Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
6.3
3.9
Journals
Catalysts
Special Issues
Enzyme-Catalyzed Biotransformations
share announcement

Enzyme-Catalyzed Biotransformations

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

Deadline for manuscript submissions: closed (30 September 2020) | Viewed by 14529

Special Issue Editor

Dr. Adam Sikora

E-Mail Website
Guest Editor
Department of Medicinal Chemistry, Collegium Medicum in Bydgoszcz, Faculty of Pharmacy, Nicolaus Copernicus University in Toruń, Dr. A. Jurasza 2, 85-089 Bydgoszcz, Poland
Interests: biocatalysis; enzyme; enzyme engineering; green chemistry; immobilization
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Today, enzyme-catalyzed biotransformations are recognized as an alternative to conventional chemical methods in chiral synthesis, with biocatalysis attracting significant attention mainly due to its high selectivity and mild reaction conditions. In recent decades, the use of biotransformation in the industry and academic society has rapidly increased based on the efficiency of the enzymes catalyzing different types of chemical transformations and their low environmental impact as well as high selectivity, lack of cofactor dependency, and ability to work in aqueous and/or organic media. Enzymes such as esterases, lipases, and proteases have allowed the production of various groups of products, such as biodiesel, agrochemicals, pharmaceuticals, and cosmetic products with great regio- and chemoselectivity during the catalytical process. Activation or protection and deprotection steps of functional groups is usually not required for enzyme-catalyzed biotransformations. What is more, a complex chemical synthesis process involving the product with multiple chiral centers may be resolved by a simple and elegant bioconversion process. Therefore, the reduced number of process steps makes biotransformation more environmentally and economically attractive.

This Special Issue is devoted to the application of various enzymatic catalytic systems in the biotransformation of chiral compounds. Reviews and original research papers are invited. The potential topics include but are not limited to:

  • New approaches in enzyme-catalyzed biotransformations;
  • Heterogeneous catalysis including immobilized molecular catalysts;
  • Heterogeneous catalysis including native molecular catalysts;
  • Biotransformation mechanisms and kinetics;
  • Enzyme immobilization protocol in the biotransformation of chiral entities.

Dr. Adam Sikora
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. 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

  • Biotransformation 
  • Enzyme 
  • Kinetic Resolution 
  • Lipase 
  • Chemoselectivity 
  • Regioselectivity 
  • Enantioselective biocatalysis 
  • Immobilization 
  • Enzyme activity 
  • Streoinversion

Published Papers (4 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

Jump to: Review

21 pages, 1432 KiB  
Article
Evaluation of Designed Immobilized Catalytic Systems: Activity Enhancement of Lipase B from Candida antarctica
by Tomasz Siódmiak, Gudmundur G. Haraldsson, Jacek Dulęba, Marta Ziegler-Borowska, Joanna Siódmiak and Michał Piotr Marszałł
Catalysts 2020, 10(8), 876; https://doi.org/10.3390/catal10080876 - 04 Aug 2020
Cited by 13 | Viewed by 3557
Abstract
Immobilized enzymatic catalysts are widely used in the chemical and pharmaceutical industries. As Candida antarctica lipase B (CALB) is one of the more commonly used biocatalysts, we attempted to design an optimal lipase-catalytic system. In order to do that, we investigated the enantioselectivity [...] Read more.
Immobilized enzymatic catalysts are widely used in the chemical and pharmaceutical industries. As Candida antarctica lipase B (CALB) is one of the more commonly used biocatalysts, we attempted to design an optimal lipase-catalytic system. In order to do that, we investigated the enantioselectivity and lipolytic activity of CALB immobilized on 12 different supports. Immobilization of lipase on IB-D152 allowed us to achieve hyperactivation (178%) in lipolytic activity tests. Moreover, the conversion in enantioselective esterification increased 43-fold, when proceeding with lipase-immobilized on IB-S861. The immobilized form exhibited a constant high catalytic activity in the temperature range of 25 to 55 °C. Additionally, the lipase immobilized on IB-D152 exhibited a higher lipolytic activity in the pH range of 6 to 9 compared with the native form. Interestingly, our investigations showed that IB-S500 and IB-S60S offered a possibility of application in catalysis in both organic and aqueous solvents. A significant link between the reaction media, the substrates, the supports and the lipase was confirmed. In our enzymatic investigations, high-performance liquid chromatography (HPLC) and the titrimetric method, as well as the Bradford method were employed. Full article
(This article belongs to the Special Issue Enzyme-Catalyzed Biotransformations)
►▼ Show Figures

Figure 1

11 pages, 2613 KiB  
Article
The Use of Ion Liquids as a Trojan Horse Strategy in Enzyme-Catalyzed Biotransformation of (R,S)-Atenolol
by Adam Sikora, Joanna Chałupka and Michał Piotr Marszałł
Catalysts 2020, 10(7), 787; https://doi.org/10.3390/catal10070787 - 14 Jul 2020
Cited by 4 | Viewed by 2380
Abstract
The enzymatic method was used for the direct biotransformation of racemic atenolol. The catalytic activities of commercially available lipases from Candida rugosa were tested for the kinetic resolution of (R,S)-atenolol by enantioselective acetylation in various two-phase reaction media containing [...] Read more.
The enzymatic method was used for the direct biotransformation of racemic atenolol. The catalytic activities of commercially available lipases from Candida rugosa were tested for the kinetic resolution of (R,S)-atenolol by enantioselective acetylation in various two-phase reaction media containing ionic liquids. The composed catalytic system gave the possibility to easy separate substrates and products of the conducted enantioselective reaction and after specific procedure to reuse utilized enzymes in another catalytic cycle. Full article
(This article belongs to the Special Issue Enzyme-Catalyzed Biotransformations)
►▼ Show Figures

Figure 1

14 pages, 2463 KiB  
Article
Enzymatic Synthesis of O-Methylated Phenophospholipids by Lipase-Catalyzed Acidolysis of Egg-Yolk Phosphatidylcholine with Anisic and Veratric Acids
by Marta Okulus and Anna Gliszczyńska
Catalysts 2020, 10(5), 538; https://doi.org/10.3390/catal10050538 - 13 May 2020
Cited by 10 | Viewed by 2403
Abstract
Lipase-catalyzed acidolysis reactions of egg-yolk phosphatidylcholine (PC) with anisic (ANISA) and veratric (VERA) acids were investigated to develop a biotechnological method for the production of corresponding biologically active O-methylated phenophospholipids. Screening experiments with four commercially available immobilized lipases indicated that the most [...] Read more.
Lipase-catalyzed acidolysis reactions of egg-yolk phosphatidylcholine (PC) with anisic (ANISA) and veratric (VERA) acids were investigated to develop a biotechnological method for the production of corresponding biologically active O-methylated phenophospholipids. Screening experiments with four commercially available immobilized lipases indicated that the most effective biocatalyst for the incorporation of ANISA into phospholipids was Novozym 435. None of the tested enzymes were able to catalyze the synthesis of PC structured with VERA. The effects of different solvents, substrate molar ratios, temperature, enzyme loading, and time of the reaction on the process of incorporation of ANISA into the phospholipids were evaluated in the next step of the study. The mixture of toluene/chloroform in the ratio 9:1 (v/v) significantly increased the incorporation of ANISA into PC. The acidolysis reaction was carried out using the selected binary solvent system, 1/15 substrate molar ratio PC/ANISA, 30% (w/w) enzyme load, and temperature of 50 °C afforded after 72 h anisoylated lysophosphatidylcholine (ANISA-LPC) and anisoylated phosphatidylcholine (ANISA-PC) in isolated yields of 28.5% and 2.5% (w/w), respectively. This is the first study reporting the production of ANISA-LPC and ANISA-PC via a one-step enzymatic method, which is an environmentally friendly alternative to the chemical synthesis of these biologically active compounds. Full article
(This article belongs to the Special Issue Enzyme-Catalyzed Biotransformations)
►▼ Show Figures

Figure 1

Review

Jump to: Research

30 pages, 7307 KiB  
Review
Biocatalysis in the Swiss Manufacturing Environment
by Katrin Hecht, Hans-Peter Meyer, Roland Wohlgemuth and Rebecca Buller
Catalysts 2020, 10(12), 1420; https://doi.org/10.3390/catal10121420 - 04 Dec 2020
Cited by 11 | Viewed by 5544
Abstract
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 [...] Read more.
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. Full article
(This article belongs to the Special Issue Enzyme-Catalyzed Biotransformations)
►▼ Show Figures

Graphical abstract

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-4
Back to TopTop