Supported Biocatalysts for Sustainable Chemistry

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

Deadline for manuscript submissions: closed (31 January 2024) | Viewed by 10423

Special Issue 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,

Nowadays, significant developments in molecular biology and biotechnology are observed and open new avenues in synthetic chemistry where biological systems could be efficiently utilized in the laboratory. In addition to known natural biological protocols, modern enzyme engineering has enabled chemists to engineer artificial enzymatic reactions to efficiently match the predefined properties of the reaction. The proper use of the combination of solvents, substrates, reactors, and overall reaction conditions could further enhance biocatalyst applications. What is more, the use of nanotechnology in parallel with the immobilization of the catalyst improves the catalyst efficiency and gives the possibility to reuse catalysts in other catalytic cycles. Nevertheless, it is still essential to perform more efforts to apply the abovementioned green technology approaches in industrial processes toward sustainable growth.

This Special Issue, “Supported Biocatalysts for Sustainable Chemistry”, focuses on biocatalysis, enzymes, enzyme engineering, green chemistry and immobilization. All studies (experimental and theoretical) within the scope of this Special Issue, including original research and review articles, short communications, and perspective articles, are invited for submission.

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

  • biocatalysis
  • enzyme
  • enzyme engineering
  • green chemistry
  • immobilization

Published Papers (7 papers)

Order results
Result details
Select all
Export citation of selected articles as:

Research

13 pages, 1105 KiB  
Article
Resilient Enzymes through Immobilisation: Stable NDP Polyphosphate Phosphotransferase from Ruegeria pomeroyi for Nucleotide Regeneration
by Kristin Hölting, Sebastian Götz, Miriam Aßmann, Paul Bubenheim, Andreas Liese and Jürgen Kuballa
Catalysts 2024, 14(3), 165; https://doi.org/10.3390/catal14030165 - 24 Feb 2024
Viewed by 782
Abstract
Immobilisation plays an important role in the industrial application of enzymes. The stabilisation and reusability of immobilised enzymes reduce the cost of the catalyst and facilitate their use in continuously operated reactors. For this purpose, an applicable type of immobilisation needs to be [...] Read more.
Immobilisation plays an important role in the industrial application of enzymes. The stabilisation and reusability of immobilised enzymes reduce the cost of the catalyst and facilitate their use in continuously operated reactors. For this purpose, an applicable type of immobilisation needs to be identified. In this study, we investigate the conversion of CDP and PolyP to CTP by NDP polyphosphate phosphotransferase 3 from Ruegeria pomeroyi (RpPPK2-3) and describe the covalent immobilisation of RpPPK2-3. In order to select a suitable carrier for the immobilisation of RpPPK2-3, a screening with different amino methacrylate (glutaraldehyde-pre-activated) and epoxy methacrylate carriers was carried out. The epoxy methacrylate carrier ECR8209M (Purolite®) was found to be the most suitable. With a half-life of 462 d when stored at 6 °C and a 50-fold reusability with a 93% residual activity, the immobilised enzyme showed a higher stability compared to the soluble enzyme with a half-life of 0.04 d. Although the half-life of the soluble enzyme could be increased to 32 d by adding PPi, it could not reach the stability of the immobilisate. Due to the resilience of the immobilisate, it is suitable for application in continuous reactor set-ups, e.g., packed-bed reactors. Full article
(This article belongs to the Special Issue Supported Biocatalysts for Sustainable Chemistry)
Show Figures

Graphical abstract

16 pages, 1516 KiB  
Article
The Studies of Sepharose-Immobilized Lipases: Combining Techniques for the Enhancement of Activity and Thermal Stability
by Tomasz Siódmiak, Jacek Dulęba, Gudmundur G. Haraldsson, Joanna Siódmiak and Michał Piotr Marszałł
Catalysts 2023, 13(5), 887; https://doi.org/10.3390/catal13050887 - 15 May 2023
Viewed by 1375
Abstract
Thermal stability is one of the essential parameters characterizing biocatalysts with potential applications in the chemical and pharmaceutical industries. Therefore, it is extremely important to develop standardized procedures for enzyme stability studies. The paper attempts to assess the thermal stability of immobilized lipases [...] Read more.
Thermal stability is one of the essential parameters characterizing biocatalysts with potential applications in the chemical and pharmaceutical industries. Therefore, it is extremely important to develop standardized procedures for enzyme stability studies. The paper attempts to assess the thermal stability of immobilized lipases in aqueous buffers: lipase B from Candida antarctica (CALB) and lipase from Candida rugosa (CRL-OF) immobilized on the Octyl-Sepharose CL-4B carrier. As part of the optimization conditions of the immobilization, the influence of time on the catalytic activity and lipase loading, as well as the effect of temperature on lipase activity (optimal incubation—14 h at 4 °C), was determined. The thermal stability test procedure was carried out for 7 days using a climatic chamber (65 °C) and a refrigerator (4 °C). The studies of immobilized lipases included the assessment of the impact of various solvents (water, citrate buffer, 1,2-dichloropropane—DCP), temperature, light in the visible spectral range (400–800 nm), and additions of calcium ions. The highest value of residual activity (564.5 ± 21.6%) was received by storing the immobilized CALB in citrate buffer (pH 4.0, 500 mM) with the addition of calcium ions (Ca2+). On the other hand, residual activity values for immobilized CRL-OF after storage in the climatic chamber were lower than 5%. A combining of techniques: immobilization onto the support in high ionic strength and low pH, with a technique of extremally high-temperature applied in a climatic chamber, with the addition of Ca2+ allowed to achieve of excellent thermal stability of the immobilized CALB, with increasing of catalytic activity more than five-fold. Additionally, performing studies on the thermal stability of the tested lipases using a climatic chamber seems to be particularly promising in the context of unifying and standardizing storage guidelines, enabling the comparison of results between different laboratories, as well as enhancing catalytic activity. Full article
(This article belongs to the Special Issue Supported Biocatalysts for Sustainable Chemistry)
Show Figures

Figure 1

15 pages, 1122 KiB  
Article
Biosynthesis of Furfurylamines in Batch and Continuous Flow by Immobilized Amine Transaminases
by Tobias Heinks, Luisa M. Merz, Jan Liedtke, Matthias Höhne, Luuk M. van Langen, Uwe T. Bornscheuer, Gabriele Fischer von Mollard and Per Berglund
Catalysts 2023, 13(5), 875; https://doi.org/10.3390/catal13050875 - 11 May 2023
Cited by 3 | Viewed by 2428
Abstract
Building blocks with amine functionality are crucial in the chemical industry. Biocatalytic syntheses and chemicals derived from renewable resources are increasingly desired to achieve sustainable production of these amines. As a result, renewable materials such as furfurals, especially furfurylamines like 5-(hydroxymethyl)furfurylamine (HMFA) and [...] Read more.
Building blocks with amine functionality are crucial in the chemical industry. Biocatalytic syntheses and chemicals derived from renewable resources are increasingly desired to achieve sustainable production of these amines. As a result, renewable materials such as furfurals, especially furfurylamines like 5-(hydroxymethyl)furfurylamine (HMFA) and 2,5-di(aminomethyl)furan (DAF), are gaining increasing attention. In this study, we identified four different amine transaminases (ATAs) that catalyze the reductive amination of 5-(hydroxymethyl)furfural (HMF) and 2,5-diformylfuran (DFF). We successfully immobilized these ATAs on glutaraldehyde-functionalized amine beads using multiple binding and on amine beads by site-selective binding of the unique Cα-formylglycine within an aldehyde tag. All immobilized ATAs were efficiently reused in five repetitive cycles of reductive amination of HMF with alanine as co-substrate, while the ATA from Silicibacter pomeroyi (ATA-Spo) also exhibited high stability for reuse when isopropylamine was used as an amine donor. Additionally, immobilized ATA-Spo yielded high conversion in the batch syntheses of HMFA and DAF using alanine (87% and 87%, respectively) or isopropylamine (99% and 98%, respectively) as amine donors. We further demonstrated that ATA-Spo was effective for the reductive amination of HMF with alanine or isopropylamine in continuous-flow catalysis with high conversion up to 12 days (48% and 41%, respectively). Full article
(This article belongs to the Special Issue Supported Biocatalysts for Sustainable Chemistry)
Show Figures

Figure 1

16 pages, 1299 KiB  
Article
Climatic Chamber Stability Tests of Lipase-Catalytic Octyl-Sepharose Systems
by Tomasz Siódmiak, Joanna Siódmiak, Rafał Mastalerz, Natalia Kocot, Jacek Dulęba, Gudmundur G. Haraldsson, Dorota Wątróbska-Świetlikowska and Michał Piotr Marszałł
Catalysts 2023, 13(3), 501; https://doi.org/10.3390/catal13030501 - 28 Feb 2023
Cited by 1 | Viewed by 1126
Abstract
The application of the climatic chamber presented in this paper to assess the storage stability of immobilized lipases is a new approach characterized by the potential of unifying the study conditions of biocatalysts created in various laboratories. The data achieved from storing lipases [...] Read more.
The application of the climatic chamber presented in this paper to assess the storage stability of immobilized lipases is a new approach characterized by the potential of unifying the study conditions of biocatalysts created in various laboratories. The data achieved from storing lipases in the climatic chambers may be crucial for the chemical and pharmaceutical industry. Our paper describes the developed protocols for immobilization via interfacial activation of lipase B from Candida antarctica (CALB) and lipase OF from Candida rugosa (CRL-OF) on the Octyl-Sepharose CL-4B support. Optimization included buffers with different pH values of 4–9 and a wide range of ionic strength from 5 mM to 700 mM. It has been shown that the optimal medium for the CALB immobilization process on the tested support is a citrate buffer at pH 4 and high ionic strength of 500 mM. Implementing new optimal procedures enabled the hyperactivation of immobilized CALB (recovery activity 116.10 ± 1.70%) under the applicable reaction conditions using olive oil as a substrate. Importantly, CALB storage stability tests performed in a climatic chamber under drastic temperature and humidity conditions proved good stability of the developed biocatalyst (residual activity 218 ± 7.3% of dry form, after 7 days). At the same time, the low storage stability of CRL OF in a climatic chamber was demonstrated. It should be emphasized that the use of a climatic chamber to test the storage stability of a dry form of the studied lipases immobilized on Octyl-Sepharose CL-4B is, to our knowledge, described for the first time in the literature. Full article
(This article belongs to the Special Issue Supported Biocatalysts for Sustainable Chemistry)
Show Figures

Figure 1

14 pages, 2535 KiB  
Article
The Application of Two-Phase Catalytic System in Enantioselective Separation of Racemic (R,S)-1-Phenylethanol
by Joanna Chałupka, Jacek Dulęba, Adam Sikora, Tomasz Siódmiak and Michał Piotr Marszałł
Catalysts 2023, 13(2), 292; https://doi.org/10.3390/catal13020292 - 28 Jan 2023
Cited by 2 | Viewed by 1341
Abstract
Kinetic resolution is one of the methods which allows obtaining enantiomerically pure compounds. In the study presented herein, enantioselective biotransformations of (R,S)-1-phenylethanol were performed with the use of various catalytic systems containing ionic liquids and n-heptane or toluene as a [...] Read more.
Kinetic resolution is one of the methods which allows obtaining enantiomerically pure compounds. In the study presented herein, enantioselective biotransformations of (R,S)-1-phenylethanol were performed with the use of various catalytic systems containing ionic liquids and n-heptane or toluene as a reaction medium, vinyl acetate or isopropenyl acetate as an acetylating agent, and lipases from Burkholderia cepacia or Candida rugosa. The conducted studies proved that the use of Burkholderia cepacia lipase, vinyl acetate, and n-heptane with [EMIM][BF4] allows obtaining enantiomerically pure 1-phenylethyl acetate, with the enantiomeric excess of products eep = 98.9%, conversion c = 40.1%, and high value of enantioselectivity E > 200. Additionally, the use of ionic liquids allowed us to reuse enzyme in 5 reaction cycles, ensuring the high operational stability of the protein. Full article
(This article belongs to the Special Issue Supported Biocatalysts for Sustainable Chemistry)
Show Figures

Figure 1

10 pages, 1025 KiB  
Communication
Technical–Economic Assessment—The Missing Piece for Increasing the Attractiveness of Applied Biocatalysis in Ester Syntheses?
by Ronaldo Rodrigues de Sousa, Rui de Paula Vieira de Castro, Nadinne Medeiros Assis, Ayla Sant’Ana da Silva, Denise Maria Guimarães Freire, Roberto Fernandez-Lafuente and Viridiana Santana Ferreira-Leitão
Catalysts 2023, 13(2), 223; https://doi.org/10.3390/catal13020223 - 18 Jan 2023
Cited by 1 | Viewed by 1451
Abstract
Although the current literature describes significant advances in biocatalytic ester syntheses, few industrial plants worldwide are currently producing esters using biocatalysts. Green and sustainable esters can be obtained via a biocatalytic route, including some operational advantages over conventional syntheses. An analysis of the [...] Read more.
Although the current literature describes significant advances in biocatalytic ester syntheses, few industrial plants worldwide are currently producing esters using biocatalysts. Green and sustainable esters can be obtained via a biocatalytic route, including some operational advantages over conventional syntheses. An analysis of the literature revealed that most articles neglect or describe the economic issues generically, without quantitative information. Scaling-up studies are also scarce in this field. The main disadvantage of biocatalysis using immobilized lipases—their cost—has not been studied at the same level of depth as other technical aspects. This gap in the literature is less intense in enzymatic biodiesel production studies and, despite the lack of a strict correlation, enzymatic biodiesel commercial plants are relatively more common. Preliminary techno-economic assessments are crucial to identify and circumvent the economic drawbacks of biocatalytic ester syntheses, opening the way to broader application of this technology in a large-scale context. Full article
(This article belongs to the Special Issue Supported Biocatalysts for Sustainable Chemistry)
Show Figures

Graphical abstract

12 pages, 1444 KiB  
Article
The Utilization of Two-Phase Catalytic System in Enantioselective Biotransformation of Racemic Atenolol
by Joanna Chałupka, Adam Sikora and Michał Piotr Marszałł
Catalysts 2022, 12(9), 1068; https://doi.org/10.3390/catal12091068 - 19 Sep 2022
Cited by 2 | Viewed by 1212
Abstract
There are several methods that allow enantiomerically pure compounds to be obtained. In the study presented herein, the enantioselective biotransformations of (R,S)-atenolol were performed with the use of various catalytic systems containing ionic liquids and toluene as a reaction [...] Read more.
There are several methods that allow enantiomerically pure compounds to be obtained. In the study presented herein, the enantioselective biotransformations of (R,S)-atenolol were performed with the use of various catalytic systems containing ionic liquids and toluene as a reaction medium, vinyl acetate as an acetylating agent as well as lipases from Candida rugosa. The conducted studies profs that, the use of the two-phase reaction system enables the reuse of the biocatalyst in another cycle and allows to achieve satisfactory kinetic resolution parameters. Full article
(This article belongs to the Special Issue Supported Biocatalysts for Sustainable Chemistry)
Show Figures

Figure 1

Back to TopTop