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Catalysts
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State-of-the-Art Enzyme Engineering and Biocatalysis in Europe
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State-of-the-Art Enzyme Engineering and Biocatalysis in Europe

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

Deadline for manuscript submissions: 31 July 2026 | Viewed by 8538

Special Issue Editors

Dr. Teodora Bavaro

E-Mail Website
Guest Editor
Department of Drug Sciences, University of Pavia, Viale Taramelli 12, I-27100 Pavia, Italy
Interests: chemoenzymatic synthesis; medicinal chemistry; biocatalysis; protein engineering
Special Issues, Collections and Topics in MDPI journals
Dr. Marina Simona Robescu

E-Mail Website
Guest Editor
Department of Drug Sciences, University of Pavia, Viale Taramelli 12, 27100 Pavia, Italy
Interests: fermentation; biocatalysis; circular economy

Special Issue Information

Dear Colleagues,

Enzyme engineering and biocatalysis represent key technologies at the interface of molecular biology, chemistry, and process engineering, offering sustainable and efficient solutions for the production of pharmaceuticals, fine chemicals, agrochemicals, bio-based materials, and more. Europe has a distinguished tradition of excellence in this field, actively driving innovation through interdisciplinary collaborations and robust industrial partnerships.

In alignment with the priorities of the European Green Deal and the objectives of Horizon Europe, this Special Issue aims to highlight the role of enzyme engineering and biocatalysis in advancing green and circular economy goals, reducing environmental impact, fostering an efficient use of resources, and enabling the sustainable production of pharmaceuticals, fine chemicals, and bio-based products.

To this end, we welcome submissions of original research articles and review papers. Topics of interest include, but are not limited to, the following:

  • Rational design and directed evolution of enzymes for improved performance and selectivity.
  • Biocatalytic approaches for the sustainable synthesis of pharmaceuticals, fine chemicals, and value-added products.
  • Insights into enzyme structure–function relationships and catalytic mechanisms.
  • Innovative strategies for enzyme immobilization and process intensification.
  • Development of multi-enzyme cascade reactions and integration with chemical catalysis.
  • Application of computational methods and artificial intelligence in enzyme design and pathway optimization.
  • Advances in bioprocess engineering for scalable and efficient biocatalytic production.

We are confident that this Special Issue will provide an inspiring overview of the state of enzyme engineering and biocatalysis in Europe, fostering collaboration and innovation across the scientific community, while contributing to the overarching goals of European research and sustainable development.

Dr. Teodora Bavaro
Dr. Marina S. Robescu
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 250 words) can be sent to the Editorial Office for assessment.

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

  • enzyme engineering
  • biocatalysis
  • directed evolution
  • enzyme immobilization
  • multi-enzyme cascade reactions
  • bioprocess engineering
  • chemoenzymatic synthesis

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Published Papers (5 papers)

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Research

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17 pages, 4014 KB  
Article
Chemo-Enzymatic Synthesis of Enantiopure (−)-Nebivolol Catalyzed by Lipase B from Candida antarctica
by Eline Flo Hoem, Sara Aasen, Aurore Massacrier, Romain Bourgade, Petter Daleng and Elisabeth Egholm Jacobsen
Catalysts 2026, 16(3), 256; https://doi.org/10.3390/catal16030256 - 11 Mar 2026
Viewed by 567
Abstract
All four isomers of 2-chloro-1-(6-fluorochroman-2-yl)ethan-1-ol, as building blocks for the two enantiomers of beta-blocker nebivolol, have been synthesized in high yield. Due to the similar physicochemical properties of these four diastereomeric halohydrins, to date, the only successful method for separation of the isomers [...] Read more.
All four isomers of 2-chloro-1-(6-fluorochroman-2-yl)ethan-1-ol, as building blocks for the two enantiomers of beta-blocker nebivolol, have been synthesized in high yield. Due to the similar physicochemical properties of these four diastereomeric halohydrins, to date, the only successful method for separation of the isomers has been preparative HPLC. To avoid this, the four halohydrins were transformed into epoxides with subsequent separation of the enantiomeric pairs by column chromatography. The enantiomeric pairs of epoxides were subsequently converted back to their corresponding halohydrins before performing kinetic resolution of the racemates catalyzed by Lipase B from Candida antarctica. (R)-2-Chloro-1-((R)-6-fluorochroman-2-yl)ethanol was isolated in 71% yield, and >99% enantiomeric excess (ee). (R)-2-Chloro-1-((S)-6-fluorochroman-2-yl)ethanol was isolated in 77% yield and >99% ee. Hydrolysis of 2-chloro-1-(6-fluorochroman-2-yl)ethyl butanoate with the same lipase yielded halohydrins (S)-2-chloro-1-((S)-6-fluorochroman-2-yl)ethanol and (S)-2-chloro-1-((R)-6-fluorochroman-2-yl)ethanol. Amination of (R)-6-fluoro-2-((S)-oxiran-2-yl)chromane with ammonia afforded (S)-2-amino-1-((R)-6-fluorochroman-2-yl)ethanol in 79% yield and >99% ee. (S)-2-Amino-1-((R)-6-fluorochroman-2-yl)ethanol was then reacted with (R)-2-chloro-1-((S)-6-fluorochroman-2-yl)ethanol to produce the desired product (R,S,S,S)-nebivolol ((−)-nebivolol) in 81% yield and >99% ee. Full article
(This article belongs to the Special Issue State-of-the-Art Enzyme Engineering and Biocatalysis in Europe)
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15 pages, 2020 KB  
Article
Comparative Analysis of G-Quadruplex DNAzyme Scaffolds and Split Modes for Programmable Biosensing
by Dunsin S. Osalaye, Raphael I. Adeoye, Sylvia O. Malomo and Femi J. Olorunniji
Catalysts 2026, 16(1), 27; https://doi.org/10.3390/catal16010027 - 30 Dec 2025
Cited by 1 | Viewed by 496
Abstract
G-quadruplex (G4) DNAzymes, guanine-rich sequences that fold into four-stranded structures and bind hemin to mimic peroxidase activity, are widely used in biosensing. Split G4 DNAzymes offer conditional activation upon target recognition, enabling high specificity and modularity. However, achieving low OFF-state leakage remains a [...] Read more.
G-quadruplex (G4) DNAzymes, guanine-rich sequences that fold into four-stranded structures and bind hemin to mimic peroxidase activity, are widely used in biosensing. Split G4 DNAzymes offer conditional activation upon target recognition, enabling high specificity and modularity. However, achieving low OFF-state leakage remains a major challenge. Here, we systematically characterized four representative G4 scaffolds, C-myc, Bcl2, PS5.M, and C-kit, under standardized ABTS/H2O2 conditions to assess their kinetic properties and suitability for split designs. C-myc exhibited the highest sustained activity and near-linear concentration dependence, making it ideal for quantitative sensing, while Bcl2 showed durable catalysis suited for extended read windows. C-kit produced rapid bursts with early plateaus, favoring binary outputs, and PS5.M initiated quickly but inactivated rapidly, suggesting potential application of systems requiring fast response. Split-mode analysis revealed that symmetric 2:2 partitions often retained significant activity, whereas asymmetric 3:1 splits reduced but did not eliminate leakage. Among the four G4 DNAzymes, PS5.M demonstrated the most promising OFF-state suppression. Design strategies to minimize leakage including non-classical splits, loop/flank edits, and template-assisted assembly could be used to optimize biosensor functionalities. These findings identify essential factors critical for designing robust split DNAzyme biosensors, advancing applications in diagnostics and molecular logic gates. Full article
(This article belongs to the Special Issue State-of-the-Art Enzyme Engineering and Biocatalysis in Europe)
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21 pages, 3858 KB  
Article
Influence of Dietary Polyphenols on Catalase Activity In Vitro
by Claudia Chivu, Anca Leonties, Speranta Avram, Ana Maria Udrea, Petruta Oancea and Adina Raducan
Catalysts 2025, 15(10), 940; https://doi.org/10.3390/catal15100940 - 1 Oct 2025
Viewed by 2141
Abstract
The study investigated the impact of three prevalent polyphenols—quercetin, ferulic acid, and caffeic acid—on catalase activity. It was determined that all three polyphenols are capable of binding to catalase, resulting in the formation of a stable complex. This finding was corroborated through fluorescence [...] Read more.
The study investigated the impact of three prevalent polyphenols—quercetin, ferulic acid, and caffeic acid—on catalase activity. It was determined that all three polyphenols are capable of binding to catalase, resulting in the formation of a stable complex. This finding was corroborated through fluorescence quenching studies and kinetic modeling. At low concentrations, each polyphenol exhibited an activation effect on catalase; however, at concentrations exceeding 100 μM, they began to function as inhibitors. Notably, caffeic acid and ferulic acid were observed to protect the enzyme from operational inactivation, whereas quercetin did not demonstrate this protective effect. The association constants derived from kinetic modeling were compared with those obtained from docking simulations. The results suggest that polyphenols may exert both beneficial and potentially detrimental effects on cellular antioxidant systems, contingent upon their concentration and specific molecular interactions. This highlights the necessity for careful consideration of dosage in any prospective therapeutic applications. Full article
(This article belongs to the Special Issue State-of-the-Art Enzyme Engineering and Biocatalysis in Europe)
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Review

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24 pages, 1560 KB  
Review
Design and Applications of Split G-Quadruplex DNAzymes for Construction of Gated Biosensor
by Raphael I. Adeoye, Dunsin S. Osalaye, Sylvia O. Malomo and Femi J. Olorunniji
Catalysts 2026, 16(2), 117; https://doi.org/10.3390/catal16020117 - 25 Jan 2026
Viewed by 673
Abstract
Split G-quadruplex DNAzymes offer unique opportunities for building gated biosensors with a wide range of applications. Splitting G4 DNAzymes involves separating guanine tracts in the G-quadruplex DNA sequence into two non-functional sequences that reconstitute into a functional G-quadruplex with peroxidase activity upon hybridisation [...] Read more.
Split G-quadruplex DNAzymes offer unique opportunities for building gated biosensors with a wide range of applications. Splitting G4 DNAzymes involves separating guanine tracts in the G-quadruplex DNA sequence into two non-functional sequences that reconstitute into a functional G-quadruplex with peroxidase activity upon hybridisation of the aptamer probe region within the split system with the target molecule. Several studies have demonstrated the reassembly of split G4 DNAzymes and their applications in the detection of various analytes. This approach offers unique opportunities for modular biosensor construction, target-dependent activation, lack of requirement for labelling, amplification-free high sensitivity, and specificity over traditional G4 sensing. In this review, we explore the strategies of splitting G-quadruplex and their applications in biomedical diagnosis, environmental sensing, food safety monitoring, cell detection, and the integration of the technology with nanomaterials for enhanced stability and sensitivity. We considered the classical intermolecular split strategies that utilise binary probes and intramolecular split systems, which integrate the spacer DNA that allow for single probes as the model G4 sequence. Finally, we explore the current challenges required to develop split G-quadruplex DNAzymes into tools for routine practical applications. Full article
(This article belongs to the Special Issue State-of-the-Art Enzyme Engineering and Biocatalysis in Europe)
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21 pages, 2505 KB  
Review
Bridging Disciplines in Enzyme Kinetics: Understanding Steady-State, Transient-State and Performance Parameters
by Yu Ma and Bekir Engin Eser
Catalysts 2025, 15(12), 1139; https://doi.org/10.3390/catal15121139 - 4 Dec 2025
Cited by 3 | Viewed by 3914
Abstract
Enzyme kinetics is fundamental across diverse fields—from enzymology and medicine to biocatalysis and metabolic engineering. Analyses of enzyme kinetics provide insights into catalytic rates, substrate affinities, inhibition patterns, productivities and mechanistic pathways, which are critical for areas such as drug development, industrial biocatalysis [...] Read more.
Enzyme kinetics is fundamental across diverse fields—from enzymology and medicine to biocatalysis and metabolic engineering. Analyses of enzyme kinetics provide insights into catalytic rates, substrate affinities, inhibition patterns, productivities and mechanistic pathways, which are critical for areas such as drug development, industrial biocatalysis and mechanistic enzymology. However, each research field emphasizes different types of kinetic parameters, leading to challenges in establishing a common ground for understanding and interpreting enzyme properties. This review covers interpretation of enzyme kinetic parameters under three main categories—steady-state, transient-state and performance metrics—in a descriptive way and discusses their relevance with respect to different scientific and applied fields that investigate and utilize enzymes. By comparatively defining key kinetic and thermodynamic parameters, the review aims to help researchers interpret and report enzyme behavior more effectively, bridging gaps across interdisciplinary fields. Full article
(This article belongs to the Special Issue State-of-the-Art Enzyme Engineering and Biocatalysis in Europe)
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