Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
7.4
4.2
Journals
Molecules
Special Issues
Applications of Microbial Enzymes in Organic Synthesis
molecules-logo
Submit to Molecules Review for Molecules Propose a Special Issue

Journal Menu

► Journal Menu

Journal Browser

► Journal Browser
share announcement

Applications of Microbial Enzymes in Organic Synthesis

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Organic Chemistry".

Deadline for manuscript submissions: closed (31 December 2021) | Viewed by 9267

Special Issue Editor

Prof. Dr. Maciej Szaleniec

E-Mail Website
Guest Editor
Jerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, Niezapominajek 8, 30-239 Krakow, Poland
Interests: metalloenzymes; catalytic mechanisms; enzymes from anaerobic metabolic pathways; modelling enzymatic reactions; reaction engineering
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The world is teeming with microorganisms occupying the most diverse ecological niches. Each of these species developed a unique set of enzymes to process food and respiratory resources or build organic molecules. The more unusual the living conditions were the more bizarre the catalytic solutions evolved. This still untapped resource has recently started to find its way into organic labs and industrial synthesis. Thanks to the effectiveness of recombinant enzyme production and a rapid increase of knowledge of genomic sequences we are gaining access to novel enzymes even from organisms that are still unculturable.

Yet another reason for the increasing popularity of enzymes is the mastering of robust hydrolases that are resistant to organic solvents and catalyze a range of reactions not encountered in living organisms e.g, promiscuous lipases catalyzing not only esterification and transamination, but also organic reactions such as Bayer–Villiger oxidation; Knoevenagel condensation; Pudovik–Abramov, Ugi and Passerini, or Mannich reactions. We observe the gradual transfer of enzymes from biotechnological labs to classical organic laboratories. Enzymes are no longer the domain of biologists—they are becoming ingredients in organic reactions.

Finally, we experience a “revolution based on (directed) evolution” gaining access to the new-to-nature enzymatic activities, such as C–C or C–Si bond formation by the modified P450 enzyme (know called P411).

The main aim of the Special Issue “Applications of Microbial Enzymes in Organic Synthesis” is to be an open forum where one can demonstrate their recent discoveries in the field of biocatalysis and organic chemistry. Thanks to the OA form of the Catalysts journal, we expect the published articles to gain high. Contributions to this Issue, both in the form of original research or review articles, may cover all aspects of biocatalytic reactions conducted with enzymes, whole-cell biotransformations, the development of promiscuous enzymatic reactions, or the discovery of new enzymatic activities. We also invite contributions not limited to bacterial enzymes but covering the widest understanding of microbial origins.

Prof. Dr. Maciej Szaleniec
Guest Editor

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. Molecules is an international peer-reviewed open access semimonthly 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

  • bacterial enzymes
  • algal enzymes
  • fungal enzymes
  • archaeal enzymes
  • organic synthesis
  • directed evolution
  • rational design
  • promiscuous enzyme

Benefits of Publishing in a Special Issue

  • Ease of navigation: Grouping papers by topic helps scholars navigate broad scope journals more efficiently.
  • Greater discoverability: Special Issues support the reach and impact of scientific research. Articles in Special Issues are more discoverable and cited more frequently.
  • Expansion of research network: Special Issues facilitate connections among authors, fostering scientific collaborations.
  • External promotion: Articles in Special Issues are often promoted through the journal's social media, increasing their visibility.
  • e-Book format: Special Issues with more than 10 articles can be published as dedicated e-books, ensuring wide and rapid dissemination.

Further information on MDPI's Special Issue polices can be found here.

Published Papers (3 papers)

Download All Papers
Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

11 pages, 2320 KiB  
Article
Role of Endogenous Cathepsin L in Muscle Protein Degradation in Olive Flounder (Paralichthys olivaceus) Surimi Gel
by Chang Woo Kwon and Pahn-Shick Chang
Molecules 2021, 26(7), 1901; https://doi.org/10.3390/molecules26071901 - 28 Mar 2021
Cited by 7 | Viewed by 2327
Abstract
We investigated the effect of endogenous cathepsin L on surimi gel produced from olive flounder (Paralichthys olivaceus). The amino acid sequences of six proteins predicted or identified as cathepsin L were obtained from the olive flounder genome database, and a phylogenetic [...] Read more.
We investigated the effect of endogenous cathepsin L on surimi gel produced from olive flounder (Paralichthys olivaceus). The amino acid sequences of six proteins predicted or identified as cathepsin L were obtained from the olive flounder genome database, and a phylogenetic analysis was conducted. Next, cathepsin L activity toward N-α-benzyloxycarbonyl-l-phenylalanyl-l-arginine-(7-amino-4-methylcoumarin) (Z-F-R-AMC) was detected in crude olive flounder extract and a crude enzyme preparation. A considerable decrease in the level of myosin heavy chain (MHC) in surimi occurred during autolysis at 60 °C. In contrast, the levels of actin, troponin-T, and tropomyosin decreased only slightly. To prevent protein degradation by cathepsin L, a protease inhibitor was added to surimi. In the presence of 1.0% protease inhibitor, the autolysis of olive flounder surimi at 60 °C was inhibited by 12.2%; the degree of inhibition increased to 44.2% as the inhibitor concentration increased to 3.0%. In addition, the deformation and hardness of modori gel increased as the inhibitor concentration increased to 2.0%. Therefore, cathepsin L plays an important role in protein degradation in surimi, and the quality of surimi gel could be enhanced by inhibiting its activity. Full article
(This article belongs to the Special Issue Applications of Microbial Enzymes in Organic Synthesis)
►▼ Show Figures

Figure 1

15 pages, 362 KiB  
Article
Microbial Synthesis of (S)- and (R)-Benzoin in Enantioselective Desymmetrization and Deracemization Catalyzed by Aureobasidium pullulans Included in the Blossom Protect™ Agent
by Renata Kołodziejska, Renata Studzińska, Agnieszka Tafelska-Kaczmarek, Hanna Pawluk, Dominika Mlicka and Alina Woźniak
Molecules 2021, 26(6), 1578; https://doi.org/10.3390/molecules26061578 - 12 Mar 2021
Cited by 4 | Viewed by 3392
Abstract
In this study, we examined the Aureobasidium pullulans strains DSM 14940 and DSM 14941 included in the Blossom Protect™ agent to be used in the bioreduction reaction of a symmetrical dicarbonyl compound. Both chiral 2-hydroxy-1,2-diphenylethanone antipodes were obtained with a high enantiomeric purity. [...] Read more.
In this study, we examined the Aureobasidium pullulans strains DSM 14940 and DSM 14941 included in the Blossom Protect™ agent to be used in the bioreduction reaction of a symmetrical dicarbonyl compound. Both chiral 2-hydroxy-1,2-diphenylethanone antipodes were obtained with a high enantiomeric purity. Mild conditions (phosphate buffer [pH 7.0, 7.2], 30 °C) were successfully employed in the synthesis of (S)-benzoin using two different methodologies: benzyl desymmetrization and rac-benzoin deracemization. Bioreduction carried out with higher reagent concentrations, lower pH values and prolonged reaction time, and in the presence of additives, enabled enrichment of the reaction mixture with (R)-benzoin. The described procedure is a potentially useful tool in the synthesis of chiral building blocks with a defined configuration in a simple and economical process with a lower environmental impact, enabling one-pot biotransformation. Full article
(This article belongs to the Special Issue Applications of Microbial Enzymes in Organic Synthesis)
►▼ Show Figures

Scheme 1

15 pages, 5527 KiB  
Article
Production of Enantiopure Chiral Epoxides with E. coli Expressing Styrene Monooxygenase
by Dominika Gyuranová, Radka Štadániová, Zuzana Hegyi, Róbert Fischer and Martin Rebroš
Molecules 2021, 26(6), 1514; https://doi.org/10.3390/molecules26061514 - 10 Mar 2021
Cited by 3 | Viewed by 2709
Abstract
Styrene monooxygenases are a group of highly selective enzymes able to catalyse the epoxidation of alkenes to corresponding chiral epoxides in excellent enantiopurity. Chiral compounds containing oxirane ring or products of their hydrolysis represent key building blocks and precursors in organic synthesis in [...] Read more.
Styrene monooxygenases are a group of highly selective enzymes able to catalyse the epoxidation of alkenes to corresponding chiral epoxides in excellent enantiopurity. Chiral compounds containing oxirane ring or products of their hydrolysis represent key building blocks and precursors in organic synthesis in the pharmaceutical industry, and many of them are produced on an industrial scale. Two-component recombinant styrene monooxygenase (SMO) from Marinobacterium litorale was expressed as a fused protein (StyAL2StyB) in Escherichia coli BL21(DE3). By high cell density fermentation, 35 gDCW/L of biomass with overexpressed SMO was produced. SMO exhibited excellent stability, broad substrate specificity, and enantioselectivity, as it remained active for months and converted a group of alkenes to corresponding chiral epoxides in high enantiomeric excess (˃95–99% ee). Optically pure (S)-4-chlorostyrene oxide, (S)-allylbenzene oxide, (2R,5R)-1,2:5,6-diepoxyhexane, 2-(3-bromopropyl)oxirane, and (S)-4-(oxiran-2-yl)butan-1-ol were prepared by whole-cell SMO. Full article
(This article belongs to the Special Issue Applications of Microbial Enzymes in Organic Synthesis)
►▼ Show Figures

Figure 1

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-3
Back to TopTop