and 409 articles published to date.

This milestone is a great time to both reflect on previous accomplishments and identify the next challenges and opportunities in “Biocatalysis”. As such, we highly encourage potential authors to be forward-thinking in their articles, by proposing important questions and obstacles in their areas of interests and means of addressing them.  We are also interested in highlighting newly emerging areas for “Biocatalysis”. We believe that this Special Issue is an opportunity to identify grand themes in “Biocatalysis”. 

While we intend to keep the scope of this Special Issue broad in order to adequately reflect the diversity of research within “Biocatalysis”, some areas of interest include: (i) discovery methodologies for desired enzyme functions; (ii) relationships among enzyme structure, function and mechanism; (iii) development and analysis of robust and sensitive enzyme assays; (iv) novel enzymes; (v) scalable 1-step, multi-step and total biocatalytic synthesis. The aims and scope of this Special Issue are, however, not limited to these five areas of interest and potential authors are also welcome to submit contributions on other biocatalysis topics. 

It is a great honor and pleasure to invite you to contribute a review article or an original research paper for peer review and possible publication in this 10th Anniversary Special Issue.

Prof. Dr. Evangelos Topakas
Prof. Dr. Roland Wohlgemuth
Dr. David D. Boehr
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 2200 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

  • biocatalysis
  • enzyme structure, function and mechanism
  • enzyme assays
  • discovery of novel enzymes
  • biocatalytic synthesis

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Published Papers (13 papers)

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Editorial

Jump to: Research, Review

3 pages, 189 KiB  
Editorial
Special Issue “10th Anniversary of Catalysts: Biocatalysis in Analysis and Synthesis—Past, Present and Future”
by Evangelos Topakas, David Boehr and Roland Wohlgemuth
Catalysts 2022, 12(12), 1626; https://doi.org/10.3390/catal12121626 - 12 Dec 2022
Viewed by 1331
Abstract
The milestone of the 10th anniversary of Catalysts is a great time to reflect on past accomplishments, present progress and challenges, as well as to identify future challenges and opportunities [...] Full article
(This article belongs to the Special Issue 10th Anniversary of Catalysts: Biocatalysis in Analysis and Synthesis—Past, Present and Future)

Research

Jump to: Editorial, Review

9 pages, 2366 KiB  
Article
Enzymatic Desymmetrisation of Prochiral Phosphines and Phosphine P-Sulfides as a Route to P-Chiral Catalysts
by Lidia Madalińska, Piotr Kiełbasiński and Małgorzata Kwiatkowska
Catalysts 2022, 12(2), 171; https://doi.org/10.3390/catal12020171 - 28 Jan 2022
Cited by 2 | Viewed by 2552
Abstract
The enzyme-catalyzed monoacetylation of prochiral bis (2-hydroxymethylphenyl)methylphosphine and bis (2-hydroxymethylphenyl)phenylphosphine and their P-sulfides gave, in one single step, as a result of desymmetrisation, the corresponding monoacetates in moderate yields and with an enantiomeric excess of 16 to 98%, depending on the substrate [...] Read more.
The enzyme-catalyzed monoacetylation of prochiral bis (2-hydroxymethylphenyl)methylphosphine and bis (2-hydroxymethylphenyl)phenylphosphine and their P-sulfides gave, in one single step, as a result of desymmetrisation, the corresponding monoacetates in moderate yields and with an enantiomeric excess of 16 to 98%, depending on the substrate structure and enzyme applied. The absolute configurations of the selected products were determined by a chemical correlation. This led to the conclusion that, in the case of phosphines, phosphine oxides and phosphine sulfides enzymes preferentially produce compounds of the same spatial arrangement. The new compounds obtained will be transformed into chiral catalysts/ligands. Full article
(This article belongs to the Special Issue 10th Anniversary of Catalysts: Biocatalysis in Analysis and Synthesis—Past, Present and Future)
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17 pages, 2824 KiB  
Article
Performance of Liquid Eversa on Fatty Acid Ethyl Esters Production by Simultaneous Esterification/Transesterification of Low-to-High Acidity Feedstocks
by Ana Carolina Vieira, Ana Bárbara Moulin Cansian, José Renato Guimarães, Angelica Marquettotti Salcedo Vieira, Roberto Fernandez-Lafuente and Paulo Waldir Tardioli
Catalysts 2021, 11(12), 1486; https://doi.org/10.3390/catal11121486 - 3 Dec 2021
Cited by 14 | Viewed by 3172
Abstract
Liquid Eversa was evaluated in hydrolysis of acylglycerols from soybean oil deodorizer distillate (SODD), as well as simultaneous esterification/transesterification of SODD with low-to-high free fatty acids (FFAs) content using ethanol as acyl acceptor. Hydrolysis of SODD at mild temperature (37 °C) and without [...] Read more.
Liquid Eversa was evaluated in hydrolysis of acylglycerols from soybean oil deodorizer distillate (SODD), as well as simultaneous esterification/transesterification of SODD with low-to-high free fatty acids (FFAs) content using ethanol as acyl acceptor. Hydrolysis of SODD at mild temperature (37 °C) and without pH control (water:SODD mass ratio of 4:1) increased its FFAs content from 17.2 wt.% to 72.5 wt.% after 48 h reaction. A cold saponification of SODD allowed a saponification phase (SODD-SP) to be recovered with 93 wt.% saponification index and 2.25 wt.% FFAs content, which was used to find the experimental conditions for simultaneous esterification/transesterification reactions by experimental design. Temperature of 35 °C, enzyme concentration of 8.36 wt.%, and molar ratio of 3.64:1 (ethanol:SODD-SP) were found as the best conditions for fatty acid ethyl esters (FAEEs) production from SODD-SP (86.56 wt.% ester yield after 23 h reaction). Under the same reaction conditions, crude SODD (17.2 wt.% FFAs) and hydrolyzed SODD (72.5 wt.% FFAs) yielded products containing around 80 wt.% FAEEs. Caustic treatment could increase the ester content to around 90 wt.% and reduce the FFAs content to less than 1 wt.%. Our results show the good performance of liquid Eversa in aqueous (hydrolysis reactions) and organic (esterification/transesterification reactions) media. Full article
(This article belongs to the Special Issue 10th Anniversary of Catalysts: Biocatalysis in Analysis and Synthesis—Past, Present and Future)
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21 pages, 1285 KiB  
Article
Simplified Method to Optimize Enzymatic Esters Syntheses in Solvent-Free Systems: Validation Using Literature and Experimental Data
by Ronaldo Rodrigues de Sousa, Ayla Sant’Ana da Silva, Roberto Fernandez-Lafuente and Viridiana Santana Ferreira-Leitão
Catalysts 2021, 11(11), 1357; https://doi.org/10.3390/catal11111357 - 12 Nov 2021
Cited by 12 | Viewed by 2367
Abstract
The adoption of biocatalysis in solvent-free systems is an alternative to establish a greener esters production. An interesting correlation between the acid:alcohol molar ratio and biocatalyst (immobilized lipase) loading in the optimization of ester syntheses in solvent-free systems had been observed and explored. [...] Read more.
The adoption of biocatalysis in solvent-free systems is an alternative to establish a greener esters production. An interesting correlation between the acid:alcohol molar ratio and biocatalyst (immobilized lipase) loading in the optimization of ester syntheses in solvent-free systems had been observed and explored. A simple mathematical tool named Substrate-Enzyme Relation (SER) has been developed, indicating a range of reaction conditions that resulted in high conversions. Here, SER utility has been validated using data from the literature and experimental assays, totalizing 39 different examples of solvent-free enzymatic esterifications. We found a good correlation between the SER trends and reaction conditions that promoted high conversions on the syntheses of short, mid, or long-chain esters. Moreover, the predictions obtained with SER are coherent with thermodynamic and kinetics aspects of enzymatic esterification in solvent-free systems. SER is an easy-to-handle tool to predict the reaction behavior, allowing obtaining optimum reaction conditions with a reduced number of experiments, including the adoption of reduced biocatalysts loadings. Full article
(This article belongs to the Special Issue 10th Anniversary of Catalysts: Biocatalysis in Analysis and Synthesis—Past, Present and Future)
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9 pages, 11472 KiB  
Article
Kinetic and Structural Properties of a Robust Bacterial L-Amino Acid Oxidase
by Simone Savino, J. Daniël-Moráh Meijer, Henriëtte J. Rozeboom, Hugo L. van Beek and Marco W. Fraaije
Catalysts 2021, 11(11), 1309; https://doi.org/10.3390/catal11111309 - 28 Oct 2021
Cited by 4 | Viewed by 2984
Abstract
L-Amino acid oxidase (LAAO) is a flavin adenine dinucleotide (FAD)-dependent enzyme active on most proteinogenic L-amino acids, catalysing their conversion to α-keto acids by oxidative deamination of the substrate. For this oxidation reaction, molecular oxygen is used as the electron acceptor, generating hydrogen [...] Read more.
L-Amino acid oxidase (LAAO) is a flavin adenine dinucleotide (FAD)-dependent enzyme active on most proteinogenic L-amino acids, catalysing their conversion to α-keto acids by oxidative deamination of the substrate. For this oxidation reaction, molecular oxygen is used as the electron acceptor, generating hydrogen peroxide. LAAO can be used to detect L-amino acids, for the production of hydrogen peroxide as an oxidative agent or antimicrobial agent, and for the production of enantiopure amino acids from racemates. In this work, we characterised a previously reported LAAO from the bacterium Pseudoalteromonas luteoviolacea. The substrate scope and kinetic properties of the enzyme were determined, and the thermostability was evaluated. Additionally, we elucidated the crystal structure of this bacterial LAAO, enabling us to test the role of active site residues concerning their function in catalysis. The obtained insights and ease of expression of this thermostable LAAO provides a solid basis for the development of engineered LAAO variants tuned for biosensing and/or biocatalysis. Full article
(This article belongs to the Special Issue 10th Anniversary of Catalysts: Biocatalysis in Analysis and Synthesis—Past, Present and Future)
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10 pages, 1769 KiB  
Communication
Enzymatic Hydrogen Electrosynthesis at Enhanced Current Density Using a Redox Polymer
by John C. Ruth, Fabian M. Schwarz, Volker Müller and Alfred M. Spormann
Catalysts 2021, 11(10), 1197; https://doi.org/10.3390/catal11101197 - 30 Sep 2021
Cited by 4 | Viewed by 2833
Abstract
High-temperature tolerant enzymes offer multiple advantages over enzymes from mesophilic organisms for the industrial production of sustainable chemicals due to high specific activities and stabilities towards fluctuations in pH, heat, and organic solvents. The production of molecular hydrogen (H2) is of [...] Read more.
High-temperature tolerant enzymes offer multiple advantages over enzymes from mesophilic organisms for the industrial production of sustainable chemicals due to high specific activities and stabilities towards fluctuations in pH, heat, and organic solvents. The production of molecular hydrogen (H2) is of particular interest because of the multiple uses of hydrogen in energy and chemicals applications, and the ability of hydrogenase enzymes to reduce protons to H2 at a cathode. We examined the activity of Hydrogen-Dependent CO2 Reductase (HDCR) from the thermophilic bacterium Thermoanaerobacter kivui when immobilized in a redox polymer, cobaltocene-functionalized polyallylamine (Cc-PAA), on a cathode for enzyme-mediated H2 formation from electricity. The presence of Cc-PAA increased reductive current density 340-fold when used on an electrode with HDCR at 40 °C, reaching unprecedented current densities of up to 3 mA·cm−2 with minimal overpotential and high faradaic efficiency. In contrast to other hydrogenases, T. kivui HDCR showed substantial reversibility of CO-dependent inactivation, revealing an opportunity for usage in gas mixtures containing CO, such as syngas. This study highlights the important potential of combining redox polymers with novel enzymes from thermophiles for enhanced electrosynthesis. Full article
(This article belongs to the Special Issue 10th Anniversary of Catalysts: Biocatalysis in Analysis and Synthesis—Past, Present and Future)
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16 pages, 2879 KiB  
Article
From Cell-Free Protein Synthesis to Whole-Cell Biotransformation: Screening and Identification of Novel α-Ketoglutarate-Dependent Dioxygenases for Preparative-Scale Synthesis of Hydroxy-l-Lysine
by Jascha Rolf, Philipp Nerke, Annette Britner, Sebastian Krick, Stephan Lütz and Katrin Rosenthal
Catalysts 2021, 11(9), 1038; https://doi.org/10.3390/catal11091038 - 27 Aug 2021
Cited by 11 | Viewed by 3428
Abstract
The selective hydroxylation of non-activated C-H bonds is still a challenging reaction in chemistry. Non-heme Fe2+/α-ketoglutarate-dependent dioxygenases are remarkable biocatalysts for the activation of C-H-bonds, catalyzing mainly hydroxylations. The discovery of new Fe2+/α-ketoglutarate-dependent dioxygenases with suitable reactivity for biotechnological [...] Read more.
The selective hydroxylation of non-activated C-H bonds is still a challenging reaction in chemistry. Non-heme Fe2+/α-ketoglutarate-dependent dioxygenases are remarkable biocatalysts for the activation of C-H-bonds, catalyzing mainly hydroxylations. The discovery of new Fe2+/α-ketoglutarate-dependent dioxygenases with suitable reactivity for biotechnological applications is therefore highly relevant to expand the limited range of enzymes described so far. In this study, we performed a protein BLAST to identify homologous enzymes to already described lysine dioxygenases (KDOs). Six novel and yet uncharacterized proteins were selected and synthesized by cell-free protein synthesis (CFPS). The subsequent in vitro screening of the selected homologs revealed activity towards the hydroxylation of l-lysine (Lys) into hydroxy-l-lysine (Hyl), which is a versatile chiral building block. With respect to biotechnological application, Escherichia coli whole-cell biocatalysts were developed and characterized in small-scale biotransformations. As the whole-cell biocatalyst expressing the gene coding for the KDO from Photorhabdus luminescens showed the highest specific activity of 8.6 ± 0.6 U gCDW−1, it was selected for the preparative synthesis of Hyl. Multi-gram scale product concentrations were achieved providing a good starting point for further bioprocess development for Hyl production. A systematic approach was established to screen and identify novel Fe2+/α-ketoglutarate-dependent dioxygenases, covering the entire pathway from gene to product, which contributes to accelerating the development of bioprocesses for the production of value-added chemicals. Full article
(This article belongs to the Special Issue 10th Anniversary of Catalysts: Biocatalysis in Analysis and Synthesis—Past, Present and Future)
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17 pages, 4338 KiB  
Article
Novel Transaminase and Laccase from Streptomyces spp. Using Combined Identification Approaches
by Erica E. Ferrandi, Jelena Spasic, Lidija Djokic, Yevhen Vainshtein, Ramsankar Senthamaraikannan, Sandra Vojnovic, Christian Grumaz, Daniela Monti and Jasmina Nikodinovic-Runic
Catalysts 2021, 11(8), 919; https://doi.org/10.3390/catal11080919 - 29 Jul 2021
Cited by 9 | Viewed by 3045
Abstract
Three Streptomyces sp. strains with a multitude of target enzymatic activities confirmed by functional screening, namely BV129, BV286 and BV333, were subjected to genome sequencing aiming at the annotation of genes of interest, in-depth bioinformatics characterization and functional expression of the biocatalysts. A [...] Read more.
Three Streptomyces sp. strains with a multitude of target enzymatic activities confirmed by functional screening, namely BV129, BV286 and BV333, were subjected to genome sequencing aiming at the annotation of genes of interest, in-depth bioinformatics characterization and functional expression of the biocatalysts. A whole-genome shotgun sequencing followed by de novo genome assembly and annotation was performed revealing genomes of 6.4, 9.4 and 7.3 Mbp, respectively. Functional annotation of the proteins of interest resulted in between 2047 and 2763 putative targets. Among the various enzymatic activities that the three Streptomyces strains demonstrated to produce by functional screening, we focused our attention on transaminases (TAs) and laccases due to their high biocatalytic potential. Bioinformatics search allowed the identification of a putative TA from Streptomyces sp. BV333 as a potentially novel broad substrate scope TA and a putative laccase from Streptomyces sp. BV286 as potentially novel blue multicopper oxidase. The two sequences were cloned and overexpressed in Escherichia coli and the two novel enzymes, transaminase Sbv333-TA and laccase Sbv286-LAC, were characterized. Interestingly, both enzymes resulted to be exceptionally thermostable, Sbv333-TA showing a melting temperature (TM = 85 °C) only slightly lower compared to the TM of the most thermostable transaminases described to date (87–88 °C) and Sbv286-LAC being even thermoactivated at temperature >60 °C. Moreover, Sbv333-TA showed a broad substrate scope and remarkably demonstrated to be active in the transamination of β-ketoesters, which are rarely accepted by currently known TAs. On the other hand, Sbv286-LAC showed an improved activity in the presence of the cosolvent acetonitrile. Overall, it was shown that a combination of approaches from standard microbiological and biochemical screens to genome sequencing and analysis is required to afford novel and functional biocatalysts. Full article
(This article belongs to the Special Issue 10th Anniversary of Catalysts: Biocatalysis in Analysis and Synthesis—Past, Present and Future)
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10 pages, 1091 KiB  
Article
Biocatalytic Silylation: The Condensation of Phenols and Alcohols with Triethylsilanol
by Emily I. Sparkes, Chisom S. Egedeuzu, Billie Lias, Rehana Sung, Stephanie A. Caslin, S. Yasin Tabatabaei Dakhili, Peter G. Taylor, Peter Quayle and Lu Shin Wong
Catalysts 2021, 11(8), 879; https://doi.org/10.3390/catal11080879 - 22 Jul 2021
Cited by 7 | Viewed by 3112
Abstract
Silicatein-α (Silα), a hydrolytic enzyme derived from siliceous marine sponges, is one of the few enzymes in nature capable of catalysing the metathesis of silicon–oxygen bonds. It is therefore of interest as a possible biocatalyst for the synthesis of organosiloxanes. To further investigate [...] Read more.
Silicatein-α (Silα), a hydrolytic enzyme derived from siliceous marine sponges, is one of the few enzymes in nature capable of catalysing the metathesis of silicon–oxygen bonds. It is therefore of interest as a possible biocatalyst for the synthesis of organosiloxanes. To further investigate the substrate scope of this enzyme, a series of condensation reactions with a variety of phenols and aliphatic alcohols were carried out. In general, it was observed that Silα demonstrated a preference for phenols, though the conversions were relatively modest in most cases. In the two pairs of chiral alcohols that were investigated, it was found that the enzyme displayed a preference for the silylation of the S-enantiomers. Additionally, the enzyme’s tolerance to a range of solvents was tested. Silα had the highest level of substrate conversion in the nonpolar solvents n-octane and toluene, although the inclusion of up to 20% of 1,4-dioxane was tolerated. These results suggest that Silα is a potential candidate for directed evolution toward future application as a robust and selective biocatalyst for organosiloxane chemistry. Full article
(This article belongs to the Special Issue 10th Anniversary of Catalysts: Biocatalysis in Analysis and Synthesis—Past, Present and Future)
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15 pages, 2452 KiB  
Article
Synthesis and Laccase-Mediated Oxidation of New Condensed 1,4-Dihydropyridine Derivatives
by Jelena Milovanovic, Miyase Gözde Gündüz, Anastasia Zerva, Milos Petkovic, Vladimir Beskoski, Nikolaos S. Thomaidis, Evangelos Topakas and Jasmina Nikodinovic-Runic
Catalysts 2021, 11(6), 727; https://doi.org/10.3390/catal11060727 - 12 Jun 2021
Cited by 5 | Viewed by 3119
Abstract
We describe herein the synthesis and laccase mediated oxidation of six novel 1,4-dihydropyridine (DHP)-based hexahydroquinolines (DHP1-DHP3) and decahydroacridines (DHP4-DHP6). We employed different laccase enzymes with varying redox potential to convert DHP1-DHP3 and DHP4-DHP6 to the corresponding pyridine-containing tetrahydroquinoline and octahydroacridine derivatives, respectively. Intensively [...] Read more.
We describe herein the synthesis and laccase mediated oxidation of six novel 1,4-dihydropyridine (DHP)-based hexahydroquinolines (DHP1-DHP3) and decahydroacridines (DHP4-DHP6). We employed different laccase enzymes with varying redox potential to convert DHP1-DHP3 and DHP4-DHP6 to the corresponding pyridine-containing tetrahydroquinoline and octahydroacridine derivatives, respectively. Intensively coloured products were detected in all biocatalytic reactions using laccase from Trametes versicolor (TvLacc), possibly due to the presence of conjugated chromophores formed in products after oxidation. The NMR assessment confirmed that the oxidation product of DHP1 was its corresponding pyridine-bearing tetrahydroquinoline derivative. Laccase from Bacillus subtillis (BacillusLacc) was the most efficient enzyme for this group of substrates using HPLC assessment. Overall, it could be concluded that DHP2 and DHP5, bearing catecholic structures, were easily oxidized by all tested laccases, while DHP3 and DHP6 containing electron-withdrawing nitro-groups are not readily oxidized by laccases. DHP4 with decahydroacridine moiety consisting of three condensed six-membered rings that contribute not only to the volume but also to the higher redox potential of the substrate rendered this compound not to be biotransformed with any of the mentioned enzymes. Overall, we showed that multiple analytical approaches are needed in order to assess biocatalytical reactions. Full article
(This article belongs to the Special Issue 10th Anniversary of Catalysts: Biocatalysis in Analysis and Synthesis—Past, Present and Future)
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Review

Jump to: Editorial, Research

35 pages, 4133 KiB  
Review
The Power of Biocatalysts for Highly Selective and Efficient Phosphorylation Reactions
by Roland Wohlgemuth
Catalysts 2022, 12(11), 1436; https://doi.org/10.3390/catal12111436 - 15 Nov 2022
Cited by 6 | Viewed by 2841
Abstract
Reactions involving the transfer of phosphorus-containing groups are of key importance for maintaining life, from biological cells, tissues and organs to plants, animals, humans, ecosystems and the whole planet earth. The sustainable utilization of the nonrenewable element phosphorus is of key importance for [...] Read more.
Reactions involving the transfer of phosphorus-containing groups are of key importance for maintaining life, from biological cells, tissues and organs to plants, animals, humans, ecosystems and the whole planet earth. The sustainable utilization of the nonrenewable element phosphorus is of key importance for a balanced phosphorus cycle. Significant advances have been achieved in highly selective and efficient biocatalytic phosphorylation reactions, fundamental and applied aspects of phosphorylation biocatalysts, novel phosphorylation biocatalysts, discovery methodologies and tools, analytical and synthetic applications, useful phosphoryl donors and systems for their regeneration, reaction engineering, product recovery and purification. Biocatalytic phosphorylation reactions with complete conversion therefore provide an excellent reaction platform for valuable analytical and synthetic applications. Full article
(This article belongs to the Special Issue 10th Anniversary of Catalysts: Biocatalysis in Analysis and Synthesis—Past, Present and Future)
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21 pages, 3487 KiB  
Review
Catalyst-Based Biomolecular Logic Gates
by Dennis S. Winston and David D. Boehr
Catalysts 2022, 12(7), 712; https://doi.org/10.3390/catal12070712 - 29 Jun 2022
Cited by 3 | Viewed by 2612
Abstract
Regulatory processes in biology can be re-conceptualized in terms of logic gates, analogous to those in computer science. Frequently, biological systems need to respond to multiple, sometimes conflicting, inputs to provide the correct output. The language of logic gates can then be used [...] Read more.
Regulatory processes in biology can be re-conceptualized in terms of logic gates, analogous to those in computer science. Frequently, biological systems need to respond to multiple, sometimes conflicting, inputs to provide the correct output. The language of logic gates can then be used to model complex signal transduction and metabolic processes. Advances in synthetic biology in turn can be used to construct new logic gates, which find a variety of biotechnology applications including in the production of high value chemicals, biosensing, and drug delivery. In this review, we focus on advances in the construction of logic gates that take advantage of biological catalysts, including both protein-based and nucleic acid-based enzymes. These catalyst-based biomolecular logic gates can read a variety of molecular inputs and provide chemical, optical, and electrical outputs, allowing them to interface with other types of biomolecular logic gates or even extend to inorganic systems. Continued advances in molecular modeling and engineering will facilitate the construction of new logic gates, further expanding the utility of biomolecular computing. Full article
(This article belongs to the Special Issue 10th Anniversary of Catalysts: Biocatalysis in Analysis and Synthesis—Past, Present and Future)
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44 pages, 3722 KiB  
Review
A Review on Biological Synthesis of the Biodegradable Polymers Polyhydroxyalkanoates and the Development of Multiple Applications
by Bryan Dalton, Purabi Bhagabati, Jessica De Micco, Ramesh Babu Padamati and Kevin O’Connor
Catalysts 2022, 12(3), 319; https://doi.org/10.3390/catal12030319 - 11 Mar 2022
Cited by 85 | Viewed by 13610
Abstract
Polyhydroxyalkanoates, or PHAs, belong to a class of biopolyesters where the biodegradable PHA polymer is accumulated by microorganisms as intracellular granules known as carbonosomes. Microorganisms can accumulate PHA using a wide variety of substrates under specific inorganic nutrient limiting conditions, with many of [...] Read more.
Polyhydroxyalkanoates, or PHAs, belong to a class of biopolyesters where the biodegradable PHA polymer is accumulated by microorganisms as intracellular granules known as carbonosomes. Microorganisms can accumulate PHA using a wide variety of substrates under specific inorganic nutrient limiting conditions, with many of the carbon-containing substrates coming from waste or low-value sources. PHAs are universally thermoplastic, with PHB and PHB copolymers having similar characteristics to conventional fossil-based polymers such as polypropylene. PHA properties are dependent on the composition of its monomers, meaning PHAs can have a diverse range of properties and, thus, functionalities within this biopolyester family. This diversity in functionality results in a wide array of applications in sectors such as food-packaging and biomedical industries. In order for PHAs to compete with the conventional plastic industry in terms of applications and economics, the scale of PHA production needs to grow from its current low base. Similar to all new polymers, PHAs need continuous technological developments in their production and material science developments to grow their market opportunities. The setup of end-of-life management (biodegradability, recyclability) system infrastructure is also critical to ensure that PHA and other biobased biodegradable polymers can be marketed with maximum benefits to society. The biobased nature and the biodegradability of PHAs mean they can be a key polymer in the materials sector of the future. The worldwide scale of plastic waste pollution demands a reformation of the current polymer industry, or humankind will face the consequences of having plastic in every step of the food chain and beyond. This review will discuss the aforementioned points in more detail, hoping to provide information that sheds light on how PHAs can be polymers of the future. Full article
(This article belongs to the Special Issue 10th Anniversary of Catalysts: Biocatalysis in Analysis and Synthesis—Past, Present and Future)
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